Diabetes: Poor Response to Anti-Anemia Drug Predicts Higher Risk of Heart Disease or Death

Diabetes: Poor Response to Anti-Anemia Drug Predicts Higher Risk of Heart Disease or Death

ScienceDaily (Dec. 29, 2010) — Patients with diabetes, kidney disease and anemia who don’t respond to treatment with an anti-anemia drug have a higher risk of cardiovascular disease or death, researchers at UT Southwestern Medical Center have found.

 

The results suggest that testing such patients’ responsiveness to the drug and keeping blood iron levels a little low might reduce their risk, said Dr. Robert Toto, professor of internal medicine and clinical sciences and a senior author of the study, which appeared in the New England Journal of Medicine.

“These patients required higher doses and ended up having lower hemoglobin anyway,” Dr. Toto said. “The results of this study might lead us in directions that can help.”

The results were an unexpected finding of a study on darbepoetin alpha, which stimulates the production of red blood cells to counteract anemia. The drug, manufactured by Amgen, is sold under the name Aranesp.

The study, called the Trial to Reduce Cardiovascular Events with Aranesp Therapy (TREAT) showed that darbepoetin alpha works no better than a placebo for improving cardiovascular and kidney outcomes, but it did lower the risk for blood transfusion and resulted in modest improvement in patient-reported outcomes among people with diabetes, kidney disease and anemia. However, people receiving darbepoetin alpha had nearly a twofold higher risk for stroke. Cancer deaths were also higher among people receiving the drug.

Darbepoetin alpha is one of a class of anti-anemia drugs that mimics erythropoietin, the body’s natural hormone that stimulates production of red blood cells.

The combination of type 2 diabetes, chronic kidney disease and anemia affect about 1 million people in the U.S.

TREAT was a double-blinded experiment with a control group that received a placebo. It included 4,038 participants, all of whom had type 2 diabetes, anemia and kidney damage, although not enough to require dialysis. Of these, 1,872 received injections of the drug, and 1,889 received placebo injections.

Participants receiving darbepoetin alpha also received periodic subcutaneous injections of the drug with the aim of increasing their levels of hemoglobin — a protein in red blood cells that carries oxygen — to a level of 13 grams per deciliter. If someone in the control group dropped to a dangerous hemoglobin level below 9 g/dl, he or she received “rescue therapy” with darbepoetin until the hemoglobin level returned to a level above 9 g/dl.

In analyzing the results, the researchers divided the participants into two groups: those whose hemoglobin levels promptly increased in response to early doses of darbepoetin alpha, and those whose bodies responded less strongly, with hemoglobin level staying low.

The participants who had poor initial responses to the drug had a higher rate of death, heart attack, stroke or heart failure, the researchers found.

The study cannot show whether those people had higher risk for those outcomes because they were in poorer health to begin with, or because of some action of the drug, the researchers stated.

However, it does raise the question of whether treatment for anemia should be customized according to a patient’s response to the drug, Dr. Toto said.

“Our studies suggest that we might be able to use the initial dose response to identify high-risk groups in future studies,” he said.

For instance, if a person’s hemoglobin level doesn’t improve within one or two months of anti-anemia treatment, it may be better to stop the drug and seek alternative treatment. A state of mild anemia might pose less cardiovascular risk in such a case than continuing or escalating the dose in an attempt to reach a normal hemoglobin level, Dr. Toto said. Conversely, for patients who respond quickly to the drug, treating them until they reach the normal goal range recommended by the Food and Drug Administration appears safer, he said.

Researchers from Brigham and Women’s Hospital and Harvard Medical School; Tufts Medical Center; the University of Erlangen-Nuremburg, Germany; the Faculdade de Medicina de São José do Rio Prieto, Brazil; University Medical Center, Groningen, the Netherlands; Northwestern University Feinberg School of Medicine; Health Sciences Centre, St. John’s, Canada; Mario Negri Institute for Pharmacologic Research, Italy; Amgen; and the University of Glasgow also participated in the study.

The study was funded by Amgen.

98.6 Degrees Fahrenheit Ideal Temperature for Keeping Fungi Away and Food at Bay

98.6 Degrees Fahrenheit Ideal Temperature for Keeping Fungi Away and Food at Bay

ScienceDaily (Dec. 22, 2010) — Two researchers at Albert Einstein College of Medicine of Yeshiva University have found that our 98.6° F (37° C) body temperature strikes a perfect balance: warm enough to ward off fungal infection but not so hot that we need to eat nonstop to maintain our metabolism. 

“One of the mysteries about humans and other advanced mammals has been why they are so hot compared with other animals,” said study co-author Arturo Casadevall, M.D., Ph.D., professor and chair of microbiology & immunology at Einstein. “This study helps to explain why mammalian temperatures are all around 37° C.” Dr. Casadevall also holds the Leo and Julia Forchheimer Chair in Microbiology and Immunology.

The research builds upon earlier work by Dr. Casadevall showing that the number of fungal species that can thrive and therefore infect an animal declines by 6 percent for every 1° C rise in temperature. This means that tens of thousands of fungal species infect reptiles, amphibians and other cold-blooded animals, but only a few hundred harm mammals. Such protection against fungal infection, Dr. Casadevall has speculated, could have been crucial for the triumph of mammals following the age of dinosaurs.

In this study, Dr. Casadevall and his Einstein coauthor, Aviv Bergman, Ph.D., professor and founding chair of systems & computational biology, devised a mathematical model that analyzed the benefits gained by body temperatures that protect against fungi versus the costs (in terms of extra food consumption) required to maintain body temperatures between 30° and 40° C. The optimal temperature for maximizing benefits while minimizing costs was found to be 36.7° C, which closely approximates normal body temperature.

“This study is a good example of how mammalian evolution has been driven by both external biological factors and internal physiological constraints,” said Dr. Bergman

Enzymes – The Forgotten Giver Of Life And Health

ENZYMES

 

Without them there is no life. Lack of them can cause health problems, illness and death. In science we know allot  of information about enzymes yet ask anyone you know about them and they will have no idea what you are talking about. Yet  enzymes should be in our conscious and  on the menu constantly if we want to experience good health and longevity. Some people will have heard of digestive enzymes but not to many people use them. I am a massive fan of Serrapeptase for helping to relieve the pain and inflammation of GOUT! and for helping to “dissolve” scar tissue and  fibroids that  some women suffer with (also known as breast mice). We should all know more about Enzymes so Below is some information from my good friend Tony Pantalleresco’s web site. Have a read and Enjoy as they could save you from pain, discomfort and could even save your life!

!

 

AMYLASE  DEFICIENCY:

  Skin Rash

  Hypoglycemia

  Depression

  Mood Swings

   Allergies

  PMS

  Hot Flashes

  Fatigue

  Cold Hands and Feet  Neck and Shoulder Ache Sprue

  Inflammation

 

PROTEASE DEFICIENCY:

 

 Back Weakness

 Fungal Forms

 Constipation

 High Blood Pressure

 Insomnia

 Hearing Problems

 Parasites

 Gum Disorders

 Gingivitis

    COMBINATION DEFICIENCY

                          Chronic Allergies

                          Common colds

                          Diverticulitis

                          Irritable Bowel

                          Chronic Fatigue

                          Sinus Infection

                         Immune Depressed Conditions

    LIPASE DEFICIENCY                                                      

                           Aching Feet

                        Arthritis

                        Bladder Problems

                        Cystitis

                        Acne

                        Gall Bladder Stress

                        Gallstones

                        Hay Fever

                        Prostate Problems

                        Psoriasis

                       Urinary Weakness

                       Constipation

                       Diarrhea

                       Heart Problems

 

PROTEASE DEFICIENCY:

Protease digests protein. Acidity is created through the digestion of protein. Therefore a protease deficiency results in an alkaline excess in the blood. This alkaline environment can cause anxiety and insomnia. In addition, since protein is required to calcium in the blood, a protease deficiency lays the foundation for arthritis, osteoporosis and other calcium-deficient diseases. Because protein is converted to glucose upon demand, inadequate protein digestion leads to hypoglycemia, resulting in moodiness, mood swings and irritability. Protease also has an ability to digest unwanted debris in the blood including certain bacteria and viruses. Therefore, protease deficient people are immune compromised, making them susceptible to bacterial, viral and yeast infections and a general decrease in immunity.

 

AMYLASE DEFICIENCY:

Amylase digests carbohydrates along with dead white blood cells (pus). When you are low in amylase you are a candidate for abscesses (inflamed areas with pus but not bacteria). Amylase is also involved in anti-flammatory reactions such as those caused by the release of histamine and similar substances. An Amylase deficiency can result in skin problems such as psoriasis, eczema, hives, insect bites, allergic bee and bug stings, atopic dermatitis, and all types of herpes. Asthma and emphysema may also be exacerbated by an amylase deficiency.

 

LIPASE DEFICIENCY:

Since lipase digests fat and fat-soluble vitamins, lipase deficient people can be expected to have a tendency towards high cholesterol, high triglycerides, difficulty losing weight and diabetes. The future outcome of these tendencies is heart disease, which kills one out of two Americans. Lipase deficient people also have decreased cell permeability, meaning nutrients cannot get in and the waste cannot get out. The condition of vertigo or labrynthis, also called Meniere’s Disease (dizziness aggravated by movement such as walking or driving), can also result from lipase deficiency.

 

CELLULASE DEFICIENCY CONDITIONS:

Cellulase breaks down the fiber in our diet. Because our body does not produce cellulase, this food enzyme is essential. We must eat it on a daily basis. Remember, ONLY RAW FOODS contain cellulase. Of all the enzymes, this deficiency carries with it the most categories of problems. The symptoms of cellulase deficiency can best be described as malabsorption syndrome (impaired absorption of nutrients, vitamins, or minerals from the diet by the lining of the small intestine). Malabsorption has many symptoms including lower abdominal gas, pain, bloating and problems associated with the jejunum and pancreas.

 

SUCRASE, LACTASE & MALTASE DEFICIENCY:

People who have malabsorption syndrome and cellulase deficiency also have a tendency towards sugar (sucrose, lactose, & maltose) and/or gluten intolerance. Sucrose, lactose and maltose are three common sugars which some people cannot tolerate. They are broken down and absorbed into the system by three enzymes; sucrase, lactase and maltase.

 

SUCROSE

intolerant people cannot split the sucrose disaccharide into twin partners, two units of glucose. Glucose is a primary brain food so expect mental and emotional problems in people who cannot get glucose into the brain. Symptoms include depression, moodiness, panic attacks, manic and schizophrenic behavior and severe mood swings.

 

LACTOSE

intolerant people also have classic symptoms which include abdominal cramps and diarrhea. Other allergic symptoms, including asthma, have been witnessed from the ingestion of lactose-containing products.

 

MALTOSE

intolerant people are generally sensitive to environmental conditions. An intolerance to sucrose, lactose, or maltose may be worsened by a deficiency in sucrose, lactase, or maltase.

 

 

Enzyme Nutrition

http://www.med-library.net/content/view/222/41/

 

 

by Ron Kennedy, M.D., Santa Rosa, CA

The energy of life is expressed through DNA, desoxyribonucleic acid. These magnificent, complex molecules reside in the genetic material located in the nucleus of each living cell. DNA contains both the program to create the body and the ability to mobilize the energy to carry out the job. The first order of creation by DNA in the daily process of living is the production of more DNA (when the cell divides), and the second order of creation by DNA is the production of RNA. RNA stands for ribonucleic acid and this molecule is made by DNA (and sometimes by other RNA) through DNA’s ability to copy amino acid sequences in a selective fashion. Whereas there is only one structure for DNA, there are many RNA structures depending on the job assignment of a particular molecule of RNA. While many molecules in the body can be considered essentially dead when measured alone, RNA inherits a full complement of the vital life force contained in DNA. The job of RNA is to make proteins (and other RNA). Proteins serve as building blocks of the body, as well as many other functions. A large percentage of lean muscle tissue, for example, is made of protein. Connective tissue, including fascia, tendon and bone also is made largely of protein.

      Enzymes

A specialized type of protein is called an “enzyme.” Enzymes are protein molecules made by RNA and other enzymes with the ability to facilitate and speed up chemical reactions throughout the body. In the haphazard process, thought to have been the beginning of biochemistry in nature which eventually gave birth to life, amino acids formed and strung themselves together by chance into polypeptide chains some of which became enzymes quite by accident. These structures, which had the ability to speed up reactions between the molecules around them, made life possible. The reactions they facilitated otherwise took so long to happen as to put off the development of life to the infinite future. Enzymes are thought to have conspired with each other to create the first nucleic acids, very large structures which eventually evolved into RNA and DNA. There now are around 3000 known enzymes in the body and probably several thousand more as yet undiscovered, one for each kind of biochemical reaction which occurs there. Enzymes inherit from RNA a full measure of the vital life force originally given to RNA by DNA. Enzymes are both the parents and grandchildren of DNA, the source of our vital life force. In the context of the living body, enzymes are living molecular entities. Enzymes work by virtue of their shape. An enzyme molecule can be compared, in shape at least, to many short strings of pearls (amino acids) strung together. This long string folds in on itself as certain sequences of amino acids (pearls) are more attracted to each other than to other sequences, thus giving the enzymes a specific shape. At one point on the surface of this string of pearls, there exists something which looks like a keyhole. This is called the “active site” on the enzyme. When matched with its specific coenzyme (a vitamin, or mineral, or trace element) this “lock” has the exact inverse contour of the “key” which is contained in the molecule of the enzyme’s “substrate,” the molecule the enzyme wants to transform into a different molecule. When the substrate appears, it inserts the “key” into the “lock.” The molecular structure of the substrate is transformed into a different molecular structure, and both enzyme and the newly transformed molecule go on their merry ways. The slowest known enzyme (lysozyme) processes one substrate every two seconds. The fastest known enzyme (carbonic anhydrase) processes a phenomenal 36 million substrate molecules per minute. The shortest lived enzymes function for twenty minutes, and the longest are around and doing their jobs for several weeks. When an enzyme is worn out, it is broken down and disposed of by other enzymes, its component amino acids and polypeptide chains used to make new enzymes.

Dr. Edward Howell

Every area of knowledge in progressive medicine has its early champion, Broda Barnes in the study of hypothyroidism, Jens Moeller in the therapeutic uses of testosterone, for example. The study of enzymes is no exception. Dr. Edward Howell has clarified enzymes and enzyme therapy for us. We owe Dr. Howell a debt of gratitude for his pioneering work. In helping us understand the role of enzymes, Dr. Howell studied man, animals and plants with equal curiosity and scientific acumen. By comparative studies of disease states in man and in animals, Dr. Howell clearly demonstrated the disastrous nutritional effect of cooking food — more about that later.

            A Classification of Digestive Enzymes

Particular types of enzymes have digestive functions. The job of a digestive enzyme is to break down food during the digestive process. The intestine is more able to absorb food which is thus broken down into smaller units, and the rest of the body is more easily able to utilize food which is in this form. There are three basic types of digestive enzymes, one type for each class of food: lipase for fat, proteinase for protein and amylase for carbohydrate. Enzymes which drive the other processes of living are called “metabolic enzymes.” There is one enzyme for each type of biochemical reaction which happens in the body. Metabolic enzymes are by far the most numerous of all enzymes. Enzymes which are present in raw, uncooked food are called food enzymes to indicate where they come from: the food itself. They also are called “exogenous” enzymes, because they come from outside your body. Enzymes which are made in the body are called “endogenous” (meaning “inside-created”) and include both metabolic and digestive enzymes. Enzymes which are eaten with your food and are made by other animals or plants, are exogenous (outside-created). Food enzymes are exogenous enzymes. Exogenous enzymes have two origins: animal enzymes from animal food (raw meat, raw eggs, raw milk, etc.) and phytoenzymes, which come from plants (phyto = plant). Autolytic (meaning “self-digesting”) enzymes, which are very important in this discussion, are endogenous enzymes contained inside cells. The purpose of an autolytic enzyme is to break down the cell in which it is contained after that cell dies. Autolytic enzymes are contained in little bag-like structures which rupture upon death of the cell, releasing the autolytic enzymes to do their jobs. Because the body is made of fat, protein and carbohydrate, these enzymes are lipases, proteinases and amylase. It is important that you understand the above terminology for purposes of this discussion. I suggest you make a note card for each type of enzyme with a definition on the reverse side of the card. This terminology may seem confusing at first but as you study it, it begins to make an elegant kind of sense. The following flow chart will help you get all this straight.

Flow Chart of Enzymes

    I.   Endogenous Enzymes: (from inside the consumer or predator, i.e., you)

    A.  Human enzymes

    1.  Endogenous metabolic enzymes (made throughout the body)

                                                                          a.            Endogenous lipases

                                                                          b.            Endogenous proteinases

                                                                           c.            Endogenous amylase

     2.   Endogenous digestive enzymes (made only in the digestive tract)

     3.   Endogenous autolytic enzymes (also lipase, proteinase and amylase)

            Exogenous Enzymes:

      A.            Animal enzymes

    1.   Exogenous metabolic animal enzymes

     2. Exogenous autolytic animal enzymes

                                                                          a.            Exogenous animal lipases

                                                                          b.            Exogenous animal proteinases

                                                                           c.            Exogenous animal amylase

   B.  Phytoenzymes (of plant origin)

     1.   Exogenous metabolic plant enzymes

      2.  Exogenous autolytic plant enzymes

    a.  Exogenous plant lipases

  b.   Exogenous plant proteinases

 c.  Exogenous plant amylase

I have underlined the enzymes in which we have the most interest in this discussion. These enzymes can do a lot of work for us and save us a lot of energy. They are what this discussion is about.

     Enzyme Activators and Inhibitors

Enzymes in the activated state are very busy little guys. They must spend most of their lives inactivated, otherwise they would digest their host organism in a few minutes. The body has elaborate mechanisms to keep enzymes inactive until they are needed. The usual condition of an enzyme circulating throughout the body is that it is held in check by an amino acid chain, which is part of the enzyme — a kind of safety latch similar to the safety latch on a gun or the lock on a door. When the action of the enzyme is needed, an associated activating enzyme is released, for example, from an area of thrombosis (a clot — inside an important artery, let us say) or, to use another example, from an area of inflammation. This activating enzyme turns off the safety latch or, in the other analogy, unlocks the door, allowing the enzyme to go to work, causing a breakdown of the blood clot or cleaning up the inflammatory debris. Another safety system is that of enzyme inhibitors. These are proteins, which fit into the active site of the enzyme molecule, thus preventing the admission of substrate (the stuff the enzyme is designed to break down). When the enzyme is needed , these proteins are signaled to release themselves from the enzyme thus freeing the enzyme to do its assigned task. Examples of exogenous enzyme inhibitors include many antibiotics, which kill bacteria by inhibiting key enzyme systems. Unfortunately, they also inhibit the identical metabolic enzyme systems in the body and thus are toxic to both bacteria and host. (You are the host.) This is one more reason I prefer to avoid the use of antibiotics, if at all possible. Another example of exogenous enzyme inhibitors are those contained in seeds and nuts (which are also seeds). From seeds (nuts are seeds) entire plants grow with only the addition of water, soil, sunshine and the right temperature. From these facts, you can guess that seeds are loaded with enzymes. However, they must be held in the inactive state until water is present. Nature has loaded seeds with enzyme inhibitors, which are deactivated by the addition of water. This process is called “germination.” Therefore, when you chow down on your favorite seeds and/or nuts, you are loading your stomach with enzyme inhibitors. These enzyme inhibitors slow down or stop the action of whatever digestive enzymes may be present with your food, whether from an endogenous or exogenous source. Therefore, either avoid seeds and nuts unless (1) you germinate them first by letting them soak in water for a few days or (2) you consume them along with sufficient extra enzyme powder to neutralize the enzyme inhibitors.

    Misconceptions About Enzymes

Professor B. P. Babkin wrote, in 1935, that when the pancreas is stimulated to secrete enzymes for digestion, it secretes equal amounts of proteinase, lipase and amylase. This was known as the “Theory of Parallel Secretion of Enzymes.” (These three enzymes are responsible for digesting protein, fat and carbohydrate respectively.) Babkin’s theory held that if you ate a meal of almost all protein, for example, your pancreas would pour out enzymes to digest not only protein but also fat and carbohydrate as well, and that these latter two enzymes would simply go to waste. The Theory of Parallel Secretion implied that enzymes are so easy for the body to manufacture, it can afford the luxury to make some and then throw them away! Regardless of how little sense this made, the theory was accepted and taught in medical schools because of the reputation of the eminent Dr. Babkin. This is an example of the operation of dogma in medical thought. The eating and digestion of dogma in medical schools is identical to the same process in theology and law schools. No enzymes are required, only lame brains. It is now known that the pancreas exhibits “selective secretion,” meaning that the organ is signaled as to what sort of food is present and needing digestion, so it can then secrete the enzymes which are specifically needed for that kind of food. This is not only experimentally true, but it also makes sense! Given how complex and specific enzymes are, obviously a lot of energy is required to create them, and it makes no sense that the body would then waste them. No intelligent being would create such a mechanism in the human body, or any other body for that matter. Nevertheless, many doctors have not reconsidered what they were taught in medical school and find the idea of “enzyme therapy” to be absurd because, as they think they know: enzymes are so easy to make, the body is willing to waste them and, being so insignificant, they could not possibly constitute a valuable therapy. For many years it was taught in medical school biochemistry classes that an enzyme was not changed in any way when it performed its function of facilitating and speeding up a reaction. Enzymes were thought to act as true “catalysts,” just as some metal ions do in purely non-biochemical chemical reactions. This is now known not to be the case. Enzymes are used up and destroyed in the process of doing their jobs, and the remains must be disposed. They are broken down by other enzymes and new enzymes are made to replace them. Enzymes do last a long time: from twenty minutes to a few weeks, doing the same job many times before wearing out. Enzyme creation and destruction is happening throughout the body at all times. It only stops when the organism dies and actually not even then as we will now see. It was also once taught in medical schools that enzymes could not pass through the gut wall and, therefore, any exogenous enzyme would have to first be digested, i.e., broken down to its component amino acids like any other protein, before it could be absorbed and used by the body. It is now known that both enzymes and ordinary proteins can be absorbed whole without being fully digested. The fact of antibody (which is protein) absorption directly through the gut wall is the basis for the transmission of immunity from mother to child through breast feeding. This has enormous therapeutic implications where enzymes are concerned, because once in the body an exogenous enzyme identical in structure to an endogenous enzyme can be used as though it were an endogenous enzyme — the body has no way to distinguish it from an enzyme made inside the body.

   Comment on Medical Politics and Dogma

The medical dogma that proteins could not be absorbed without being broken down to the component amino acids died hard in standardized medical circles and medical schools, and this delayed the popular perception of the value of oral enzyme therapy immeasurably. The heyday of enzyme therapy has not yet come in the United States, although it certainly has arrive in other countries, notably Europe and Japan. It is truly unfortunate that the medical establishment in the U.S. is so intensely nationalistic as to believe that if a therapy has not been proven inside the boundaries of the U.S.A., then it is worthless until proven otherwise.

     Autolysis

All animals and plants contain the enzymes to “autolyze” themselves when they die. “Autolysis” literally means “self breaking” and refers to the fact that plant and animal tissues digest themselves after they die. Nature, folks, has thought of everything. The Egyptians developed a process to prevent bacterial breakdown of the body after death; however, they could not solve the problem of enzymatic autolysis. Therefore, a mummy, while it retains the essential form of the original body, is not exactly ready for a hot date. This fact, autolysis, leads us into the field of enzyme therapy. Unfortunately for humans, we have discovered how to cook our food. Cooking destroys the autolytic enzymes contained in food! All enzymes are extremely heat sensitive. If you cook them, they die! While pre-fire man received all the benefits of exogenous enzymes, post-fire man is starved for exogenous enzymes and must rely almost entirely on endogenous digestive enzymes, those he makes for himself.

       The Function of Fever

If you raise temperature a few degrees above normal body temperature, enzymes become hyperactive. The enzymes in the immune system are activated and powered up to fight infection by acceleration of the activity of certain white cells which literally eat and digest bacteria. This process is called “phagocytosis,” which means literally “eating cells.” At 104 degrees Fahrenheit, enzymes and phagocytic cells are at their maximum state of activation. Therefore, a fever should not be artificially brought down unless it exceeds 104 degrees Fahrenheit. At 106 degrees, brain damage (i.e., enzyme destruction) begins. When there is a fever it should be monitored every thirty minutes and treated if it exceeds 104.

    Cooking: The Great Nutritional Disaster

If you raise the temperature to 118 degrees for a few minutes enzymes are completely destroyed. It is practically impossible for the body to create such an intense fever; however, cooking can easily exceed this temperature. Therefore, cooking, even at low temperatures, is the death of enzymes.Since man mastered the use of fire, the practice of cooking food has been with us. From a nutritional standpoint, this was a great disaster. Let me explain that. Enzyme production is so labor-intensive that the eating habits of animals in nature are designed to take advantage of the presence of living enzymes in food. Fortunately for animals, they have not discovered how to cook their food.

      The Overgrown Pancreas

Because of cooking, our digestive organs, especially the pancreas, are called upon to do the job of enzyme production alone. In a person who eats even a moderate percentage of cooked food, the pancreas is hypertrophied (overgrown) to two or three times its normal size (that size found in people who eat only raw food).Animals in the wild eat raw food and their pancreases are approximately 1/3 the size of the typical human pancreas when corrected for body weight. Those animals are busy taking advantage of exogenous digestive enzymes contained in the raw food they eat. 

“So what?” you ask. So what, is that you have an organ (the pancreas) which is hypertrophied and is begging, borrowing and stealing from the rest of the body, so that enough enzymes can be produced to digest the food you eat. The precursors of metabolic enzymes, the amino acids and polypeptides, which are needed in the rest of the body are being hogged up by the pancreas to produce digestive enzymes because the pancreas is getting no help from the enzymes contained in raw food. Cooking has destroyed them. It is this simple: if living enzymes can be derived from food sources, the body does not have to expend its precious energy making digestive enzymes in large quantity. It can utilize that energy in the process of living healthier and longer by concentrating its ability to make enzymes on the production of metabolic enzymes. This is important. If you do not understand this, read it again until you do.

    Cooking Milk

Pasteurization — the heating of milk to 145 degrees centigrade for thirty minutes — totally destroys not only bacteria from sick cows but all enzymes as well. There was a time, before the turn of the nineteenth into the twentieth century, when doctors recommended a raw milk diet for the cure of many diseases. This was before cows were locked up, pumped up (on drugs and enzymeless feed) and sucked out, but rather were allowed to roam freely, foraging for raw plant food and came in every morning to be milked by hand. Unpasteurized and unhomogenized milk, made in this fashion, is loaded with valuable enzymes and, if you can find it, will serve as a therapy for a number of diseases. Given what has happened to milk in this century, informed doctors recommend that you avoid milk like the plague rather than drink it as a treatment for illness. It was inevitable, I guess, that man would finally think of cooking (pasteurizing) milk also. This avoids the necessity to monitor the milk cows to insure that they are free of disease.

     Eat Raw Meat? Thanks, But No Thanks

While it is true that raw meat contains loads of living enzymes, I am not suggesting that you eat raw meat. Given how animals are treated in modern animal husbandry, you cannot count on raw meat for being only raw meat. It also will contain hormones, antibiotics, herbicides and pesticides before and after cooking. Also, there is the matter of how it tastes.

        But The Eskimos Did!

For primitive, fireless man and for Eskimos, before acculturating to white man ways, raw meat was a great source of energy which kept these people free from degenerative diseases. The name “Eskimo” is an Indian term meaning “he eats it raw.” Alas, it is no longer so. Most Eskimos now are eating potato chips and hamburgers, having adopted the white man’s habits. Eskimo forebears knew empirically (simply by observation) that raw food, even raw meat, is healthy food. Nature has designed a process of assisted autolysis using both cathepsin made in your stomach and cathepsin contained in the raw meat. Cathepsin is a proteinase enzyme, able to break down protein, including meat. Eskimos did not know this explanation, but they knew they felt good and stayed healthy when they ate raw meat. Besides, that was almost all that was available to them. Vegetables do not grow so well in snow and ice. The only choice the Eskimos had was to cook their meat or not. Empirically, by the way they felt after eating raw meat, they chose not to cook it.The problem with raw meat is, of course, the possibility of infection with parasites living in the meat. However, in the colder climates meat-borne parasites are non-considerations. Because the life cycles of most parasites involve an out of body experience (out of the body of the host, that is), usually at the egg or larval stage, they are not able to survive in cold weather — they bite the ice, usually by having their eggs or larvae frozen solid. They do thrive, on the other hand, in warm tropical climes, and they do well in temperate climes. Eskimos did not have the parasite problem. The point of this discussion about Eskimos is that the phobia of meat and fat is not justified. We should focus our attention where it belongs: the fact that cooking is the real culprit. If you are a vegetarian and you cook your vegetables, guess what? You would be better off not doing that.

     Stomach Physiology

The first part of the stomach, called the “antrum” or “cardia,” or as Dr. Howell named it: the “food enzyme stomach,” is similar in function to the “extra” stomach(s) in ruminants (cattle, deer, elk, moose, etc), in cetacea (whales, porpoises and dolphins) and in seed-eating birds such as chickens and pigeons. In all of these animals, the first stomach (or stomachs in some cases) and the food enzyme stomach in man, are where, together with cathepsin contained in raw meat, protein is partially digested. Of course, if you cook the meat, that portion of exogenous cathepsin is destroyed. In the food enzyme stomach, fats and carbohydrates eaten from raw sources (and thus containing lipases and amylase for autolysis), proceed to autolyze (predigest) themselves. In the food enzyme stomach, food is allowed to autolyze as much as it will for a period up to one hour. In humans, the food enzyme stomach functions as a separate organ by virtue of the fact that the lower stomach, also called the “fundus” or “pyloric stomach” (it could also be called the “endogenous enzyme stomach”), remains shut, the potential space closed by forcible opposition of the anterior and posterior walls of the stomach against each other. After autolysis the fundus opens, receiving the food, making a load of hydrochloric acid and pepsin and proceeding with digestion. Under “normal” circumstances of raw sources of protein, about half the stomach digestion of protein is achieved in the antrum or food enzyme stomach with cathepsin and other autolytic enzymes and the other half in the fundus with pepsin and hydrochloric acid. The typical doctor might disagree with this description and cite “barium swallow” fluoroscopy studies which show the entire stomach frantically contracting and relaxing after a barium swallow. This may be how the stomach behaves when insulted with a solution of barium, but barium is not food! The stomach behaves differently when engaged in digestion and is not being assaulted by a barium swallow. If your stomach contracted frantically after a meal you would know it, you would not need a barium assault to prove it. The point is: we can see by the behavior of the stomach during digestion that it is designed to take advantage of the enzymes which are contained in raw foods, so that we do not have to expend the large amounts of energy and resources necessary to make a huge load of endogenous digestive enzymes to do it on our own.

      Exogenous Enzymes and Longevity

Lest you still are not taking this discussion seriously, let us consider some research relating to enzymes, health and longevity. Because insects are cold-blooded and short-lived, it is easy to demonstrate the value of enzymes to their longevity. A study done with Daphnia magna, the water flea, demonstrated that raising its environmental temperature from 46 degrees to 82 degrees Fahrenheit cuts its life-span to 1/4 of that at 46 degrees. Increased temperature raises enzyme activity, and when enzyme vitality is used up, life is over. The same can be said for you, not because of increased temperature — because you are a warm-blooded animal, able to regulate your temperature — but because you deplete your enzyme stores in another way: by eating cooked food and requiring your body to divert precious resources to making digestive enzymes. This shortens your life span and robs you of your natural state of health. Many people, even people otherwise well-educated in nutrition, do not take the idea of enzyme support seriously. Many seem to think that enzyme support should be done only if the pancreas is weak, while the truth is that it should also be done if it is strong. If the pancreas is strong — enlarged and producing triple doses of enzymes, thus robbing the rest of the body, including the immune system, of precious enzyme precursors — we would do well to supplement endogenous enzyme production with exogenous food enzymes contained in raw foods. People who eat lots of raw food live longer and feel better. If you are interested in living long and remaining healthy, perhaps I can get your attention with the fact that enzyme production, both digestive and metabolic, decreases with age. When the enzymes finally check out, so do you. Maybe Methuselah really did live a long time, if he ate pure raw food as the Bible assures us that he did. However, if he lived in excess of 900 years, we still need to know more about how he did that! Most scientists consider this account fiction; however, I prefer to keep an open mind about things outside my personal experience.

         Enzymes and Obesity

Still don’t have your attention? Let us talk about being fat. Have you noticed how many people are overweight, I mean, uh, fat? You may be one of them. If the body is starved for the vital energy of enzymes which have been depleted in the cause of digestion, that body craves more energy. The only way the body knows to get more energy is to eat, and the only way to insure that you eat is to create the experience of hunger. So you eat and eat and eat, trying to get satisfied. What is missing is not calories but vital life energy, which has been robbed from your enzyme system. So you eat more dead, enzyme-free food, the calories are stored as fat, and the craving goes on. You can eat more calories and lose weight, if your source of calories is raw food because you are consuming vital life energy, i.e., enzymes, with your food, and this energy will convert more food to motion and thought and less to fat. When the body is presented with exogenous food-derived enzymes, it is able to make more endogenous enzymes for metabolism. One class of endogenous enzymes is lipase. The job of lipase is to break down fat. Got a fat problem? Get some lipase. Lipases are contained in all raw, uncooked food containing fat. Do not be afraid of fat, be afraid of fatty food which has been cooked and stripped of its autolytic lipases. Remember what Einstein taught us: mass and energy are interchangeable. With exogenous, food-derived enzymes, you can convert some of your mass to energy, maybe not at the speed of light squared, but fast enough.

           Too Skinny?

Some people weigh much less than they want to weigh because their pancreas has been exhausted by a lifetime of no support from exogenous enzymes. This person may eat loads of food and yet remain underweight. The solution for such an underweight individual is not to eat more but to digest better. If pancreatic exhaustion is the problem, digestive enzyme supplementation is the solution and will produce better digestion and dramatic weight gain.

      Fasting and Enzymes

It has long been known by practitioners of fasting that health can be restored by this ancient practice. Water fasting — no food consumed, only pure water — relieves the body of the necessity of producing enzymes for digestion. The enzyme precursors can therefore be used for metabolic enzyme production. The same is true in juice fasting, which requires that only freshly prepared vegetable juices, and sometimes a smaller quantity of freshly prepared fruit juices, be consumed along with pure water. In this kind of fasting, fresh enzymes are given to the body in concentrated form in the juice. If illness is present, it may be helped through fasting. The immune system is given what it needs to correct illness — enzymes — and thus a sufficient supply of enzyme precursors. There may be a “healing crisis,” or detoxification stage, which is uncomfortable to go through but which leads to a new level of vital health. Fasting can be considered a form of enzyme therapy.

      Enzymatic Therapy For Arthritis

Still not convinced? Lets talk about treating and avoiding disease. In the 1940s, Dr. Arnold Renshaw of Manchester, England suspected rheumatoid arthritis to be a digestive disease. He based his suspicions, published in the Annals of Rheumatic Disease in 1947, on many observations at autopsy of the small intestines of people who had rheumatoid arthritis at the time of death. He found the small intestines to be consistently atrophied. Dr. Renshaw tested his hypothesis by having an enzyme preparation made for oral administration. He found that rheumatoid arthritis patients improved dramatically in just over one half of 556 patients. Another 219 of these 556 patients were improved to a lesser extent.He also discovered that the pain of osteoarthritis could be helped with enzyme therapy. The time required for improvement in these illnesses varied from two months to two years, so persistence is the key in this type of therapy. Similar results can be obtained with raw diets. It may be a long time to wait for results, but for most people it is worth waiting for and easier to confront knowing that this type of therapy benefits the rest of the body as well.

         Enzyme Therapy For Cancer

You may have heard of cases of cancer cured using only raw foods. If this happens, one of the explanations is clear: the immune system is powered up by a surge of enzyme precursors available when exogenous food enzymes are added to the diet, thus allowing the immune system to defeat (eat? digest?) the cancer. Enzyme treatment is the most exciting and promising approach to cancer. It attempts to duplicate the spontaneous cancer cures which are sometimes seen in oncology. Some doctors, including Dr. Howell, offer enzyme therapy for treatment of cancer. It stands to reason that if a prolonged fast or a diet of only raw vegetables can help some cases of cancer, massive doses of enzymes should also be able to help. This kind of therapy is done in a hospital and involves frequent small meals and doses of enzymes every thirty minutes. The need for careful supervision is obvious. I do not offer such a therapy, however, the folks at the Bradford Research Institute in Tijuana, Mexico offer this therapy along with others.

        Enzymes and Allergy

It is undeniable that some people react to certain foods. The explanation is that digestion is proceeding badly due to poor enzyme and/or stomach acid production. This causes food to arrive in the lower small intestine and colon relatively undigested. This upsets the normal flora of bacteria found there by favoring those bacteria able to digest that food. These bacteria replace so-called friendly species of bacteria which normally live symbiotically with us. The overall result is a condition called “dysbiosis” and malabsorption. The body forms antibodies to foods and bacterial breakdown products in the lower gut. These antibodies also attack, as if to neutralize, normal tissue of the body such as joint and skin tissue. Arthritis and skin disease are only two examples of diseases which have their origin in disordered digestion, diseases which have long been considered incurable in medical circles.

         Lipase and Atherosclerosis

As we grow older, the supply of all endogenous enzymes decreases. This includes lipase. It may be that the decrease in lipase as a function of aging has a lot to do with fatty deposits on the walls of arteries and the acceleration of atherosclerosis. Decreased supplies of lipase occurs in the intestines and in the serum (the noncellular part of blood). Therefore, as we grow older, it becomes increasingly important to either cut fat intake or to ingest exogenous lipase along with fat to help prevent atherosclerosis. This means raw food or supplementation with enzyme powder. Elsewhere, I have expressed the opinion that fat is not so disagreeable to the human body (provided there are plenty of antioxidants on board), rather what is in the fat constitutes the problem: herbicides, pesticides, synthetic hormones, antibiotics, etc., all fed to cattle to increase production. For an older person, it also may be that it is what is not in the fat: lipase is not in the fat if the fat is heated to 118 degrees Fahrenheit for only a few minutes. A rational approach to vascular disease is to load up on lipase with each meal containing fat. If you cannot bear to eat raw meat and you have no access to raw dairy products, buy some enzyme powder from your friendly health food store or organic grocery. In this manner, you can obtain the nutrition contained in the fat (the most powerful source of calories available) and not have to be concerned with the consequences. Nevertheless, it is not wise to unbalance your food intake in any direction, including excess fat.

           Comparative Pathology

Let us see how can we be relatively sure of the importance of ingesting exogenous enzymes. Domesticated animals suffer the same degenerative diseases which humans are subject to: cancer, arthritis, atherosclerosis; whereas this does not happen with animals in the wild. Animals procured from the jungle, when dissected, show no evidence of arthritis, cancer, or atherosclerosis, unless they live close to human pollution. But pity the health of the animal in captivity which is fed processed food. The explanation which makes the most sense to me is that domesticated animals fed processed food, because they receive no exogenous enzymes, fall ill with the same diseases we have. Processed human food (heat is part of the “process”) is stripped of its enzyme content. It is what some people call “dead food.” The animal equivalent is dog and cat chow, as well as cattle and chicken feed, which has gone through heat processing. This stuff is the animal version of the dead food we eat ourselves. Animals in the wild must eat fresh raw food, because nothing else is available. Therefore, they receive liberal amounts of all enzymes.

    The Point

The purpose of this discussion is to point out to you the importance of enzymes. Enzymes are not yet in the consciousness of the public, whereas the importance of vitamins and minerals is firmly entrenched. Your nutritional regime is not complete until cooked-food-induced enzyme starvation is corrected.  The best solution, of course, would be to revert to raw food exclusively. The next best solution would be to revert to eighty percent raw food. A salad with your meal is a nice gesture, but it is not enough, although every little bit helps, I suppose.If you are not able or, more likely, not willing to make the change to exclusively raw food, the next best solution is to supplement your diet with enzymes. These should be taken just as you begin to eat, and they should be in powder form. If you have the type which is powder in a capsule, separate the capsule, and pour the powder on your first bite of cooked food after it has cooled to around body temperature (otherwise, the enzyme is destroyed by the heat of the food). Do not use the tablet form of enzymes unless you chew it up.

   Sources

§                              Ambrus JL et al. Absorption of exogenous and endogenous proteolytic enzymes Clin. Pharmacol. Ther. 8:362;1967.

§                              Barrett AJ Proteinases in mammalian cells and tissues Elsevier, North Holland Biomedical Press; 1967.

§                              Baumueller M XXIV FMS World congress of sport medicine Symposium on enzyme therapy in sports injuries May 29, 1990, p. 9 Elsevier Science Publishers, Amsterdam 1990.

§                              Beard J Enzyme therapy of cancer. In: Wolf, M. (Hrsg.) Maudrich-Verlag, Vienna;1971.

§                              Blonstein JL Oral enzyme tablets in the treatment of boxing injuries Practitioner 198: 547; 1967.

§                              Bramwell FWR The transmission of passive immunity from mother to young Frontiers of Biology, Vol. 18, North-Holland, Amsterdam;1970.

§                              Ekerot LK, Ohlsson K, Necking L Elimination of protease-inhibitor complexes from the arthritic joint Int. J.Tissue Reac. VII:391;1985.

§                              Emele JF, Shanaman J, Winbury MM The analgesic-anti-inflammatory activity of papain Arch Int Pharmacyn Ther 159:126;1966.

§                              Gardner MLG Intestinal assimilation of intact peptides and proteins from diet — a neglected field? Biol Rev 59:289-331;1984.

§                              Jaeger H Hydrolytic enzymes in the treatment of HIV disease General Medicine (Allgemeinmedizin) 19(4):160-164;1990.

§                              Layer P, et. al Fate of pancreatic intestinal enzymes during small intestinal aboral transit in humans Am J Physiol Gastrointest Liver Physiol 251:475;1986.

§                              Lopez DA, Williams RM, Miehlke M Enzymes, The Fountain of Life The Neville Press Inc. 1994 ISBN 1-884303-00-5.

§                              Neuhofer C Enzyme therapy in multiple sclerosis Hufeland Journal 2:47-50;1986.

Howell E Enzyme Nutrition, The Food Enzyme Concept Avery Publishing Group Inc., Wayne, New Jersey 1985 ISBN 0-89529-221-1.

 

ENZYME DEFICIENCIES

http://www.enzymes.com/enzyme_deficiencies.html

“How is it possible that I am sick even though I eat the most organic foods, am very careful with my diet and exercise regularly?”

The answer tends to be: ENZYME DEFICIENCY.

The following is a brief summary of several of the more common enzyme deficiency conditions.

~~~: Protease digests protein. What happens when you are protease deficient? You will have protein deficiency symptoms, depending on how deficient you are in protease. Protease deficiency creates alkaline excess in the blood. This is not because protease itself is acidic; it is not. Acidity is created through the digestion of protein with protease. Some people may be vegetarian not by choice, but because they are protease deficient and cannot digest protein. Since acidity comes from the digestion of protein with protease, protease-deficient people may have an alkaline excess which can produce anxiety states. Often people take tranquilizers such as Xanex and then they zombie around in a fog, when simply taking protease can, through increased digestion of protein, acidify them to HOMEOSTASIS with resulting relief of their anxiety. Homeostasis is the dynamic equilibrium within the body. Without successful physiological homeostasis (balance), in which relatively constant conditions are maintained in the internal environment, the body cannot survive. The maintenance of homeostasis involves a number of factors in addition to metabolism, such as water intake and retention, acid-base balance, excretion of waste matter and control of body temperature. In other words our body will do whatever it must to stay in homeostasis. Protein is also required to carry protein-bound calcium in the blood. Insufficient protein-bound calcium lays the foundation for arthritis and other calcium deficient diseases. Why? When the blood cannot carry calcium because it lacks protein, it withdraws the necessary calcium from the bones to maintain homeostasis. This situation is aggravated in people who take calcium carbonate supplements, such as Tums or other antacids, because this adds to the alkaline stress on the blood. The blood cannot carry ionic calcium as efficiently because ionic calcium requires a certain level of acidity to be present. Overly alkaline people have a multitude of calcium metabolism problems, such as osteoarthritis, osteoporosis, gouty arthritis, degenerative disc problems, bone spurs and related disorders such as sciatica and ligament problems. Because 46% of digested protein is converted to glucose upon demand, inadequate protein digestion leads to hypoglycemia (hypoglycemia also has other causes such as hypothyroidism and vitamin deficiency). Symptoms include moodiness, mood swings and irritability among many others. Water follows protein (literally). Inadequate protein in the blood also means inadequate water. Where does the water go? Into the tissues after the protein! This causes tissue swelling (edema ). Water is forced into the capillaries and into the tissues by the pressure of blood being pumped around the body. By a reverse process, which depends on the water-drawing power of the proteins in the blood, it is reabsorbed in the capillaries from the tissues. These two mechanisms need to remain in balance. Protein maldigestion leads to a toxic colon. People in this category often have problems in the area of the descending colon (lower right quadrant of the abdomen). This includes developing appendicitis and even more serious problems such as mucous colitis and even colon cancer. Another of the most common results of protein maldigestion is chronic ear infections and fluid in the ears, especially in children. This is a protease calcium deficiency. To drain fluids from the middle ear, you must increase protease in the blood. Protease will pull water out of the middle ear, and also the ankles, hands and feet during PMS, and put it back into the blood. Protease is also involved in the immune system via its action on bacterial debris, certain viruses, and its ability to break down circulating immune complexes. Protease has an ability to digest unwanted debris in the blood and should be considered your friendly blood cleanser. Protease deficient people are immune compromised, making them susceptible to bacterial, viral and yeast Infections and a general decrease in immunity. Protease deficient women are predisposed towards PMS. The only people who cannot tolerate protease are those who suffer from ulcers, gastritis or hiatus hernias. The already damaged mucosal tissue cannot handle the extra acidity from the digested protein

 

~~~AMYLASE DEFICIENCY CONDITIONS: Amylase digests carbohydrates or polysaccharides into smaller disaccharide units, eventually converting them into monosaccharides such as glucose. People who are fat intolerant (can’t digest fats) often eat sugar and carbohydrates to make up for the lack of fat in their diet. If their diet is excessive in carbohydrates, they develop an amylase deficiency and symptoms arising therefrom. Amylase digests not only carbohydrates but also dead white blood cells (pus). For example, when you are low in amylase you are a candidate for abscesses (areas with pus but not bacteria). if you have a toothache and are being treated with antibiotics, but it doesn’t go away, chances are you may have an abscess. Amylase is involved in anti-inflammatory reactions such as those caused by the release of histamine and similar substances. The inflammatory response usually occurs in organs which are in contact with the outside world such as the lungs and skin. These include skin problems such as psoriasis, eczema, hives, insect bites, allergic bee and bug stings. atopic dermatitis, and all types of herpes. The lung problems including asthma and emphysema require amylase plus other enzyme formulas depending on the particular condition. Carbohydrates require phosphorus. If excess refined carbohydrates are consumed, a phosphorus deficiency will result.  ~~~Phosphorus deficiencies include: thick blood, tendency towards gastritis (inflammation of the gastrointestinal tract) and stiff joints, especially in the morning. Why stiff joints? Adequate phosphorus prevents the deposit of calcium oxalate and calcium carbonate in the joints. If phosphorus is deficient due to excess consumption of sugar, joint pain results from deposits of oxalates and carbonates Phosphorus deficiency is often accompanied by thick blood and high blood pressure. Please do not feel you can run out and get a phosphorus supplement to solve this problem. Quite the contrary. The only way the calcium and phosphorus can be balanced is by getting them both from the foods in which they originate in a natural, balanced proportion.

~~~LIPASE DEFICIENCY CONDITIONS: Since lipase digests fat and fat-soluble vitamins, lipase deficient people can be expected to have a tendency towards high cholesterol, high triglycerides, difficulty losing weight and diabetes or a tendency towards glucosuria (sugar in the urine without symptoms of diabetes). The down-the-road outcome of these tendencies is heart disease. Because lipase requires the co-enzyme chloride, lipase deficient people have a tendency towards hyphochlorhydria (low chlorides in our electrolyte balance). This can be easily remedied with lipase, but often nutritionists recommend using betaine HCL, which places acidic stress on the blood, leading to an inability to provide the alkalinity required to activate the body’s pancreatic enzymes. Lipase requires a high pH for its activation among food enzymes. That is why fats are the hardest of all foods to digest. Fat intolerant people can be helped by taking a lipase supplement, but the fat intolerance problem still exists. (i.e …. Taking a food combination containing lipase will gradually reduce the size of gall stones, thus reducing symptoms, but this does not cure fat intolerance just as surgery does not cure disease.) The lipase will help prevent an aggravated condition ONLY if the fat intolerant person minimizes fat consumption. Lipase deficient people have decreased cell permeability, meaning nutrients cannot get in and the waste cannot get out of the cell. For example, diabetics are lipase deficient and cannot get glucose into their cells, and wastes or unwanted substances cannot get out. People with ‘hidden viruses” that are often diagnosed with “Chronic Fatigue Syndrome” also fall into this category. Lipase modulates cell permeability so that nutrients can enter and wastes can exit. Of course, waste-eating enzymes (such as protease) must be taken to help cleanse the blood of the unwanted debris. A common symptom of lipase deficiency is muscle spasms. This is not the “muscle cramp” (tetany) resulting from low ionized blood calcium. It commonly occurs as trigger point pain in the muscles across the upper shoulders, but it can occur in other muscles, such as those in the neck or anywhere in the small or large intestines including the muscles of the rectal tissues. If chronic muscle spasms keep you going back to a chiropractor, osteopath or acupuncturist for repeated adjustments or therapy, try adding some lipase to your diet. It may help you hold your adjustments.People with “spastic colon” may be lipase deficient. They are given toxic muscle relaxant drugs to control the symptoms, but what they really need is a simple food enzyme called lipase. ~~~The condition of vertigo, or labrynthis, also called Meniere’s Disease (dizziness aggravated by movement such as walking or driving), can result from lipase deficiency. A nutritionist saw this condition develop suddenly in a young man after the typical American fat challenge test – a meal which consisted of a fried fish sandwich with tartar sauce, double cheeseburger plus a bag of french fries. The dizziness was accompanied by severe nausea and vomiting which was aggravated by movement. This condition lasted several days. Lipase can relieve a condition like this, often within minutes. The condition of menopause is often associated with lipase deficiency because lipase addresses the gonadal tissue. However, PMS is more often associated with protease deficiency.

~~~CELLULASE DEFICIENCY CONDITIONS: Our body makes no cellulase at all, whereas our pancreas produces enzymes similar to protease, amylase and lipase. They are similar, but not identical, because ONLY FOOD ENZYMES WORK IN THE STOMACH. Pancreatic enzymes work in the duodenum when it is at the right alkaline pH (third part of digestion). Because our bodies do not make cellulase, this food enzyme is essential. We must eat it on a daily basis. Remember, ONLY RAW FOODS contain cellulase. Of all the enzymes, this deficiency carries with it the most categories of problems. Cellulase deficiency is a malabsorption syndrome (impaired absorption of nutrients, vitamins, or minerals from the diet by the lining of the small intestine) with its many symptoms of lower abdominal gas, pain, bloating and problems associated with the jejunum and pancreas. Other conditions associated with cellulose deficiency include nervous system conditions such as Bell’s Palsy, Tic and facial neuralgia, all of which respond remarkably to cellulase. Certain toxic conditions, such as chemicals, drugs and toxic metals, including silver amalgam fillings (mercury in the teeth) are greatly alleviated with cellulase. This also includes acute food allergies. People who have malabsorption syndrome and cellulose deficiency have a tendency toward sugar and/or gluten intolerance.

~~~SUCROSE INTOLERANCE: This condition exists when people cannot split the sucrose disaccharide into its twin partners, two units of glucose. Glucose is a primary brain food so expect mental and emotional problems in people who cannot get glucose into the brain. These symptoms include the whole gamut from depression and moodiness to panic attacks, manic and schizophrenic behavior and severe mood swings, which often lead to toxic behaviormodifying drugs. Seizures, cranial problems and headaches in sucrose intolerant people have been observed, not to mention the symptoms of B-vitamin deficiency resulting from the use of refined white sugar. One researcher has observed almost a universal intolerance syndrome among childhood asthmatics. Whether from genetic intolerance or over consumption, the symptoms are the same. Do not be fooled by thinking that refined white sugar is the only culprit and that other synthetic sugars are okay. Many people do not think that such synthetic sugars as corn syrup, fructose, Nutrasweet, saccharin, Sorbital and Mannitol are harmful. However, severe health problems have occurred from one or all of these as well.

~~~LACTOSE INTOLERANCE: People who are intolerant of lactose also have classic symptoms which include abdominal cramps and diarrhea. Other allergic symptoms have been recorded, not the least of which was asthma, from the ingestion of lactose-containing products. You should know that the FDA allows the addition of lactose as a food additive without labeling. Do not think that your children are safe if they are lactose intolerant just because they do not drink milk.

 

~~~GLUTEN INTOLERANCE: Gluten intolerance is associated with Celiac Disease and Malabsorption Syndrome. It is also associated with Crohn’s Disease. The insidious thing about gluten intolerance is that it creates a sugar intolerance because when gluten intolerant people eat food containing gluten, the brush border cells of the jejunum are injured and thus unable to secrete the disaccharidases (sucrose, lactase and maltose) leading to sugar intolerance. Double Trouble! Most gluten intolerant individuals usually do not need to abstain from all the gluten grains (wheat, oats, rye and barley). However, sometimes it is a must.

 You can find The ariginal information HERE Check out Tony’s site there is LOTS of information! or keep popping back to this site and  educate yourself to good health and longevity!

 

New Cell Biological Mechanism That Regulates Protein Stability in Cells Uncovered

New Cell Biological Mechanism That Regulates Protein Stability in Cells Uncovered

ScienceDaily (Dec. 28, 2010) — The cell signaling pathway known as Wnt, commonly activated in cancers, causes internal membranes within a healthy cell to imprison an enzyme that is vital in degrading proteins, preventing the enzyme from doing its job and affecting the stability of many proteins within the cell, researchers at UCLA’s Jonsson Comprehensive Cancer Center have found.

The finding is important because sequestering the enzyme, Glycogen Synthase Kinase 3 (GSK3), results in the stabilization of proteins in the cell, at least one of which is known to be a key player in cancer, said Dr. Edward De Robertis, senior author of the study and a Jonsson Cancer Center scientist.

“Surprisingly, we found that the degradation of about 20 percent of proteins in the cell is triggered by the GSK3 enzyme,” said De Robertis, who also is a Howard Hughes Medical Institute investigator. “That’s a great many proteins and one of them, beta-Catenin, is known to cause cancer. We also know that Wnt signaling is activated in about 85 percent of colorectal cancers and other forms of cancer start with mutations that activate Wnt signaling. So, this finding could have ramifications for potential new treatments for cancer.”

The study, a collaboration with cell biologist Dr. David D. Sabatini of New York University, appears in the Dec. 23, 2010 issue of the peer-reviewed journal Cell.

De Robertis said Wnt signaling requires inhibition of GSK3, but the enzyme sequestration mechanism was not known until now. The enzyme becomes imprisoned inside membrane-bounded organelles, known as multivesicular bodies, found within the cell cytoplasm.

“We knew these multivesicular bodies were involved in degradation of proteins, but that they had a role in how cells communicate with each other by switching on a signaling pathway was not known,” De Robertis said. “This finding raises the possibility that other signaling pathways could operate through this sequestration mechanism.”

When cells receive Wnt, it’s a signal for cells to degrade their proteins more slowly, to keep them for a longer period of time because they’re needed to regulate cell functions, such as proliferation. Wnt signaling, for example, is very high in all stem cells and rises during the regeneration of most tissues, De Robertis said.

“Perhaps one of the functions of Wnt is to stabilize certain cell functions and it may be that cancer needs higher protein stability than other cells, which is why increased Wnt signaling if found in so many cancers,” De Robertis said. “These findings may give us new therapeutic targets for preventing sequestrations inside these membranes, which would decrease Wnt signaling.”

De Robertis said this study also links two formerly unrelated areas of biology. The cell cytoplasm is filled with internal membranes that shuttle proteins to their final destinations. Cells in tissues communicate with their neighbors by receiving external signals called growth factors. The new work links the cell biology of membrane trafficking and the interpretation of the signals that control cell proliferation.

“Protein degradation is a very important part of the life of a cell. About 10 percent of the genes in the genome are dedicated to protein degradation,” De Robertis said. “We now know that Wnt causes an enzyme that degrades proteins to be sequestered and because of that becomes a regulator of cellular protein stability.”

De Robertis characterized this finding as “very unexpected.”

“No one thought you could have cell signaling through sequestration of an enzyme inside a membrane organelle like these multivesicular bodies,” he said. This is because the GSK3 enzyme is normally found everywhere in the cell, but becomes tightly bound to the internal side of membrane receptors when the Wnt signal is received.

The study was funded by the National Institutes of Health, Howard Hughes Medical Institute and the Norman Sprague Endowment for Molecular Oncology

The Remedy – Tony Pantalleresco – Show of the Week December 27 2010

The Remedy – Tony Pantalleresco – Show Sscripts of the Week  December 27 2010

 

Canada’s public water systems could be up for sale under CETA 

Nitric Oxide-Donating Nonsteroidal Anti-Inflammatory Drugs Inhibit the Growth of Various Cultured Human Cancer Cells: Evidence of a Tissue Type-Independent Effect — 

Recipe for Nitric Oxide and Acetylsalicylic acid 

Original Human ‘Stone Age’ Diet Is Good For People With Diabetes,

Trans-Palmitoleic acid –dairy fatty acid cuts type 2 diabetes risk

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Canada’s public water systems could be up for sale under CETA

 The Council of Canadians and The Canadian Union of Public Employees (CUPE) released a report last week raising serious concerns about the threat a trade deal with the European Union poses to Canada’s public water systems.
  Public Water For Sale: How Canada will privatize our public water systems is a report to municipal, provincial and territorial governments regarding the Canada European Comprehensive Economic and Trade Agreement (CETA). It warns that public water in Canada will be lost unless the provinces and territories take immediate steps to remove water from the scope of negotiations.>
CETA would open up public municipal water systems across Canada to privatization. Europe is home to private water giants such as Veolia Environment and Suez. At the request of these private, for-profit water corporations, Canada’s provincial and territorial governments are considering including drinking water and wastewater services in their services commitments under CETA. Once systems are privatized, public control and accountability would be lost.—  “CETA is a water privatization deal,” says Maude Barlow, National Chairperson of the Council of Canadians. “Our public water is being negotiated away behind closed doors. We need to act now or we will wake up one morning and our public water systems will be gone.“–CUPE and the Council of Canadians are calling on the provinces and territories to assert their jurisdiction and protect water from being opened up to private corporate interests.
 
 To read the report, go here: http://council-of-canadians.c.topica.com/maaor51ab1X0HaRVblqbaeQy7T

 

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EXECUTIVE SUMMARY

The federal, provincial and territorial governments in Canada are currently negotiating a Comprehensive Economic and Trade Agreement (CETA) with the European Union that presents a serious threat to Canada’s public water systems. At the request of Europe’s large private water companies, the provinces and territories are considering including drinking water and wastewater services in their CETA commitments. EU negotiators are also asking that Canada’s municipalities and their water utilities be included in a chapter on public procurement. Initial provincial-territorial offers in services, procurement and investment will be sent to the European Commission early in January 2011. —If CETA is negotiated on these terms, it would be the first time that Canada has allowed our drinking water to be fully covered under a trade treaty and the first instance that a trade agreement has covered municipal procurement of water services. The services and procurement commitments proposed in CETA would be protected by strong investor rights. The effect of these rights as they relate to the services and procurement provisions would be to lock in existing private water contracts, restrict how local governments regulate the activity and investment of private water companies, and to encourage more private sector involvement in a number of public service sectors, including water. —The federal, provincial and territorial governments are being asked to make these commitments to the EU during what has been described as an infrastructure crisis in Canada. Municipalities and First Nations communities are under pressure to upgrade aging water facilities, and to meet new environmental and safety legislation without access to proper financial resources. At least $31 billion is needed to cover the cost of the facility upgrades, and the estimated cost of the new sanitation regulations is $20 billion. Not surprisingly, the private water industry sees leaky pipes as an opportunity to increase its role in water delivery and treatment. Existing government programs, including the Building Canada Plan, and funding initiatives under Public Private Partnershps Canada (PPP Canada Inc.), encourage privatization as a condition of receiving federal money for municipal infrastructure projects. Experiments with privatization have failed all over the world, and a growing trend in Europe, the United States and Latin America is toward remunicipalization (or de-privatization) of private and P3 water projects. Time and again, partial or full privatization of water systems has been a disaster; accountability disappears, water rates go up, workers are laid off, service levels decline. Once public revenues are transformed into private profits remunicipalization will become next to impossible under the services, investment and procurement rules set out in CETA. There are no economic or social gains from agreeing to the EU requests as they relate to water services. There are only unnecessary and costly risks to Canada’s municipalities and First Nations.– Provincial, territorial and municipal governments must take immediate action to protect Canada’s public water systems from decay and privatization –. As one of the wealthiest countries in the world, solving the infrastructure crisis in municipalities and First Nations communities is a matter of political will, not adequate funding. First, government procurement and trade-in-services commitments related to water systems must be rejected in CETA. Provincial and territorial governments must work with municipalities and the federal government to develop a public funding plan to upgrade Canada’s neglected water infrastructure. Finally, all levels of government must be transparent with Canadians about the effect that CETA will have on the provision of public services and development of social policy. They should seek informed consent from Canadians on what provisions a trade agreement with the EU should and should not include.

 

SAFE DRINKING WATER FOR FIRST NATIONS ACT

Bill S-11 titled “Safe Drinking Water for First Nations Act” was tabled in Parliament on May 26, 2010. The stated objective of ensuring First Nations have access to safe drinking water was swiftly called into question when the federal government did not make clear how these regulations would be implemented. On June 9, 2010 the National Chief issued a national bulletin on the issue stating that–Bill S-11, does not guarantee that First Nations will have access to safe drinking water. Without funding for infrastructure/facilities, skills, resources, training and support, safe drinking water for First Nations will not be guaranteed. … the AFN is calling on the federal government to engage in real action to address the capacity gap as well as working towards a regulatory regime that reflects our rights, jurisdiction and delivers equitable and guaranteed access to safe drinking water.17–Among the many concerns regarding Bill S-11 are the fact that First Nations communities were never consulted, and the fact that Canada will have the authority to force First Nations into agreements with third parties to operate First Nation water systems. The private sector will have the ability to enter First Nations as owners and operators of water and wastewater facilities due to a lack of infrastructure, resources and training within First Nations. Private operation of public facilities can lead to higher costs of service and user fees downloaded to First Nations resulting in further inequality. An added problem is that set-asides 9 Public Water for Sale: How Canada Will Privatize Our Public Water Systems — for First Nations companies, an important means for provincial-territorial governments to encourage economic development, may be lost to the CETA procurement chapter.

»»RECOMMENDATION 2: The federal government should respect the right of First Nations communities to prior informed consent, and must consult and include them in any negotiations having to do with the water and wastewater facilities on First Nations reserves. Direct financial support will also be required to improve water and wastewater facilities on First Nations reserves and communities beyond 2012 when funding for the First Nations Water and Wastewater Action Plan (FNWWAP) expires.

 

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PUBLIC-PRIVATE PARTNERSHIPS: A FAILED MODEL GLOBALLY

London, England: Metronet was one of two P3s used for maintenance and upgrade of the London Underground system in the UK. In 2007 it collapsed when it ran out of money after overspending by ₤2 billion (nearly CDN$4 billion) through a P3 where it awarded its own shareholders overpriced contracts. It also failed to carry out work on time or on budget. A parliamentary report written after its failure stated:“Whether or not the Metronet failure was primarily the fault of the particular companies involved, we are inclined to the view that the model itself was flawed and probably inferior to traditional public-sector management. We can be more confident in this conclusion now that the potential for inefficiency and failure in the private sector has been so clearly demonstrated. In comparison, whatever the potential inefficiencies of the public sector, proper public scrutiny and the opportunity of meaningful control is likely to provide superior value for money. Crucially, it also offers protection from catastrophic failure. It is worth remembering that when private companies fail to deliver on large public projects they can walk away—the taxpayer is inevitably forced to pick up the pieces.”10

Manila, Philippines: After passing the Water Crisis Act in 1995 the Philippines signed a $283 million privatization plan managed partially by multinational firms Suez and Bechtel. It wasn’t long before tariff prices increased, water service and quality worsened, and public opposition skyrocketed. Today, some Filipinos still don’t have water connections, tariffs have increased from 300 to 700 per cent in some regions, and outbreaks of cholera and gastroenteritis have killed six people and severely sickened 725 in Manila’s Tondo district.11

Frankfurt, Germany: In 2007 the government in Germany entered into a P3 agreement with Hochtief for several schools. Using conventional public procurement the construction of the educational centre would have been €4million cheaper, according to an audit report. For the next 20 years the contract with Hochtief required €12.1 million annually which amounted to between 17% and 36% of the total budget for school buildings in Frankfurt, leaving the remaining schools with very limited budgets.

Montreal, Quebec: In June 2010, the Quebec Auditor General slammed the Montreal Public Private Partnership project and found the public option would save the province $10.4 million. For four years in a row, Quebec’s Auditor General has found that the choice to pursue a P3 for upgrades to Montreal’s University Health Centres (MUHC)12 is based on faulty and inaccurate assumptions and will end up costing taxpayers millions more than if they chose a public model.

British Columbia, Canada: BC’s Sea-to-Sky Highway will cost taxpayers $220 million more than if it had been financed and operated

 

COMMITTED TO THE ENVIRONMENT YOU SAY…

The city of Brussels terminated a contract with Veolia in 2010 after Aquiris, a consortium created in 2001 by Veolia Environment to support a BOT (build own operate transfer) in the city, deliberately dumped the wastewater from 1.1 million people into the river Zenne for 10 days. The chief executive of the regional water authority described this action as equal to “releasing an atomic bomb” into the river.15 Aquiris took this action while in a dispute with public authorities. One official noted that “whatever the rights and wrongs in the dispute it is hard to imagine that a publicly owned and operated company would have stopped the pumps like this.”16

 

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Nitric Oxide-Donating Nonsteroidal Anti-Inflammatory Drugs Inhibit the Growth of Various Cultured Human Cancer Cells: Evidence of a Tissue Type-Independent Effect 

 

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Recipe for Nitric Oxide and Acetylsalicylic acid (aspirin ) Take One gram ( 1000mgs) with 81 mg of aspirin ( unenterocoated you want this to break down and quickly in the system )-add to 2 oz of water and 1 tablspoon of vinegar—mix well and drink—the impact can be felt almost readily—in areas of pain you can feel the inflammatory markers cox will feell like they diminish—Take this either every 2 hours for the first few servings and then after every 4 hour for chronic pain—this is not to be used forever and must be cautioned for potential bleeding in the stomach—but forsomeone with cancer this for a short interim maybe what is the answer —THIS IS AN INFORMATIVE AND  EDUCATIONAL SITE, USES OF THIS INFORMATION IS ENTIRELY THE RESPONSIBILITY OF THOSE WHO WISH TO CHOSE TO USE THIS INFO FOR PERSONAL HEALTH OR USES AT THE DISCRETION OF THOSE INDIVIDUAL(S)-SEEK CONSUL FROM QUALIFIED HEALER(S) THAT ARE AWARE OF ALTERNATIVES

 

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Original Human ‘Stone Age’ Diet Is Good For People With Diabetes, Study Finds

ScienceDaily (June 28, 2007) — Foods of the kind that were consumed during human evolution may be the best choice to control diabetes type 2. A study from Lund University, Sweden, found markedly improved capacity to handle carbohydrate after eating such foods for three months.—During 2.5 million years of human evolution, before the advent of agriculture, our ancestors were consuming fruit, vegetables, nuts, lean meat and fish. In contrast, cereals, dairy products, refined fat and sugar, which now provide most of the calories for modern humans, have been staple foods for a relatively short time.—Staffan Lindeberg at the Department of Medicine, Lund University, has been studying health effects of the original human diet for many years. In earlier studies his research team have noted a remarkable absence of cardiovascular disease and diabetes among the traditional population of Kitava, Trobriand Islands, Papua New Guinea, where modern agrarian-based food  ( Farmed Produced )is unavailable. In a clinical study in Sweden, the research group has now compared 14 patients who were advised to consume an ‘ancient’ (Paleolithic, ‘Old stone Age’) diet for three months with 15 patients who were recommended to follow a Mediterranean-like prudent diet with whole-grain cereals, low-fat dairy products, fruit, vegetables and refined fats generally considered healthy. All patients had increased blood sugar after carbohydrate intake (glucose intolerance), and most of them had overt diabetes type 2. In addition, all had been diagnosed with coronary heart disease. Patients in the Paleolithic group were recommended to eat lean meat, fish, fruit, vegetables, root vegetables and nuts, and to avoid grains, dairy foods and salt. —-The main result was that the blood sugar rise in response to carbohydrate intake was markedly lower after 12 weeks in the Paleolithic group (–26%), while it barely changed in the Mediterranean group (–7%). At the end of the study, all patients in the Paleolithic group had normal blood glucose. —The improved glucose tolerance in the Paleolithic group was unrelated to changes in weight or waist circumference, although waist decreased slightly more in that group. Hence, the research group concludes that something more than caloric intake and weight loss was responsible for the improved handling of dietary carbohydrate. The main difference between the groups was a much lower intake of grains and dairy products and a higher fruit intake in the Paleolithic group. Substances in grains and dairy products have been shown to interfere with the metabolism of carbohydrates and fat in various studies.—“If you want to prevent or treat diabetes type 2, it may be more efficient to avoid some of our modern foods than to count calories or carbohydrate,” says Staffan Lindeberg.—This is the first controlled study of a Paleolithic diet in humans.—Story Source: The above story is reprinted (with editorial adaptations by ScienceDaily staff) from materials provided by Lund University.

 

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Trans-Palmitoleic acid –dairy fatty acid cuts type 2 diabetes risk

Researchers at the Harvard School of Public Health claim to have identified a fatty acid in diary products that may reduce risk of type 2 diabetes. —Writing in the Annals of Internal Medicine, the scientists examined data from a study that followed 3,736 adults from 1992 to 2006. –They found that those adults with the highest circulating levels of trans-palmitoleic acid – the fatty acid found in dairy – were exposed to the lowest risk of diabetes. —The 20 per cent with the highest trans-palmitoleic acid levels were found to have a 60 per cent lower risk of developing diabetes compared to the people at the bottom 20 per cent of the sample. Lead author Dariush Mozaffarian said: This represents an almost three-fold difference in risk of developing diabetes among individuals with the highest blood levels of this fatty acid.”

“Striking” magnitude —Mozaffarian described the magnitude of the findings as “striking” but added that the study should be followed up with more observational studies and controlled trials to confirm any initial conclusions. –However, the scientist suggested that the positive effect that trans-palmitoleic acid appears to have on diabetes risk may not be that surprising. He said: “We wonder whether this naturally occurring trans fatty acid in dairy fats may partly mimic the normal biologic role of its cis counterpart, cis-palmitoleic acid, a fatty acid that is produced in the body. In animal experiments, cis-palmitoleic acid protects against diabetes.”

Caution

Deepa Khatri, clinical advisor at Diabetes UK, called for more research and advised caution when interpreting the study results.

“People should not take the findings of this research as a reason to exceed the recommended portion amounts of dairy food in order to prevent their risk of developing Type 2 diabetes. Milk and dairy foods can be high in fat, which if eaten in excess can contribute to weight gain.” -Funding for the research was provided by National Heart, Lung, and Blood Institute and the National Institute of Diabetes and Digestive and Kidney Diseases of the National Institutes of Health.

Source: Annals of Internal Medicine

Trans-Palmitoleic Acid, Metabolic Risk Factors, and New-Onset Diabetes in U.S. Adults

Authors: Dariush Mozaffarian, Haiming Cao, Irena King, Rozenn Lemaitre, Xiaoling Song, David Siscovick, Gokhan Hotamisligil

 

Compound That Prevents the Growth of Prostate Cancer Cells Identified

Compound That Prevents the Growth of Prostate Cancer Cells Identified

ScienceDaily (Dec. 20, 2010) — Researchers from VTT Technical Research Centre of Finland and the University of Turku have demonstrated that an antibiotic called “monensin” prevents the growth of prostate cancer cells. Monensin is used in the meat and dairy industry, for example.

 

Evidence pointing to the effects of monensin emerged in a project investigating the effects of nearly 5,000 drugs and micromolecules on the growth of prostate cancer cells. The project involved most of the drugs on the market today. Researchers found that small amounts of compounds — disulfiram (Antabus), thiram, tricostatin A, and monensin — can prevent the growth of prostate cancer cells without significant effects on the growth of the normal human prostate epithelial cells.

Further studies revealed that monensin caused prostate cancer cell death by reducing the amount of testosterone receptor and by increasing production of reactive oxygen species and inducing DNA damage. In addition, monensin was shown to have combined effects with anti-androgens — the drugs suppressing the effects of androgens — in preventing prostate cancer cell growth.

“These research findings give rise to a potential new use for the monensin. The results also demonstrate that the effects of anti-androgens in suppressing the growth of cancer cells can be enhanced by using drugs inducing production of reactive oxygen species,” say Senior Research Scientist Kristiina Iljin from VTT and Research Scientist Kirsi Ketola from the University of Turku.

The research findings concerning the effects of drugs and micromolecules were published in the Clinical Cancer Research journal in 2009. The effects of monensin on preventing the growth of prostate cancer was published in the Molecular Cancer Therapeutics journal in December 2010.

Recently, medical companies have shown great interest in these kinds of projects aiming at finding novel indications for established drugs. Since the dosage and adverse effects of drugs already in use and their combined effects with other drugs are relatively well known, this kind of drug repositioning may result in considerable cost savings.

Prostate cancer is the second most common cause of cancer death in men after lung cancer. It has been estimated that globally about 300,000 men die from prostate cancer every year.

Human Immune System Has Emergency Backup Plan

Human Immune System Has Emergency Backup Plan

ScienceDaily (Dec. 27, 2010) — New research by scientists at the University of California, San Diego School of Medicine and Skaggs School of Pharmacy and Pharmaceutical Sciences reveals that the immune system has an effective backup plan to protect the body from infection when the “master regulator” of the body’s innate immune system fails. The study appears in the December 19 online issue of the journal Nature Immunology.

The innate immune system defends the body against infections caused by bacteria and viruses, but also causes inflammation which, when uncontrolled, can contribute to chronic illnesses such as heart disease, arthritis, type 2 diabetes and cancer. A molecule known as nuclear factor kappa B (NF-κB) has been regarded as the “master regulator” of the body’s innate immune response, receiving signals of injury or infection and activating genes for microbial killing and inflammation.

Led by Michael Karin, PhD, Distinguished Professor of Pharmacology, the UC San Diego team studied the immune function of laboratory mice in which genetic tools were used to block the pathway for NF-κB activation. While prevailing logic suggested these mice should be highly susceptible to bacterial infection, the researchers made the unexpected and counterintuitive discovery that NF-κB-deficient mice were able to clear bacteria that cause a skin infection even more quickly than normal mice.

“We discovered that loss of NF-κB caused mice to produce a potent immune-activating molecule known as interleukin-1 beta (IL-1β), which in turn stimulated their bone marrow to produce dramatically increased numbers of white blood cells known as neutrophils,” said Karin. Neutrophils are the body’s front-line defenders against infection, capable of swallowing and killing bacteria with a variety of natural antibiotic enzymes and proteases.

The new research demonstrates that the innate immune system deploys two effective strategies to deal with invasive bacterial infection, and that the IL-1β system provides an important safety net when NF-κB falls short.

“Having a backup system in place is critical given the diverse strategies that bacterial pathogens have evolved to avoid bacterial clearance,” said Victor Nizet, MD, professor of pediatrics and pharmacy, whose laboratory conducted the infectious challenge experiments in the study. “A number of bacteria are known to suppress pathways required for NF-κB activation, so IL-1β signaling could help us recognize and respond to these threats.”

While helpful in short-term defense against a severe bacterial infection, the dramatic increase in neutrophil counts seen in the NF-κB-deficient mice ultimately came at a cost. Over many weeks, these activated immune cells produced inflammation in multiple organs and led to the premature death of the animals. Long-term blockade of NF-κB signaling has been explored extensively by the biotechnology and pharmaceutical industry as a strategy for anti-inflammatory or anti-cancer therapy, perhaps unaware of the risks suggested by this new research.

“One might contemplate adding a second inhibitor of IL-1β signaling to protect against the over-exuberant neutrophil response,” said Karin. “Unfortunately, loss of both the NF-κB pathway and the backup IL-1β pathway rendered the mice highly susceptible to invasive bacterial infection which they no longer cleared.”

Altogether, the UC San Diego research sheds new light on the complex and elegant regulatory pathways required for a highly effective innate immune system. The scientists noted that future investigations must take into account these interrelationships in order to design novel drugs against inflammatory diseases that achieve their treatment goals while minimizing the risk of infection.

Lead authors of the study were former UC San Diego postdoctoral fellows Li-Chung Hsu, now at National Taiwan University in Taipei, and Thomas Enzler, currently at the University of Goettingen in Germany. Additional contributors include Guan-Yi Yu and Vladislav Temkin of the UCSD Department of Pharmacology; Anjuli Timmer of the UCSD Department of Pediatrics; Jun Seita and Irving Weissman of the Institute for Stem Cell Biology at Stanford University School of Medicine; Chih-Yuan Lee, Ting-Yu Lai, Guann-Yi Yu, and Liang-Chuan Lai of National Taiwan University; and Ursula Sinzig and Thiha Aung of the University of Goettingen.

The research of Karin, Nizet and Weissman was supported by grants from the National Institutes of Health.

Modified probiotics may help to fight fat: Study

Modified probiotics may help to fight fat: Study

By Nathan Gray, 23-Dec-2010

Related topics: Research, Probiotics and prebiotics, Weight management

Probiotic bacteria strains tailored to express produce conjugated linoleic acid (CLA) may be able to modify fat tissues, and could play a role in the prevention and treatment of obesity, according to new research in mice.

The study, published in Microbiology, produced Lactobacillus probiotics that were specially designed to express a CLA producing enzyme from other bacteria. The researchers said that their findings could lead to specialised probiotics that have a role in the prevention or treatment of weight management issues.

“These data demonstrate that a single gene (encoding CLA isomerase) expressed in an intestinal microbe can influence the fatty acid composition of host fat,” said the researchers, from the Alimentary Pharmabiotic Centre (APC), Cork, Ireland.

The scientists successfully cloned and overexpressed a gene known to produce CLA from Propionibacterium acnes in Lactococcus lactis bacteria, resulting in a probiotic strain that achieved conversion rates of more than 50 percent of linoleic acid to t10, c12 CLA – a specific type of CLA known to be beneficial in fat tissues.

“To our knowledge the first report to demonstrate that oral administration of a genetically modified t10, c12 CLA-producing strain (containing the single gene for t10, c12 CLA production) results in modulation of the fatty acid composition of the host, including significantly higher concentrations of t10, c12 CLA in adipose tissue, which is directly attributable to the presence of the t10, c12 CLA isomerase gene,” said the researchers.

Good bacteria

The authors noted that evidence is emerging to support the concept that the microbiota can have “profound effects on human health and disease, involving complex host–bacteria interactions that are as yet poorly understood.”

They noted that the gut microbiota is important to the host with regard to metabolic functions, providing nutrients and may offer some resistance to bacterial infections. In addition, the microbiota has been shown to have an effect on disease processes outside the gut.

“CLA has already been shown to alleviate non-alcoholic fatty liver disease that often accompanies obesity. Therefore, increasing levels of CLA in the liver by ingestion of a probiotic strain is of therapeutic relevance,” said Dr Catherine Stanton one of the lead authors of the study.

“Furthermore, fat is not an inert layer around our bodies, it is active and pro-inflammatory and is a risk factor for many diseases, including cancers. The work shows that there is potential to influence this through diet-microbe-host interactions in the gut,” she explained.

Study details

The researchers investigated whether the recombinant Lactobacillus, expressing CLA isomerase from Propionibacterium acnes could influence the fatty acid composition of bodily tissues in a mouse model.

Linoleic-acid-supplemented diets were fed in combination with either a recombinant t10, c12 CLA-producing Lactobacillus or a control strain, to mice for 8 weeks.

Stanton and colleagues reported that ingestion of the strain expressing the CLA isomerase was associated with a 4-fold increase in t10, c12 CLA in the fat tissues of mice when compared with mice that received the non-CLA-producing strain.

“This study demonstrates that t10, c12 CLA production occurred in vivo when a recombinant

Lactobacillus strain harbouring the gene encoding t10, c12 CLA isomerase was administered to mice,” they said.

“We need to further investigate the effects of CLA-producing bacteria on human metabolism, but our work so far certainly opens up new possibilities for the use of probiotics for improvement of human health,” added Dr Stanton.

“It is possible that a CLA-producing probiotic may also be able to keep colon cancer cells in check. All our findings to date demonstrate that the metabolism of gut bacteria can modulate host cell activity in ways that are beneficial to the host,” she said.

Source: Microbiology
Published online ahead of print, doi: 10.1099/mic.0.043406-0
“Recombinant lactobacilli expressing linoleic acid isomerase can modulate the fatty acid composition of host adipose tissue in mice”
Authors: E. Rosberg-Cody, C. Stanton, L. O’Mahony, R. Wall, F. Shanahan, E.M. Quigley, G.F. Fitzgerald, R.P. Ross

‘Un-Growth Hormone’ Increases Longevity, Researchers Find

‘Un-Growth Hormone’ Increases Longevity, Researchers Find

ScienceDaily (Dec. 23, 2010) — A compound which acts in the opposite way as growth hormone can reverse some of the signs of aging, a research team that includes a Saint Louis University physician has shown. The finding may be counter-intuitive to some older adults who take growth hormone, thinking it will help revitalize them.

 

Their research was published in the Dec. 6 online edition of the Proceedings of the National Academy of Sciences.

The findings are significant, says John E. Morley, M.D., study co-investigator and director of the divisions of geriatric medicine and endocrinology at Saint Louis University School of Medicine, because people sometimes take growth hormone, believing it will be the fountain of youth.

“Many older people have been taking growth hormone to rejuvenate themselves,” Morley said. “These results strongly suggest that growth hormone, when given to middle aged and older people, may be hazardous.”

The scientists studied the compound MZ-5-156, a “growth hormone-releasing hormone (GHRH) antagonist.” They conducted their research in the SAMP8 mouse model, a strain engineered for studies of the aging process. Overall, the researchers found that MZ-5-156 had positive effects on oxidative stress in the brain, improving cognition, telomerase activity (the actions of an enzyme which protects DNA material) and life span, while decreasing tumor activity.

MZ-5-156, like many GHRH antagonists, inhibited several human cancers, including prostate, breast, brain and lung cancers. It also had positive effects on learning, and is linked to improvements in short-term memory. The antioxidant actions led to less oxidative stress, reversing cognitive impairment in the aging mouse.

William A. Banks, M.D., lead study author and professor of internal medicine and geriatrics at the University of Washington School of Medicine in Seattle, said the results lead the team “to determine that antagonists of growth hormone-releasing hormone have beneficial effects on aging.”

The study team included as its corresponding author Andrew V. Schally, M.D., Ph.D., a professor in the department of pathology and division of hematology/oncology at the University of Miami Miller School of Medicine.

Disclaimer: This article is not intended to provide medical advice, diagnosis or treatment. Views expressed here do not necessarily reflect those of ScienceDaily or its staff

Sales are niche, but “omega-3 craze” is not over, says industry

Sales are niche, but “omega-3 craze” is not over, says industry

Post a commentBy Shane Starling, 21-Dec-2010

Related topics: Health claims, Omega-3, Industry, Nutritional lipids and oils, Cardiovascular health, Cognitive and mental function

High-profile omega-3 product withdrawals or underperforming products do not signal a crisis in the category, rather an acknowledgement of its nascent status, industry figures have said.

 

Danino spells ‘withdrawn’ in Canada

Responding to a recent article in Kids Nutrition Report (KNR) that highlighted market removal of a Danone DHA-fortified yogurt in Canada called Danino and underwhelming sales of a Sara Lee DHA bread in the US, Ocean Nutrition Canada chairman Robert Orr said the state of play reflected an industry that was still figuring out the best way to incorporate omega-3s into foods and market them.

Orr said the global deficiency in omega-3s was only slowly being addressed, the broader functional foods market still developing, and therefore sectors like his were taking the “long view”.

“Yes there have been failures – but the omega-3 success rate for new products is still significantly better than average of new products,” he said, noting sales were modest but above other food industry sectors.

“Yes they will remain predominantly niche and lifestyle oriented for some years yet as the food industry figures out how to market health and products that cost more because their ingredients cost more.”

 

“The truth is that EPA and DHA are important to human health and well being. Omega-3s are among the largest dietary deficiencies in the western diet. The need and demand to improve health is not going away.”

 

Rethink

 

The KNR story said another product, a Unilever omega-3 dairy drink called Amaze marketed with brain health claims, had been pulled from the market in Turkey after four years and was no longer showing up in Unilever’s Indian communications.

“Omega-3 has become a major success in some areas: around the world the omega-3 dietary supplement business is thriving, with supplement sales up 10% in the US in 2010, to over $1 billion (€750 million), making omega-3 the biggest dietary supplement category,” the article states.

 

“Omega-3 has also become a standard ingredient in infant formula. But in food and beverage the omega-3 craze is over – until the omega-3 industry rethinks its strategy. Every year producers of omega-3 oils – from marine and from algal sources – hope for their big-break through. And every year produces another disappointment; 2010 was no exception, and until there’s a major re-think among ingredient suppliers about their technology and strategy, 2011 will be no better, and nor will any following year.”

The article goes on to highlight how formulation improvements are necessary to enable higher-dose foods and drinks to compete with dietary supplements and other heart health offerings like pomegranate and fiber.

RDIs

KNR said the establishment of recommended dietary intakes (RDIs) which the omega-3 industry had lobbied for and been rewarded with in the European Union recently, would not be as valuable as the industry expected.

“Japan has an RDA for omega-3 fatty acids – it is recommended that 2,600mg of DHA be consumed daily – but even so it’s had limited effect on the omega-3 market. Japanese people prefer to get their omega-3 from fish or from supplements – and Westerners are showing every sign of going the same way.”

 

Adam Ismail, the executive director of the Global Organization for EPA and DHA Omega-3s (GOED) said RDIs were important for reasons that were not directly related to their on-package advice.

“An RDI does provide a point of differentiation, in that those countries where omega-3s have RDIs make omega-3s the only ingredient for heart health that has the recognition of an RDI (with the exception of vitamin E),” he said.

“Also, health claims and fortification levels tend to stem from RDIs. In Europe for example, the new daily recommended value (DRV) for omega-3s is actually based on its heart health benefits, and the dosage levels required for using heart health claims will in turn based on this DRV. So in countries with meaningful RDIs, consumers get meaningful dosages in their products.”

GOED will be discussing the issue of RDIs at a conference it is hosting in Salt Lake City on January 14-15, 2011.