X Protocol Health Topic

The X Protocol is a combination approach utilizing ATP for ready cellular energy, systemic enzymes for ready enzyme stores, and sanguinarine for its immune properties.

Learn More About ATP

ATP: The Perfect Energy Currency for the Cell

All organisms from the simplest bacteria to humans use ATP as their primary energy currency. Without ATP, life as we understand it could not exist. The ultimate source of energy for constructing ATP is food. ATP is used for many cell functions including moving substances across cell membranes and supplying the energy needed for muscle contraction. A major role of ATP is supplying the needed energy to synthesize the multi-thousands of types of macromolecules that the cell needs to exist. ATP is manufactured as a result of several cell processes including fermentation, respiration and photosynthesis.
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Attacking Cancer's Sweet Tooth May Be Effective Against Tumors

Cancer cells are energetically expensive - they reproduce quickly and need a readily available source of ATP. Though glycolysis uses up more glucose, it is faster than the oxidative route. And it is safer for the cancer cell. Knocking out the glycolytic pathway could deliver a big blow to tumor cells.

Energy Molecule May Help Cancer Patients

A compound that provides energy in the body could help prevent the muscle loss and weakness that make life miserable and sometimes prove fatal, researchers reported. An infusion of ATP (adenosine 5-triphosphate) stopped weight loss and improved the quality of life in patients with advanced lung cancer.

Randomized Clinical Trial of Adenosine 5'-Triphosphate in Patients With Advanced Non-Small-Cell Lung Cancer

Extracellular adenosine 5'-triphosphate (ATP) is involved in the regulation of a variety of biologic processes, including neurotransmission, muscle contraction, and liver glucose metabolism. In nonrandomized studies involving patients with different tumor types, ATP infusion appeared to inhibit loss of weight and deterioration of quality of life. In randomized studies, ATP had beneficial effects on weight, muscle strength, and quality of life of patients. In patients who were losing weight, ATP prevented further weight loss and maintained muscle strength.
SCIENTIFIC STUDY

Generation of Extracellular ATP in Blood and Its Mediated Inhibition of Host Weight Loss in Tumor-Bearing Mice

The anticancer activities which correlate with the elevated blood plasma ATP concentrations are proposed to be the result of direct action of extracellular ATP on the tumor and host tissues.
SCIENTIFIC STUDY

How Cells Obtain Energy From Food

The energy to drive ATP synthesis in mitochondria ultimately derives from the breakdown of food molecules. Glucose breakdown (which provides chemical energy in the form of ATP) dominates energy production in most animal cells. The complete oxidation (aerobic) of a molecule of glucose to H2O and CO2 is used by the cell to produce about 30 molecules of ATP. In contrast, only 2 molecules of ATP are produced per molecule of glucose by glycolysis (anaerobic) alone. Glycolosis produces ATP without the involvement of molecular oxygen. For many anaerobic organisms (those which do not utilize molecular oxygen and can grow and divide without it) glycolysis is the principal source of the cell's ATP. Quantitatively, fat is a far more important storage form than glycogen, in part because the oxidation of a gram of fat releases about twice as much energy as the oxidation of a gram of glycogen.

Lactic Acid

Most glucose from dietary carbohydrates bypasses the liver and enters the general circulation where it reaches muscle and converts into lactic acid. Lactic acid then goes back into the blood and returns to the liver where it is used as a building block to make liver glycogen. Lactic acid fuels glucose and glycogen production in the liver. Lactic acid may also signal the release of human growth hormone (hGH) from the pituitary. Lactic acid, formed from the breakdown of glucose, is split into a lactate ion and a hydrogen ion. The hydrogen ion is the "acid" in lactic acid that interferes with electrical signals in nerve and muscle tissue. When the rate of lactic acid entry into the blood exceeds our ability to control it effectively, then hydrogen ions begin to lower the pH of muscle, interfering with how the muscles contract.

The Cori/Lactate Cycle

The Cori Cycle is the metabolic pathway in which lactate produced by anaerobic (without oxygen) glycolysis in the muscles moves to the liver and is converted to glucose (gluconeogenesis), which then returns to the muscles and is converted back to lactate. During intese physical exercise, lactate produced in the muscles is sent to the bloodstream and can be used by the liver as a gluco-neogenic substrate. In the Cori cycle the gluconeogenic leg of the cycle is energy consuming. While there is a gain of 2 moles of ATP in the anaerobic glycolysis of glucose, there is a cost of 6 moles of ATP in the gluconeogenesis part of the cycle. The cost of the 4 moles of ATP means the cycle cannot be sustained continuously.
1. The Cori Cycle on Wikipedia
  
  The cycle is also important in producing ATP, an energy source, during muscle activity.
2. Graphic of the Cori Cycle
  
  Illustration showing the Cori cycle's circuit through muscle, blood, and the liver.
3. The Chemical Logic Behind Gluconeogenesis: Lactate Cycle Diagram (scroll to bottom)
  
  Although 6 ATP are used by the liver for each new glucose synthesized and only 2 ATP per glucose are released in the muscle under anaerobic conditions, this "lactate cycle" is advantageous to the organism, since it allows the maintenance of the anaerobic exercise for a little longer (and this can be crucial for survival, e.g., by allowing a prey to outrun its predator, or a predator to keep chasing its prey).

Cancer Cachexia Demonstrates the Energetic Impact of Gluco-neogenesis in Human Metabolism

In growing tumours the oxygen (O2) concentration is critically low. Mammalian cells need O2 for the efficient oxidative dissimilation of sugars and fatty acids, which gives 38 and 128 moles of ATP per mole glucose and palmitic acid, respectively. In the absence of sufficient O2 they have to switch to anaerobic dissimilation, with only 2 moles of ATP and 2 moles of lactic acid from 1 mole of glucose. Since mammalian cells cannot ferment fatty acids, in vivo tumour cells completely depend on glucose fermentation. Growth of these tumour cells require about 40 times more glucose than should be required in the presence of sufficient O2. Compensatory glucose is provided by hepatic (liver) gluconeogenesis from lactic acid. Since lactic acid lowers the intracellular pH, it decreases the activity of pyruvate dehydrogenase, stimulates fermentation, and thus amplifies its own fermentative production. The liver extracts the required energy from amino acids and especially from fatty acids in an oxidative way. The liver must invest 3 times more energy to synthesize glucose (anaerobically) than can be extracted by tumour cells. This may account for weight loss, even when food intake seems adequate. In the liver 6 moles of ATP are invested in the gluconeogenesis of one mole of glucose. The energy content of 4 out of these 6 moles of ATP is dissipated as heat.
SCIENTIFIC ARTICLE

Enhancing ATP Production to Prevent Cancer Cachexia: A New Combinatorial Therapy

Mitochondria are the major intracellular organelles producing ATP molecules via the electron transport chain. Cancer cells have a deviant energy metabolism, and a high rate of glycolysis is related to a high degree of dedifferentiation and proliferation. The overall net ATP production is diminished with cancer, which ultimately leads to cancer cachexia. The present study was designed to investigate the altered energy metabolism in cancer cells and to enhance ATP production in the normal host cell metabolism by enhancing the activities of mitochondrial enzymes.
SCIENTIFIC STUDY

ATP and the High-Fat, Low Carb (Anabolic) Diet

ATP is the source of all metabolic activity in the human body. It is a popular misconception that you must have glycogen and glucose, which come from carbohydrates, for the body to produce and replenish ATP. Protein and fat have their own mechanism for providing energy to the body and replenishing ATP. When carbs make up the bulk of your diet, you basically burn the glucose from the carbs as energy. Glucose enters the body, and insulin is secreted by the pancreas to utilize it for immediate energy, or store it as glycogen in the liver and muscles. The glucose not stored as glycogen is made into triglycerides (body fat). When needed for energy, the stored glycogen is converted back to glucose. On a high fat diet, you are burning fat as your primary fuel instead of using glycogen or breaking down precious (body) protein. When you're utilizing carbs as your main source of energy, the body will break down muscle protein to form glucose to burn for energy once immediate stores are exhausted. One important by-product of the "metabolic shift" that takes place when you move from a high carb diet to the high fat diet is that fat becomes a protector of protein in the body. Red meat is high in creatine, which is one of the compounds that increases high energy phosphates in the blood and the availability of ATP. There's no lack of energy while following the anabolic (muscle-building) diet.

Why Low-Carb Diets Must Be High-Fat, Not High-Protein

Our bodies use carbs for only one purpose: to provide energy. When we cut down on carbs, the energy our bodies need has to come from somewhere else. There are only two choices: protein or fat. During fasting in humans, blood glucose levels are maintained by the breakdown of glycogen in liver and muscle and by the production of glucose primarily from the breakdown of muscle proteins. Dietary proteins are converted to glucose at about fifty-eight percent efficiency, so approximately 100g of protein can produce 58g of glucose via gluconeogenesis. There are 3 basic fuel sources for ATP production: Glucose (mainly from carbohydrates although protein can also be utilised as a glucose source ), Fats (both from the diet and from stored body fats), and Ketones (derived from the metabolism of fats).

Creatine Supplementation in Athletes

Muscle cells generate mechanical work from an energy liberating chemical reaction â€“ ATP is split into ADP and P (phosphate). ATP can be used by muscle cells very quickly, but there is only an extremely limited supply â€“ usually only enough for a few seconds of high intensity work. When the ATP is gone, work stops. Fortunately, the body has several ways to convert ADP back to ATP. The fastest method is to move the phosphate group off of phosphocreatine and onto ADP. This yields ATP â€“ which is immediately available for muscular work â€“ and creatine. There is enough phosphocreatine to keep ATP levels up for several more seconds. So at this point we've moved from 2-3 seconds of all-out work (ATP) to almost 10 seconds (ATP + creatine).
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Creatine and ATP for Muscle Building

Creatine is used for the resynthesis of ATP. There are several methods by which the body rebuilds ATP. The fastest method, without oxygen, is through creatine phosphate. Creatine phosphate is split to yield the phosphate portion of the molecule. This phosphate portion bonds to the ADP (adenosine diphosphate), turning it back to ATP (adenosine triphosphate). Once creatine phosphate stores within the cell are depleted, the body must use other methods to replenish ATP. It is known that creatine phosphate is used to replenish ATP, and that increasing dietary creatine allows the maximum amount of creatine phosphate storage to be reached, which in turn provides more capacity to regenerate ATP.

Foods High in Creatine

Creatine monohydrate is highly useful for the production of phosphocreatine, an element highly vital to produce ATP. Creatine is formed in the liver, pancreas, and kidneys. One of the prime natural sources of natural creatine is red meat, especially lean meat. It is estimated that every one pound of raw meat contains two grams of creatine. Another great source of natural creatine is fish like tuna, salmon, sashimi, and sushi, which have in it properties such as methionine and Omega 3 fatty acids that aid for creatine synthesis. Likewise, a minimal amount of creatine can be found in milk and cranberries.

Glycolysis and Alcoholic Fermentation

When the oxygen supply runs short in heavy or prolonged exercise, muscles obtain most of their energy from an anaerobic (without oxygen) process called glycolysis. Glycolysis is the chemical breakdown of glucose to lactic acid. This process makes energy available for cell activity in the form of a high-energy phosphate compound known as adenosine triphosphate (ATP).
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The Therapeutic Potential of ATP (Adenosine Triphosphate) as an Immune Modulator in the Treatment of HIV/AIDS

The research goal is to utilize ATP as part of an HIV eradication protocol given along-side traditional highly active antiretroviral therapies (HAART). As a natural compound, adenosine triphosphate (ATP), applied to the outside of cells elicits profound changes in how a cell will function.
SCIENTIFIC STUDY

Adenosine Triphosphate for Cancer Cachexia (pdf)

Cancer cachexia adversely affects quality of life by invariably producing deilitating fatigue and psychological distress. The conclusion of the study was that ATP supplementation improved nutritional status by maintaining energy intake without reducing resting energy expenditure. In addition, muscle strength and quality of life did not decline in the ATP study group. The benefit of ATP appears to be in preventing further decline in nutritional and functional status produced by the cachectic process. Treatment should ideally be given at the earliest evidence of cachexia when patients still have good function.
SCIENTIFIC STUDY

Tags: ATP and adenosine triphosphate, ATP and adenosine diphosphate, ATP and ADP, ATP and energy, ATP and lactic acid, ATP and lactate, ATP and cori cycle, ATP and lactate cycle, ATP and liver, ATP and gluconeogenesis, ATP and glycolosis, ATP and cachexia, ATP and creatine, ATP and protein, ATP supplement, ATP and AIDS, ATP and HIV

ATP has not been evaluated or approved by the FDA for the any of the following topics indicated in the links above: Aids/HIV, bodybuilding, cachexia, cancer, energy production

Statements on this website have NOT been evaluated by the Food and Drug Administration and are NOT intended to diagnose, treat, cure, or prevent any disease; research is ongoing. All third-party health topic links provided on this website are for information purposes only. Always consult your doctor or nutritionist about any health or nutrition-related questions you might have.

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Learn More About Enzymes

Proteolytic Enzymes

Enzymes are proteins that facilitate chemical reactions in living organisms. All of the minerals and vitamins you eat, and all of the hormones your body produces need enzymes in order to work properly. In fact, enzymes govern every single metabolic function in your body. The vast majority of metabolic enzymes in the body â€“ the enzymes that regulate everything from liver function to the immune system â€“ are proteases, or proteolytic enzymes, which regulate protein function in the body. When we eat foods that are enzyme-dead (cooked or processed), we force the body to divert its production of enzymes away from metabolic proteolytic enzymes, which govern metabolic functions, into digestive proteolytic enzymes designed to break down dead proteins in our diets. Supplemental proteolytic enzymes can help reduce inflammation, speed healing of bruises and other tissue injuries (including fractures), and reduce overall recovery time when compared to athletes taking a placebo. Proteolytic enzymes are the primary tools the body uses to "digest" organic debris in the circulatory and lymph systems.
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The Condensed Enzyme Fact Reference

Raw foods naturally contain enzymes. However, even raw food contains only enough enzymes to digest that particular food, not enough to be stored in the body for later use. The cooking or processing of food destroys all of its enzymes. Since most of the foods we eat are cooked or processed in some way and since the raw foods we do eat contain only enough enzymes to process that particular food, our bodies must produce the majority of the digestive enzymes we require, unless we use supplemental enzymes. We are born with the ability to produce a finite number of enzymes during our lifetime. Unless those enzymes are in the (living) food we just ate, we use much of our enzyme potential making the digestive enzymes necessary to digest our food. This limits our ability to produce metabolic enzymes. Using supplemental enzymes to promote digestion reduces our need to produce digestive enzymes, allowing our body to produce the metabolic enzymes needed. Proteases break down protein, amylase breaks down carbohydrate and starch, and lipase breaks down fat. lactase breaks down lactose (dairy), maltase and sucrase break down food sugars, and cellulase breaks down cellulose. Obese individuals were found to have deficiency in the enzyme lipase, which aids the body in breaking down and storing fats. Research has shown abundant laboratory proof of profoundly disturbed enzyme chemistry in cancer patients. Allergies may be helped if certain enzyme supplements are taken that can act as scavenger enzymes or as protein digestive enzymes. A complete and robust array of enzymes in our bodies is the most important requirement for a strong immune system.
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Raw Foods and Enzymes

Once enzymes are exposed to heat, they are no longer able to provide the function for which they were designed. Cooked food's enzyme content is damaged and thus requires us to make our own enzymes to process the food. Digestion of cooked food demands much more energy than the digestion of raw food. In general, raw food is so much more easily digested. Raw foods are rich in enzymes. The human body makes approximately 22 different digestive enzymes. Eating enzyme-dead foods places a burden on your pancreas. In 1930, research in Switzerland found that after a person eats cooked food, his/her blood responds immediately by increasing the number of white blood cells. This is a well-known phenomena called 'digestive leukocytosis'. Eating raw, unaltered food did not cause a reaction in the blood.
Immuno-Enzymatic Therapy: A Review of the Literature

All enzymes accelerate reactions, or even permit reactions that otherwise would not happen, while the enzymes themselves end up unchanged. Enzymes therefore are catalysts and can act over and over again doing the same thing. Most enzymes are highly specific. Proteases are specifically directed to proteins, glucosidases attack sugars, lipases attack fats. Each digestive enzyme acts upon one substance at a time. The substance acted on is termed a substrate. Thus an enzyme first encounters a substrate to form an enzyme-substrate conjugation. After reaction, the enzyme is left intact and there is now an altered substrate. The way substrates are digested by enzymes is beautifully simple: some part of a length of protein (or carbhohydrate or fat) fits into a specific site or pocket on the enzyme. Within this comformable pocket is a niche called the active site where the actual reaction or cleavage takes place. This mutual fit between enzyme and substrate is often compared to a key in a lock. We know now that enzymes are flexible and plastic during their functioning, and for an enzyme to function properly, it must be flexible. Thus an enzyme attaches, undergoes flexure thus straining the substrate, and a bond is broken in the substrate. Many enzymes require helper molecules. Such factors can be vitamins, minerals or simple molecules. These co-enzymes must be present to facilitate attachment to the substrate. The pancreas has two major functions: production of insulin (endocrine pancreas) and the production of the digestive enzymes (exocrine pancreas). Pancreatic enzymes are important in cancer therapy. The pancreas and its enzymes are a true component of the immune system. For any enzyme, any substrate can be an inhibitor. While the substrate is attatched to the enzyme, the enzyme is not able to act on other substrates. For this reason, when there is a large ratio of substrate versus enzyme, the enzymatic transformation is limited. The best way to overcome this is to increase the amount of enzymes. A cancer cell secretes a number of substances that reversibly inhibit the proteases of the body, usually glyco-proteins. Pancreatic enzymes must work over time to overcome this inhibition. Usually this is too much of a burden for the pancreas without risking enlargement, inflammation and dysfunction. Vegan diets and certain forms of vegetarianism can alter the metabolism unfavorably, especially with regard to enzyme synthesis. Systemic amylase levels are actually higher in meat eaters than in vegetarians. Low amylase levels can result in poor reactions to enzymatic therapy. A study by researchers in Israel showed that proteolytic enzymes of the serine type (trypsin, chymotrypsin and carboxypeptidase for example) caused human myeloid leukemic cells to undergo differentiation to benign and functionally normal leukocyte cells.
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Pancreatic Cancer, Proteolytic Enzyme Therapy and Detoxification

The Scottish embryologist, John Beard, who worked at the University of Edinburgh at the turn of the century, first proposed in 1906 that pancreatic proteolytic enzymes, in addition to their well-known digestive function, represent the body's main defense against cancer. He further proposed that pancreatic enzymes would most likely be useful as a cancer treatment.
Food Enzymes, the First Line of Defense

Research by Scottish embryologist named Dr. John Beard is documented in "The Enzyme Treatment of Cancer and Its Scientific Basis" copyrighted in 1911. Research shows that protein digesting enzymes can dissolve the protein coating from around cancer cells, and this enables white blood cells (which are part of the immune system) to destroy the cancer cells. Cancer cells are actually trophoblasts cells that are misbehaving. Trophoblasts cells are basic to the development of every newly conceived baby. But if out of control trophoblast activity begins to occur in later life, then cancer is the result. the pancreas has a limited capability to produce enzymes. The pancreas is almost always overworked trying to produce enough digestive enzymes to digest the cooked food that we eat. Cooked, refined and processed foods have no enzymes.
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Evaluation of Pancreatic Proteolytic Enzyme Treatment of Adenocarcinoma of the Pancreas, with Nutrition and Detoxification Support

A 2-year, unblinded, 1-treatment arm, 10-patient, pilot prospective case study was used to assess survival in patients suffering inoperable stage II-IV pancreatic adenocarcinoma treated with large doses of orally ingested pancreatic enzymes, nutritional supplements, "detoxification" procedures, and an organic diet. This pilot study suggests that an aggressive nutritional therapy with large doses of pancreatic enzymes led to significantly increased survival over what would normally be expected for patients with inoperable pancreatic adenocarcinoma.
SCIENTIFIC STUDY
Pancreatic Enzyme Extract Improves Survival in Murine Pancreatic Cancer

The treatment with porcine pancreatic enzyme extracts significantly prolongs the survival of mice with human pancreatic cancer xenografts and slows the tumor growth. The data indicate that the beneficial effect of porcine pancreatic enzyme extracts on survival is primarily related to the nutritional advantage of the treated mice.
SCIENTIFIC STUDY
Pancreatic Enzymes Block Food Allergy Reactions

In one study, administration of pancreatic enzymes markedly reduced the severity of food-induced symptoms in ten patients with know food allergies. It is possible that some of the improvement (e.g., the intestinal symptoms) was due to an enhancement of digestive function, rather than to an anti-allergy mechanism.
Spider Veins and Enyzme Therapy

Vitamins and minerals are really co-enzymes and co-factors. They are things that make enzymes work better; but what if you don't have much of the enzymes to begin with? Then the co-enzymes won't work! Systemic enzymes effect on spider veins was discovered when patients in Europe, where doctors prescribe systemic enzymes, reported the clearing up of spider veins and easing of varicose vein discomfort.
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Enzymes and Life Processes (Introduction to Enzymes)

Metabolism is the process of chemical and physical change which goes on continually in the living organism. Build-up of new tissue, replacement of old tissue, conversion of food to energy, disposal of waste materials, reproduction â€“ all the activities that we characterize as "life." Enzymes and are responsible for bringing about almost all of the chemical reactions in living organisms. Without enzymes, these reactions take place at a rate far too slow for the pace of metabolism.
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Digestive Enzymes

There are three classes of digestive enzymes: proteolytic enzymes needed to digest protein, lipases needed to digest fat, and amylases needed to digest carbohydrates. Digestive enzymes include pancreatic enzymes, plant-derived enzymes, and fungal-derived enzymes. They work optimally at specific temperature and pH.
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Effects of pH (Introduction to Enzymes)

Enzymes are affected by changes in pH. The most favorable pH value â€“ the point where the enzyme is most active â€“ is known as the optimum pH. Extremely high or low pH values generally result in complete loss of activity for most enzymes. pH is also a factor in the stability of enzymes. As with activity, for each enzyme there is also a region of pH optimal stability. Includes chart showing the pH for optimum activity of various enzymes.
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The Importance of Digestive Enzymes for Health and Longevity

Systemic enzyme therapy fights inflammation: fights fibrosisa type of scar tissue formation containing fibrin: helps increase the immune response; maintains a normal blood flow by helping to prevent blood clots and platelet aggregations within blood vessels; and disrupts a virus' outer protein wall and renders it inert by inhibiting replication.

Tags: enzymes, digestive enzymes, proteolytic enzymes, enzymes and processed foods, enzymes and raw foods, enzymes and pH, enzymes and co-factors, enzymes and pancreas, enzymes and inflammation, enzymes and allergies, enzymes and cancer, enzymes and pancreatic cancer, enzymes and leukemia, enzymes and spider veins, enzymes and varicose veins, enzymes and the immune system.

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Learn More About Sanguinarine

Differential Antiproliferative and Apoptotic Response of Sanguinarine for Cancer Cells Versus Normal Cells

Sanguinarine, derived from the root of Sanguinaria canadendid, has been shown to possess antimicrobial, anti-inflammatory, and antioxidant properties. Sanguinarine is a potential antiproliferative agent that can be developed as a potential agent for skin cancer. The life-span of normal cells as well as cancer cells within a living system is regarded to be significantly affected by the rate of apoptosis. Because apoptosis is a discrete manner of cell death that differs from necrotic cell death and is regarded as an ideal way to eliminate damaged cells, agents that can modulate apoptosis may be used for the management and therapy of cancer. Sanguinarine imparts a cell growth-inhibitory response in human squamous carcinoma (A431) cells via an induction of apoptosis. Sanguinarine also functions as a potent inhibitor of the oxidant- and/or tumor promoter-mediated activation of NF-ÎºB. Studies have indicated that NF-ÎºB promotes cell survival by inhibiting apoptosis. Sanguinarine treatment resulted in dose-dependent apoptosis in A431 cells. Sanguinarine treatment also resulted in necrosis of A431 cells. The apoptotic response of sanguinarine was not limited only to the A431 cells because similar treatment also resulted in the apoptotic cell death of other human cancer cell types. By modulating apoptosis, sanguinarine may be able to affect the steady-state cell population and thus possesses a potential for development as an agent for cancer chemotherapy.
SCIENTIFIC STUDY
Activation of Prodeath Bcl-2 Family Proteins and Mitochondrial Apoptosis Pathway by Sanguinarine in Immortalized Human HaCaT Keratinocytes

Because mitochondrial pathway is critical for the regulation of apoptosis, we studied the involvement and regulation of mitochondrial events in sanguinarine-mediated apoptosis. In the process of apoptosis, mitochondria plays a central but complex role. Mitochondria is increasingly appreciated as a target for the management of cancer, and the agents that can modulate mitochondrial events and the process of apoptosis (thereby being able to affect the steady-state cell population) may be useful in the management of cancer. Sanguinarine treatment results in an inhibition of cell proliferation and induction of apoptosis in HaCaT keratinocytes. Sanguinarine, a naturally occurring alkaloid extract of S. canadensis, has been shown to possess antioxidative, antitumor, antibacterial activities, and anti-inflammatory properties in animals and to reduce gingival inflammation and supragingival plaque when used clinically. It has been used in many over-the-counter products, including toothpaste, mouthwash, cough and cold remedies, and homeopathic preparations. Sanguinarine has a broad in vitro activity against Gram-positive and Gram-negative bacteria, fungi, and some protozoa. In ancient times, sanguinarine- containing herbs such as bloodroot were believed to possess anticancer activity. These herbs have long been used by Native American healers to treat cancer. Sanguinarine has been shown to inhibit several enzymatic activities and signaling pathways. Impaired apoptosis is a crucial step in the process of cancer development. The modulation of mitochondrial events and the process of apoptosis by sanguinarine may be useful in the management (chemoprevention as well as chemotherapy) of skin cancer and possibly other hyperproliferative skin disorders by promoting endogenous apoptosis-inducing mechanisms. Sanguinarine treatment did not result in apoptosis of the normal human epidermal keratinocytes at similar dose.
SCIENTIFIC STUDY
Sanguinarine Causes Cell Cycle Blockade and Apoptosis of Human Prostate Carcinoma Cells

Sanguinarine, an alkaloid derived from the bloodroot plant Sanguinaria canadensis, induced growth inhibitory and antiproliferative effects in human prostate carcinoma cells irrespective of their androgen status.
SCIENTIFIC STUDY
Suppression of Angiogenesis by the Plant Alkaloid Sanguinarine

Angiogenesis is indispensable for inflammation, and most angiogenesis is dependent on vascular endothelial growth factor (VEGF). Sanguinarine markedly suppressed VEGF-induced endothelial cell migration, sprouting, and survival in vitro. Sanguinarine potently suppressed blood vessel formation in vivo. Sanguinarine is a potent antiangiogenic natural product, and its mode of action could involve the blocking of VEGF-induced Akt activation. In addition to antibacterial, antifungal, and anti-inflammatory activities, sanguinarine has a novel antiangiogenic role.
SCIENTIFIC STUDY
In Vitro Susceptibility of Helicobacter Pylori to Isoquinoline Alkaloids from Sanguinaria Canadensis

The rhizome extracts, as well as a methanol extract of Sanguinaria canadensis suspension-cell cultures inhibited the growth of H. pylori in vitro.
SCIENTIFIC STUDY
Bloodroot on Drugs.com

Bloodroot is an early spring wildflower. The stout rhizome yields a bright red latex when cut, giving the plant its common name. Bloodroot was used by eastern Native American tribes as a red dye and in the treatment of ulcers, skin conditions, and as a blood purifier. The root entered 19th century medicine as a caustic topical treatment for skin cancers, polyps, and warts. Virtually all isolates from human dental plaque were growth-inhibited by sanguinarine. Another similar clinical study of sanguinarine with zinc chloride found reductions in plaque bacteria. Although sanguinarine is modestly effective in dental plaque and gingivitis prevention and treatment, it is inferior to newer agents under development.
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Bloodroot on Health Line

Bloodroot (Sanguinaria canadensis) is a perennial plant with a white flower that blooms in early spring. It belongs to the poppy family (Papaveraceae) and grows in wooded areas throughout the northeastern regions of the United States and Canada. Bloodroot gets its name from its bright red root that, when cut open, oozes a crimson, blood-like juice.
Neoplasene (Bloodroot Extract) and Animal Cancers (pdf file)

WARNING: CONTAINS GRAPHIC IMAGERY
Case studies: treatment of neoplasm, proud flesh and warts with sanguinarine and related isoquinoline alkaloids.
VETERINARY STUDY

Tags: sanguinarine, sanguinarine and apoptosis, sanguinarine and cancer, sanguinarine and skin cancer, sanguinarine and prostate cancer, sanguinarine and angiogenesis, sanguinarine and dental caries, sanguinarine and dental plaque, sanguinarine and bloodroot, sanguinarine and neoplasene

Sanguinarine has not been evaluated or approved by the FDA for the any of the following topics indicated in the links above: apoptosis, cancer, dental caries

PLEASE READ FULL DISCLAIMER HERE

Questions? 1 (951) 639-9708

X Protocol Health Topic

Learn More About ATP

Learn More About Enzymes

Learn More About Sanguinarine