Category Archives: Cancer

Glutamine Deprivation May Slow Pancreatic Cancer

Tumor growth in pancreatic cancer patients may be slowed using glutamine. Glutamine is an amino acid, which is one of the building blocks of proteins. Although it is typically considered a non-essential amino acid (meaning the body may make it on its own), glutamine is technically a conditionally essential amino acid. The term “essential” means that it must be gotten through the diet, so this amino acid is—in certain circumstances—acquired via intake of food.

Glutamine, which is the most abundant amino acid in the human body, plays a role in cancer tumor growth; so depriving the cancer cells of glutamine may hold the key to slowing the spread of cancer of the pancreas, a study shows.

Study on pancreatic tumor growth and glutamine

At the Division of Genomic Stability and DNA Repair, Department of Radiation Oncology (part of the Dana-Farber Cancer Institute) in Boston, Massachusetts, a group of researchers and doctors, J Son, CA Lyssiotis, et al., have investigated just how the amino acid glutamine is involved with the KRAS-regulated metabolic pathway, which is part of the cause of tumor growth within the pancreas itself.

The researchers studied the metabolism of cancer cells and glutamine dependencies since, unlike normal cells, the cells within cancer tumors maintain their own type of metabolism. They said that “an increased use of the amino acid glutamine to fuel anabolic processes. Indeed, the spectrum of glutamine-dependent tumors and the mechanisms whereby glutamine supports cancer metabolism remain areas of active investigation.”

Because human pancreatic cells use a non-standard pathway, which identifies ductal adenocarcinoma (PDAC) cells, most cells use “glutamate dehydrogenase (GLUD1) to convert glutamine-derived glutamate.” What this means is that the PDAC cells “are strongly dependent … as glutamine deprivation or genetic inhibition of any enzyme in this pathway leads to [a] series of reactions [that] results in a pronounced suppression of PDAC growth in vitro and in vivo.”

The scientists established that because the glutamine metabolism is reprogrammed and “mediated by oncogenic KRAS, the signature genetic alteration in PDAC [represses] key metabolic enzymes in this pathway.”

With the PDAC pathway and pancreatic cells being dispensable, the glutamine in normal cells then becomes a possible new therapeutic approach in treating pancreatic tumors in humans. Hopefully more will be forthcoming on this new technique in the near future.

Reference:

http://www.ncbi.nlm.nih.gov/pubmed/23535601

Prevent Prostate Cancer with Three Amino Acids?

Three specific amino acids may aid in the prevention of prostate cancer according to a study. The three aminos include methionine, phenylalanine, and tyrosine. During protein synthesis by the body, the amino acids tyrosine, methionine, and phenylalanine are utilized. Restriction of these amino acids depends on glucose metabolism, which when altered aids in cell death of cancer cells within human prostate cancer, and may aid in preventing prostate cancer.

Study linking amino acids and prostate cancer prevention

YM Fu, H Lin, et al., did a study at the Department of Pharmaceutical Sciences at Washington State University said that it is selective amino acid restriction of tyrosine and phenylalanine, plus methionine or glutamine that target mitochondria in cells that are linked to prostate cancer cell death.

Glucose metabolism modulation is tied to the process and “crucial switches connecting metabolism and these signaling molecules to cell survival during amino acid restriction” become target factors preventing prostate cancer, say the researchers.

Second study on prostate cancer and amino acids

Another study by YS Kim from Washington State University showed an identification of molecular targets regarding specific amino acid dependency and how it modulates specific kinds of prostate cancer cells. To find out how the amino acids can prevent prostate cancer, they investigated if restriction of tyrosine, phenylalanine, and methionine could inhibit the growth and metastasis of prostate cancer.

Kim progressed outward in this field of research because of the “underlying the anticancer activity of tyrosine/phenylalanine and methionine restriction. This is especially important research since there still is no satisfactory drug for treatment of androgen-independent, metastatic human prostate cancer.”

Even though further research is needed regarding the amino acids phenylalanine, tyrosine, and methionine for prostate cancer prevention, it has expanded avenues for antimetastatic, anti-invasive, apoptosis-based therapies for the preventing prostate cancer.

Prostate cancer, being one of the major cancers that kill men in the North American continent, is the reason why males should be regularly screened for this deadly disease.

Reference:

http://www.ncbi.nlm.nih.gov/pubmed/20432447

http://prevention.cancer.gov/funding/recently-funded/ca04004/1R01CA101035-01A1

Part 2: Alzheimer’s Prevention? Special Foods and Cysteine and Glutathione Levels

CONTINUED FROM Part 1: Alzheimer’s Prevention? Special Foods and Cysteine and Glutathione Levels, where we covered the research done on Alzheimer’s patients that found Resveratrol affected cysteine and glutathione levels, raising the former, and reducing the latter, and their connection to reduced brain plaques. 

Chemopreventive agents that help cancer patients may also help Alzheimer’s patients…

Chemopreventive agents (food constituents), cysteine, and glutathione

Food-derived chemopreventive agents may help when used by normal-risk populations with long-term use. According to a study by GJ Kelloff, JA Crowell, et al., and their assessment, there are 40 promising agents and food combinations “being evaluated clinically as chemopreventive agents for major cancer targets including breast, prostate, colon and lung. Examples include green and black tea polyphenols, soy isoflavones, Bowman-Birk soy protease inhibitor, curcumin, phenethyl isothiocyanate, sulforaphane, lycopene, indole-3-carbinol, perillyl alcohol, vitamin D, vitamin E, selenium and calcium.” Many of these agents are available to purchase online from supplement vendors such as: GNC.com, Powdercity.com and Vitaminshoppe.com

Additionally, some natural sources that have anti-cancer, antioxidant, anti-tumor, antibacterial, antifungal, and anti-viral constituents includes a huge variety of medicinal mushrooms like reishi, maitake, cordyceps, shiitake, and so on. Lion’s mane mushroom (Hericium erinaceus), in particular, boasts boosting of cognitive function, memory, and learning in those who take them regularly, as well as immune-enhancing health benefits.

Many amino acids are also known to be brain food. Cysteine and glutathione were the aminos that were implicated in the first study mentioned above, although it was the higher levels of cysteine and lowered glutathione that helped the plaque in Alzheimer’s patients.

Cysteine is a semi-essential (normally listed as a non-essential) amino acid. When it is used as a food additive, it has the E number “E920”. In rare cases this amino acid may be important for infants or the elderly, or for people with malabsorption syndromes or metabolic disease. As long as enough methionine is available, cysteine can usually be synthesized by the body.

Cysteine is found in protein foods like: beef, pork, poultry, eggs, and dairy, and in lesser amounts in plant sources such as garlic, onions, broccoli, red peppers, Brussels sprouts, granola/oats, wheat germ, or lentils.

The non-essential amino acid glutathione works as an important antioxidant in animals and plants, fungi and some bacteria, as well as archaea, preventing free radicals and peroxides damage. However, glutathione is not considered an essential nutrient since it can be produced by the body (outside of food) from the amino acids L-cysteine, L-glutamic acid, as well as glycine.

Interestingly, the sulfhydryl (thiol) group of the amino acid cysteine is actually the amino acid responsible for glutathione’s activity in the body. This is why they are connected. Cysteine limits glutathione synthesis in cells since glutathione is rare in foodstuffs.

Remember that in the original study on Alzheimer’s patients and reduced brain plaque formation, it was the connection of increased cysteine and decreased glutathione that may be the link. That study, according to the researchers, “supports the concept that onset of neurodegenerative disease may be delayed or mitigated with use of dietary chemo-preventive agents that protect against beta-amyloid plaque formation and oxidative stress.”

With this in mind, be aware of the fact that chemopreventive foods like Resveratrol in red wine, or garlic, not only may help prevent cancer or improve cardiovascular health, but also are connected to a reduction in Alzheimer’s disease rates due to how it affects amino acids cysteine and glutathione levels. Please check with your doctor before altering your diet.

References:

http://www.ncbi.nlm.nih.gov/pubmed/19041676

http://nutrition.highwire.org/content/130/2/467S.full

http://naturalsolutionsradio.com/blog/natural-solutions-radio-administrator/amazing-nutrient-reduces-alzheimers-plaque-formation-nine

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2797420/

Part 1: Aspartic Acid and Phenylalanine in Aspartame

What are aspartic acid and phenylalanine, and what are their roles as ingredients in the manmade product called aspartame? Is aspartame dangerous or linked to cancer? Many claims exist, but here are some facts and information on the subject, which you might want to consider.

First of all, aspartame is an artificial sweetener; it is known as NutraSweet® and Equal® as well as Spoonful, and Equal-Measure, and is claimed to be up to 200 times sweeter than sugar. Aspartame was, in 1981, approved for use in dry goods, and later in 1983 approved for carbonated beverages. Aspartame basically has three main ingredients: aspartic acid, phenylalanine, and methanol.

I will go briefly over these three ingredients below and then discuss their use in aspartame…

Aspartic acid

Amino acids are the building blocks of proteins, and aspartic acid, also known as asparaginic acid, is a non-essential amino acid. “Non-essential” means that it is not necessary to get this amino acid from food or supplements since the human body makes it on its own. Our bodies need and use aspartic acid within cells to help the body work, especially regarding nervous system functioning, and hormone production/release.

Phenylalanine

Phenylalanine is also an amino acid, but an essential amino acid, which means it can only be gotten from food (our body does not make it on its own). Phenylalanine is the precursor for the amino acid tyrosine, which acts as a neurotransmitter in our brain for signaling dopamine, norepinephrine (noradrenaline), epinephrine (adrenaline), and melanin (skin pigment).

Phenylalanine is also found in breast milk and is a necessary nutrient for newborn babies, which is why it is added to baby formulas. Phenylalanine is a nutritional supplement in food and drink products and is known for its antidepressant and analgesic effects.

All 22 common amino acids, including aspartic acid and phenylalanine, can be gotten from protein foods such as meats, fish, and eggs, and smaller amounts from dairy, legumes, nuts, and vegetables.

Methanol

Where aspartic acid and phenylalanine are natural substances, and needed for proper bodily functioning, methanol is toxic to the human body. Methanol is known as wood alcohol, methyl alcohol, wood naphtha, or wood spirits and is a chemical produced mostly as a byproduct of the destructive distillation of wood. Modern methanol is produced industrially from hydrogen, carbon monoxide, and carbon dioxide. Methanol is simple as alcohols go, flammable, volatile, colorless, and sweeter than ethanol (drinking alcohol). Methanol is used for producing biodiesel, as a fuel, denaturant for ethanol, and is a greenhouse gas.

Ingesting large quantities of methanol causes it to be metabolized to formate salts and formic acid. These may cause coma, blindness, or even death, because they are poison to the central nervous system. Special emphasis on “large quantities.” Why? Keep reading…

CONTINUE TO Part 2: Aspartic Acid and Phenylalanine in Aspartame

References:

http://www.nlm.nih.gov/medlineplus/ency/article/002234.htm

http://articles.mercola.com/sites/articles/archive/2011/11/06/aspartame-most-dangerous-substance-added-to-food.aspx

http://www.cancer.org/cancer/cancercauses/othercarcinogens/athome/aspartame

http://andevidencelibrary.com/topic.cfm?cat=4089&auth=1

L-tyrosine for Treating Depression Symptoms

Alleviating depression can sometimes be daunting, even with pharmaceutical antidepressants prescribed by your doctor. But there are some natural things you can do to help with depression, too, says researchers. Tyrosine, also known as L-tyrosine, is a viable option as a natural-source antidepressant.

In fact, amino acids help play a role in many diseases, and can be used as a tool to predict such diseases since the biological compounds involved in the normal functioning of humans can be involved in the pathogenesis of these same diseases.

W Krzysciak at the Department of Medical Diagnostics at the Jagiellonian University in Poland, talks about aromatic amino acids like tyrosine, and that some of the diseases that are tied to amino acids include the diagnosing and treating of “social disorders, such as cancers; psychiatric disorders: depression, anxiety states, schizophrenia, bipolar affective disorders; neurodegenerative, and cardiovascular diseases; chronic kidney insufficiency or diabetes.”

L-Tyrosine for Depression

There are three aromatic amino acids commonly used to treat or diagnose disorders: tyrosine, tryptophan, and phenylalanine. Where phenylalanine is a pain reliever, and tryptophan promotes sleep, it is tyrosine that acts as an antidepressant.

Dr. Greene (at DC Nutrition) also has information about L-tyrosine, and explains how this aromatic amino acid works to treat depression, saying, “Tyrosine is an essential amino acid that readily passes the blood-brain barrier. Once in the brain, it is a precursor for the neurotransmitters dopamine, norepinephrine and epinephrine, better known as adrenalin. These neurotransmitters are an important part of the body’s sympathetic nervous system.”

L-tyrosine also relieves pain—both emotional pain and physical pain.

Dr. Greene says, “Tyrosine therapy is very useful in a variety of clinical situations. … An average human dose equivalent of 500 mg of tyrosine given intravenously reduces susceptibility to life-threatening ventricular fibrillation in experimental animals. More tyrosine is needed under stress, and tyrosine supplements prevent the stress-induced depletion of norepinephrine and can cure biochemical depression.” The exceptions would include psychosis (since antipsychotic drugs work by inhibiting L-tyrosine metabolism).

Larger doses of L-tyrosine may help reduce hunger as well as alleviate depression symptoms in obese patients. Low doses actually stimulate the appetite, however.

Dr. Greene says that even physicians at Harvard Medical School have used between 1-6 grams of tyrosine to effectively treat depression that was medication-resistant, saying, “The minimum daily requirement for adults of tyrosine and its precursor, phenylalanine, is 16 mg/kg a day or about 1000 mg total. Hence, 6 g is at least six times the minimum daily requirement.”

Please have a discussion with your doctor or naturopath to see if L-tyrosine might be able to help with depression.

References:

http://www.ncbi.nlm.nih.gov/pubmed/22175049

http://www.dcnutrition.com/AminoAcids/Detail.CFM?RecordNumber=129

Tyrosine and Tyrosine Kinase for Thyroid Cancer

Tyrosine amino acid has a number of health benefits; however, it may not be helpful for skin cancer. That said, related to this is the enzyme tyrosine kinase, which is used to treat thyroid cancer according to some research done at the Department of Medicine at Baylor College of Medicine in Houston, Texas.

Thyroid cancer statistics from the American Cancer Society includes:

“About 62,980 new cases of thyroid cancer (47,790 in women, and 15,190 in men)
“About 1,890 deaths from thyroid cancer (1,060 women and 830 men)
“Thyroid cancer is commonly diagnosed at a younger age than most other adult cancers. Nearly 2 out of 3 cases are found in people younger than 55 years of age. About 2% of thyroid cancers occur in children and teens.”

Although tyrosine, an essential amino acid (which means your body produces it on its own rather than relying on diet alone). Protein foods like meats, eggs, and fish provide all 22 amino acids. However, the enzyme tyrosine kinase has been researched as a helpful supplement for treating thyroid cancer. Standards for the treatment are needed, but this medical study below examples how tyrosine kinase is an effective cancer treatment.

Tyrosine kinase as a thyroid cancer treatment

Tyrosine kinase is an enzyme that transfers a phosphate group from ATP over to proteins within cells, which attaches to the amino acid tyrosine on these proteins. The enzyme also attaches to other amino acid such as threonine or serine, but tyrosine kinases have a special ability to mutate to an “on” position. This allows growth of the cells to happen, which is extremely important for treating cancer.

These are called tyrosine kinase inhibitors and can help in cancer treatments, including for thyroid cancer.

A study by AA Carhill, ME Cabanillas, et al., in Houston’s Division of Endocrinology, Diabetes, and Metabolism, have studied tyrosine kinase inhibitor therapy in regards to creating standards for treating patients with thyroid cancer.

The researchers needed a “systematic approach to the clinical application of these agents in order to improve patient safety and monitoring promote consistency among providers, and ensure compliance with both institutional and industry standards.”

Their conclusions were based on the tyrosine kinase inhibitor applications they reviewed, including professional guidelines for thyroid cancer, plus reports, trials, and articles, etc., all published in the prior decade. They also included older studies for tyrosine kinase inhibitors.

The research allowed them to develop a “standardized approach related to prescribing commercially available tyrosine kinase inhibitors … for patients with advanced thyroid cancer.”

It is already important to note the already-established knowledge of enzyme-based tyrosine kinase inhibitor therapy, just as tyrosine and other amino acids are well known for their health benefits, but to help develop a standard for thyroid cancer therapy using enzymes was needed, and the void met.

References:

http://www.ncbi.nlm.nih.gov/pubmed/23185034

http://en.wikipedia.org/wiki/Tyrosine_kinase

http://www.cancer.org/cancer/thyroidcancer/detailedguide/thyroid-cancer-key-statistics

Amino Acids – Their Role in Aggressive Brain Cancer

There is an enzyme that causes the breakdown of certain amino acids, which makes brain cancer aggressive. Scientists have discussed their findings in the Nature Medicine journal. These researchers from the German Cancer Research Center (DKFZ) were looking for new kinds of therapies against aggressive brain cancer when they discovered the amino acids hunger is increased in certain forms of brain cancer.

Tumors that grow quickly and aggressively need more energy feeding them than regular (non-aggressive) brain cancer tumors. Tumors also need the right molecular building blocks to build the components of the cells in order to grow. Cancer is now known to feed on sugar (glucose), and some tumors can also catabolize glutamine, which is an amino acid.

Amino acids and role of enzymes in aggressive tumors

Primary glioblastomas are extremely malignant brain tumors. Glioblastomas also have a connection with the two enzymes BCAT1 and IDH (isocitrate dehydrogenase) because these enzymes cooperate together in decomposing branched-chain amino acids.

Amino acids are the building blocks of proteins, and these proteins can act as a food sources that increase the hunger, or aggressiveness, of cancer cells. For the first time, these scientists have been able to show that branched-chain amino acids have a significant role in the aggressive growth of certain malignant tumors.

Some years ago some researchers found gene coding mutations in IDH for a number of types of brain cancers, such as glioblastomas. If they lacked the IDH gene, then they would grow more slowly due to being defective. Radlwimmer, from the German Cancer Research Center, said that, “we can see that overexpression of BCAT1 contributes to the aggressiveness of glioblastoma cells.”

Their team compared the activity of genes from several hundred brain tumors to find out if intact or altered IDH enzymes had characteristics that might explain the aggressive tumor growth. They did, in fact, find a significance difference between two groups studied. The BCAT1 enzyme in a normal brain breaks down branched-chain amino acids, producing ketoglutarate (BCAT1 needs this molecule). So only intact IDH in tumor cells have the BCAT1 enzyme, so Bernhard Radlwimmer says, “The two enzymes seem to form a kind of functional unit in amino acid catabolism.”

Glioblastomas are what makes the brain cancer tumors particularly aggressive, and when the effects of BCAT1 is blocked, the tumor cells lose their capacity to grow or invade the healthy brain tissue. Also, at that point the cells also release less of the amino acid neurotransmitter—glutamate. When someone has brain cancer they often will get epileptic seizures, which are associated with high glutamate amino acid levels.

Because of this association, and how the researchers understand it now, agents are being searched for to target against the enzymes that are responsible for the aggressive tumor growth. BCAT1 expression is also being studied since it may be a marker to help diagnose brain cancer malignancy.

Reference:

http://www.dkfz.de/en/presse/pressemitteilungen/2013/dkfz-pm-13-35-Brain-Cancer-Hunger-for-Amino-Acids-Makes-It-More-Aggressive.php

Carnitine Deficiency and Cancer Survival Rate

Childhood cancer survivors are at higher risk of developing heart disease than the general population, but a study published in brings good news. Testing for carnitine deficiency could prevent the development of congestive heart failure.

Childhood cancer is the second most common cause of death in children between one and 14 in the US. Leukemia is one of the most common of these cancers of children.

Some cancers, including leukemias, are treated by anthracyclines. Anthracyclines work by slowing or even stopping the growth of cancer cells.

They are extremely effective at treating the cancer, but have serious side effects. The most serious side effect is cardiotoxicity, which means the drugs damage the heart. Anthraclyclines could make the heart weaker, leading to less efficient pumping and circulation. This is known as congestive heart failure.

Researchers (Armenian SH, Gelehrter SK, et al) with Population Sciences, City of Hope, sought to investigate the link between anthracyclines and cardiac dysfunction, and if congestive heart failure could be prevented.

Study finds link between carnitine deficiency and heart failure in cancer survivors

The study, published in Cancer Epidemiol Biomarkers Prev on April 9, 2014, analyzed the hearts and blood plasma of 150 childhood cancer survivors who had previous been treated with anthracyclines.

Their hearts were tested with echocardiograms (ECG). 23% of the study participants had cardiac dysfunction.

When testing the blood plasma levels, which included testing levels of amino acids, the researchers discovered that the participants with cardiac dysfunction had significantly lower plasma carnitine levels.

The researchers concluded discovering this link to carnitine deficiency could lead to prevention, as a carnitine deficiency can be treated before and during anthracycline administration.

Additionally, testing for low levels of carnitine could become part of the screening process for low for patients at high risk of developing heart failure.

Sources: http://www.ncbi.nlm.nih.gov/pubmed/24718281

Part 2: Aspartic Acid and Phenylalanine in Aspartame

In Part 1: Aspartic Acid and Phenylalanine in Aspartame, I covered what the amino acids “aspartic acid” and “phenylalanine” are, and the wood alcohol “methanol” is. Next will be whether any of these have a scientifically known link to cancer or not.

Dangers of aspartame and cancer?

According to some sources claiming aspartame causes cancer, as well as a host of other diseases and health problems, it is important to note that aspartame is made up of approximately 40% aspartic acid, 50% phenylalanine, and 10% methanol. Where some of these sources claim that aspartic acid and phenylalanine could be to blame for health issues, others think that methanol may actually be the culprit.

According to the experts at the American Cancer Society, there is no scientifically discovered proof that aspartame has been linked with cancer. A large study, says the ACS, discussed cancer rates in over 500,000 older adults and found that “compared to people who did not drink aspartame-containing beverages, those who did drink them did not have an increased risk of lymphomas, leukemias, or brain tumors.”

Putting aspartame’s ingredients into perspective

Bernadene Magnuson, PhD, from Cantox Health Sciences International, wrote Relationship Between Aspartame, Methanol and Formaldehyde Explained and put the reality of aspartame into perspective as thus:

“Aspartame is a dipeptide molecule produced by joining phenylalanine and aspartic acid. Aspartame itself does not occur naturally but is a manufactured substance. When aspartame is consumed, it is completely broken down by the enzymes in the digestive system (esterases and peptidases) into the two amino acids and a type of alcohol called methanol. The amounts of these are much less than found in foods. …

“It is important to understand that the human body is well-equipped to use small amounts of methanol produced from foods and beverages, as well as from aspartame. …

“First, the methanol from the intestinal tract goes to the liver via portal blood, where the liver enzyme alcohol dehydrogenase converts methanol into formaldehyde. The body very rapidly uses formaldehyde and so formaldehyde never builds up in the body. If the body doesn’t need it, formaldehyde is converted to formic acid within seconds. The formic acid will be either excreted in the urine or broken down to carbon dioxide and water. …

“The breakdown of formic acid is slower than the breakdown of formaldehyde, so if there is a very large dose of methanol (or formaldehyde) coming into the body, formic acid can build up and that causes the adverse effects seen in methanol poisoning.

“To put this into perspective, studies in healthy adults and infants consuming up to 200mg per kg of body weight (50 times the amounts Americans consume on average), showed no change in the levels of formic acid in the blood.”

Bottom line about aspartic acid, phenylalanine, and methanol

Although the jury is still out for some people on whether aspartame is dangerous, it is clear that aspartic acid and phenylalanine are typically safe for human consumption and needed by the human body.

However, whether small amounts of methanol are “safe” is a factor that some prefer to avoid in their diet, just in case, while others simply consume the poison in these minute amounts. Methanol is typically only poisonous in large quantities. It is really up to the consumer to do the research and decide, as well as seek out professional opinions on the matter.

Please ask your doctor as well, if you have further questions on whether aspartame (or its ingredients aspartic acid, phenylalanine, and methanol) might be safe enough to consume for you in your particular diet and circumstance.

http://www.nlm.nih.gov/medlineplus/ency/article/002234.htm

http://articles.mercola.com/sites/articles/archive/2011/11/06/aspartame-most-dangerous-substance-added-to-food.aspx

http://www.cancer.org/cancer/cancercauses/othercarcinogens/athome/aspartame

http://andevidencelibrary.com/topic.cfm?cat=4089&auth=1

Carnitine Promotes Cancer Cell Death, Treats TRAIL-Resistant Cancer

Cancer is often treated by selectively inducing cell death—apoptosis–in tumors. However, many cancers develop resistance to this apoptosis-inducing ligand (TRAIL). Researchers are currently investigating treatments to target the TRAIL-resistant cancer cells. Will the amino acid carnitine (also called L-carnitine) become part of a new therapeutic strategy for fighting cancer?  

Researchers SJ Park, SH Park, et al, with the Graduate School of East-West Medical Science, at Kyung Hee University in South Korea, are exploring the use of carnitine as part of a combination cancer treatment.

TRAIL is a protein which kills cancer cells by causing apoptosis (programmed cell death) in tumor cells. The molecules of the TRAIL protein bind to death receptors in the cancer cells. This has been a promising anti-cancer therapy, particularly because TRAIL has no toxicity to normal cells, unlike, for example, chemotherapy.

However, many cancer cells and primary tumors are resistant to TRAIL, which means the body cannot kill the cancer cells. And some cancer cells, including highly malignant tumors, which were originally sensitive to TRAIL can become resistant after repeated exposure. Can these cancer cells become vulnerable to TRAIL again?

The researchers hoped carnitine would help. Carnitine is biosynthesized in our bodies from the essential amino acids lysine and methionine. Carnitine transports long-chain molecules, and enhances the expression of various proteins, including a protein which induces apoptosis (Bax).

Study shows carnitine makes cancer cells vulnerable, promotes cell death

The researchers tested a combination of carnitine and TRAIL in lung cancer cells, colon carcinoma cells, and breast carcinoma cells. Results showed that carnitine sensitizes TRAIL-resistant cancer cells to TRAIL proteins. The cancer is now vulnerable to the apoptosis-inducing proteins, and the cancer cells are killed.

The study concluded that combining carnitine with TRAIL reverses the resistance of cancer cells. Formulating a combined delivery method of carnitine and TRAIL could become a successful new therapeutic strategy to treat TRAIL-resistant cancer cells.

Sources:

http://www.ncbi.nlm.nih.gov/pubmed/23068102