Tag 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 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

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

Can Carnitine Help Prevent Colon Cancer?

A Canadian in vitro study investigated the effects of two nutrients on colon cancer. Would the amino acid carnitine improve the anticancer effect of a fatty acid? Results were promising.

Colon cancer, or colorectal cancer, is one of the most common cancers in the world. The risk of developing colon cancer is about 1 in 20. However, if caught early, the cancer can be cured. The 5-year survival rate for stage 1 (the earliest stage) is almost 75%.

Not all risk factors for developing colon cancer are known, though people with inflammatory bowel disease have an increased risk. People with Type 2 diabetes also have a higher risk of developing colon cancer.

Nutrition and diet are other risk factors. A diet high in red meat and processed meat increases the risk of developing colon cancer. Diets high in vegetables and fiber could reduce the risk, though studies are continually ongoing.

Researchers (M Roy, S Dionne, et al) from the University of Montreal’s Department of Nutrition (Quebec, Canada) developed a study to investigate the effect of diet and colon cancer. The study focused on butyrate and the amino acid carnitine.

Butyrate is a short-chain fatty acid, found in dietary fiber and dairy products. Butyrate has potential anticancer affects. And butyrate’s effectiveness is enhanced by carnitine. Would these two nutrients inhibit colon cancer?

Carnitine and colon cancer cells: results

Human colon cancer cells were incubated with butyrate and carnitine. The colon cancer cells were tested for proliferation–reproducing, and apoptosis—programmed cell death.

The researchers found that butyrate and carnitine acted on the cancer cells at the molecular level. Proteins which cause apoptosis were increased by the butyrate and carnitine, and the cancer cell genetic expression was decreased.

The study concluded that carnitine and butyrate do prevent colon cancer cells from spreading, and also that carnitine and butyrate cause apoptosis in colon cancer cells. This could lead to further in vivo studies, with the hope of finding new treatments for colon cancer

Sources:

http://www.ncbi.nlm.nih.gov/pubmed/19619983

Carnitine Supplements Prevent Toxicity Caused By Chemotherapy

Cancer chemotherapy is continually being refined. Many chemotherapy drugs successfully treat tumors, but they also have severe side effects. Can carnitine (L-carnitine) supplements prevent some of these side effects?

MM Sayed-Ahmed, with King Saud University’s Department of Pharmacology, College of Pharmacy, Riyadh, Saudi Arabia, reviewed the role that the amino acid carnitine has in cancer chemotherapy-induced multiple organ toxicity.

Chemotherapy has some extreme side effects, which can greatly reduce quality of life. Nausea, vomiting, and loss of appetite make the patient feel weak. Numbness and muscle and joint pain are also distressing common side effects.

Even worse, some chemotherapy can lead to life-threatening multiple organ toxicity. It’s not usually the anticancer activity of the chemotherapy drugs which cause organ toxicity, but because the chemotherapy drugs affect the absorption of other nutrients.

If carnitine cannot be absorbed and therefore used by the body, the patient develops a carnitine deficiency. And patients with cancer cachexia—the extreme wasting, muscle loss caused by the cancer—are at particular risk from carnitine deficiencies. Cancer cachexia patients are not getting enough nutrition.

Carnitine is found in red meat and dairy products. It’s also found in soybeans, wheat, and avocados. And the active form, it is readily available as a supplement.

Carnitine affects fatty acids and energy production. It also reduces blood triglycerides and cholesterol.

Carnitine depletion leads to toxicity

The anticancer chemotherapy drugs are crucially important, often the only means to treat the cancer. So preventing carnitine deficiency is a key goal. Supplementation with this amino acid, and carefully monitored levels, are necessary to reduce the toxic effects of chemotherapy. Carnitine supplementation does not affect the anticancer activities of the chemotherapy.

The review concluded that carnitine is depleted by several anticancer chemotherapy drugs, and carnitine supplementation must be considered to prevent multiple organ toxicity.

Sources:

http://www.ncbi.nlm.nih.gov/pubmed/23960728

Whey Protein: The Superfood that Slows Aging – Amino Acids and Glutathione

Lots of chatter has been going on about so-called Superfoods these days, such as spinach being packed with nutrition, when vegetables like swiss chard have far more nutrients ounce-for-ounce. Similarly, there is chatter about what is or is not a Superfood, like whey protein, since it is considered a supplement rather than a whole food. However, according to Dr. Mercola—whom has written on the “Top 7 Foods That Slow Your Aging” it is whey protein that is the exception and should be added to the list. Why? Although there are a number of reasons, amino acids plus glutathione are .

Glutathione is an antioxidant produced from other amino acids. Additionally, increasing glutathione levels through food containing those amino acids brings a host of health benefits. Whey protein is one way to do this.

Anti-aging health benefits of glutathione & amino acids from whey protein

Dr. Mercola says that whey can “increase your body’s stores of the antioxidant glutathione, or GSH.” Additionally, telomeres in your DNA are in every cell in your body, and they get shorter with age; glutathione increases the integrity of telomeres since free radicals (that cause DNA mutations) tend to damage them.

Glutathione keeps us healthy. GSH levels tend to drop in people who have oxidative stress-related health issues, such as diseases like AIDS or cancer. Patients get sicker after glutathione levels drop. Eating whey can help keep your glutathione levels up.

Glutathione supplements are NOT recommended, but precursors instead

You cannot ingest glutathione directly, however, for it is actually made inside your cells from the amino acid precursors: glycine, cystine, and glutamate. So no need to take glutathione supplements… just eat foods—like whey protein—that can help your body manufacture the antioxidant glutathione you need to fight the aging process and keep your telomeres intact.

Dr. Mercola states that biologists are now saying that lengthening telomeres actually may REVERSE aging, and a flurry of excitement is spinning around this concept in medical and research circles on antiaging methods.

Mercola states that the “best way to increase and maintain your GSH (glutathione) levels is to make sure your diet includes foods (such as animal foods and eggs) rich in the sulfur amino acids your cells need to synthesize glutathione. Whey protein is the easiest and most convenient way to do this.”

Just be sure, Mercola warns, that the whey protein you consume is not just any variety, because it needs to be “high quality and very carefully processed from grass fed organic cows to preserve the fragile amino acid precursors.”

It comes down to the quality of food that we are putting into our bodies, and ensuring that we take care of ourselves daily, in order to help reverse the aging process.

Reference:

http://articles.mercola.com/sites/articles/archive/2010/02/27/top-7-foods-that-slow-your-aging.aspx