Comment from Martin Tornberg:
“One thing that gives me pause with respect to consuming too much glycine is the study on?http://www.sciencemag.org/content/336/6084/1040.abstract‘that ?identified glycine consumption and expression of the mitochondrial glycine biosynthetic pathway as strongly correlated with rates of proliferation across cancer cells? and noted that ?Antagonizing glycine uptake and its mitochondrial biosynthesis preferentially impaired rapidly proliferating cells.
While this may be of primary concern to cancer patients (who might therefore be well advised to limit both glycine and methionine, which basically means sticking to a low protein diet), it may also be relevant for any of us who feel we might be at risk of cancer and might have small amounts of cancer cells in our bodies that are not yet large enough to form a tumor but that we don’t want to feed. The study is described in an article here:http://www.boston.com/whitecoatnotes/2012/05/24/boston-area-team-finds-cancer-cells-have-appetite-for-glycine-providing-lead-effort-halt-tumors/k6yFTmSKUeoqYtNprjjSsM/story.html.
Dr. Brind, I would naturally welcome your thoughts on this, as it implies that just eating a lot of glycine (or glycine-rich foods) to offset high methionine consumption from dairy and animal proteins may not be a wise strategy; consuming only moderate amounts of both glycine and methionine (ie, avoiding high protein diets and consuming only modest amounts of animal protein) would seem to be a safer approach (and one that is more consistent with what we know about the typical diets of very long lived people across different cultures).
On the other hand, perhaps that study on glycine was flawed or misleading, I am not sure; I am only posting it for informational and discussion purposes and would love to find out what others think about this.”
Response from Dr. Joel Brind
Thanks for this thoughtful comment, Martin. My answer will not be a short one, as this issue actually gets to the heart of my whole philosophical approach to science. The 2012 article in Science, the abstract of which you link to, by Mohit Jain et al., I am well familiar with (BTW, the second link you gave, to a popular journal article about the Jain article, no longer works). The Jain article actually follows on a 2009 article in Nature (Nature and Science are probably THE most prominent scientific journals begin published, btw), which showed a high prevalence of glycine production in human prostatic tumors, and claimed a tumor growth-promoting effect of sarcosine, the product of GNMT. There were warnings then also in some quarters about the hypothetical dangers of glycine supplementation.
Re: the Jain article, in that issue of Science, there was an editorial touting the study, and waxing philosophically about the emerging predominance of “data-driven science”, at the expense of “hypothesis-driven science”, the two studies we are discussing being examples of “data-driven science”. My view: Hypothesis-driven science is what we used to call “science”. Data-driven science starts with the mountains of data now possible to generate by new biochemical assay techniques that can simultaneously measure hundreds of metabolites, proteins, genes, etc., thus generating whole new fields of enquiry called, respectively, metabolomics, proteomics, genomics, etc. In actuality, these are not really new scientific disciplines, but advanced data mining techniques. It has become fashionable, however, to generate scientific research projects with such “-omics-generated” datasets. So, in the example you provided, Jain et al. ran such a metabolomic profile of 219 metabolic intermediates in 60 human-derived cancer cell lines developed at the US National Cancer Institute operation, to see if any particular metabolites stood out as correlating with these cancers, compared to normal cells. They found that glycine synthesis and utilization was highly correlated with these cancers, from which finding they generated the most simplistic hypothesis, namely, that too much glycine might give you cancer or make an existing cancer worse.
So you see, in this typical “data-driven” approach, the researchers start by figuratively throwing mud up against a wall to see what sticks, and then try to figure out why the mud stuck to the cancer side of the wall and not the normal side of the wall. To me, that’s not good science. (Back in the day, reviewers used to call that a “fishing expedition”, not generally worthy of grant funding. If you like fishing analogies, “data-driven science” is to “hypothesis-driven science” as trawling is to fly-fishing.)
Please don’t get me wrong: These “-omics” techniques are enormously valuable, enabling the testing of many more hypotheses much more thoroughly and quickly than ever before. But they are no substitute for good scientific reasoning.
Now let me give you my interpretation of the results obtained by Jain et al. in 2012, and those of Sreekumar et al. in 2009. It starts with an understanding of how cancer develops in the body. The prevailing wisdom (which I believe is essentially correct) is that abnormal, potentially cancerous cells develop all the time, even in healthy bodies, but a healthy immune system normally eliminates them efficiently. But when conditions?usually some form of chronic inflammation?makes cells multiply abnormally quickly, mutations develop at a much higher rate. The abnormal cells which result ultimately develop such mutations as to breed independently of normal cell growth control mechanisms, and they may overrun the immune defenses and become a dangerous, invasive tumor. During this process, a Darwinian natural selection process selects those cells which are most able to grow, escape immune surveillance, and invade other tissues; thus exploiting the weaknesses of the immune system and the body’s internal environment as a whole. (I know we are used to thinking of natural selection as occurring over eons, rather than months and years, but when we are talking about individual cells, whose generations are measured in hours instead of years, evolution is very quick.)
Now let’s take a look at some well established findings re: human cancer. Many human cancersuperhaps a majority?are actually much more methionine-dependent than normal cells. They have lost the ability to recycle and regenerate and salvage methionine. In fact the use of the bacteria-derived enzyme methioninase, to help deny methionine to cancer cells in afflicted patients, is an active and somewhat fruitful area of cancer research and therapy. Now let’s refer back to the metabolic pathways, and the intimate relationship of methionine and glycine metabolism. The easiest way for a cell to waste methionine is to override the “off switch” to THE methionine-wasting enzyme, GNMT (glycine-N-methyltransferase). Why would a cell do this? It will do this if there is a selective advantage to avoid the energy expenditure of conserving and recycling methionine. Under what circumstances would this be advantageous? It would be advantageous in an environment that is chronically methionine loaded. Of course, when GNMT is always active, the synthesis of glycine is always maximal also, so there will be lots of glycine produced (as well as sarcosine, the product of GNMT.) So then, what did the metabolomics people?Sreekumar in 2009 and Jain in 2012?actually find? They really just found the flip side of the increased methionine-dependence of many human cancers, i.e., the increased glycine-independence of many human cancers.
So my interpretation of these results is that they offer hard evidence that many human cancers are selected for, and therefore arise in, bodies which are chronically methionine-loaded and glycine-deficient. Thus, they underscore the need for the proper balance between glycine and methionine. As far as diet is concerned, all that means is that the high intake of methionine in muscle meats needs to be balance with a proportionally high intake of glycine, which we usually throw away with the collagen of the bones and connective tissues. If you don’t care for bone broth or gelatin, just a glycine supplement will do the trick.
About the Author
Joel Brind, Ph.D. has been a Professor of Biology and Endocrinology at Baruch College of the City University of New York for 28 years and a medical research biochemist since 1981. Long specializing in steroid biosynthesis and metabolism and endocrine-related cancers, he has specialized in amino acid metabolism in recent years, particularly in relation to glycine and one-carbon metabolism. In 2010 he founded Natural Food Science, LLC to make and market glycine supplement products via http://sweetamine.com , which includes his own blog HERE.
Thanks for elaborating on that.
What went through my mind when I was reading this was the raw vegan low protein diets that tend to temporarily stop cancer from progressing. (The diet advocated at Hippocrates Health Institute for example). Many people who attend the clinic there experience a temporary slowing of their cancer that almost seems like it is going away entirely. (Which is why these places give people so much hope only to disappoint greatly in the end in most cases)
It must have something to do with methionine and the lack of it in a diet that is all vegetables and fruit.
Thanks Dr. Brind…..I am not sure if I follow what you are saying 100% or what the implications are, but if I am understanding you correctly, it seems to me that you are basically saying that the nature of cancer cells is that they synthesize their own glycine (and presumably therefore also consume that glycine), so your interpretation of the study is that it simply confirms this theory, but that it does NOT mean that we should not eat glycine….
Your overall cancer theory, if I am extrapolating correctly from what you wrote, seems to be that cancer develops & thrives in an environment in which there is chronic excess methionine and not enough glycine, and in such an environment, cells produce more GNMT (glycine-N-methyltransferase), the enzyme that breaks down methionine, and “when GNMT is always active, the synthesis of glycine is always maximal also, so there will be lots of glycine produced.”
So you seem to be implying that the cancer cells consume glycine because they are producing it, and they are producing it because they have a lot of GNMT, and they have a lot of GNMT because over time, historically, they’ve gotten too much methionine and too little glycine. Therefore, to prevent this over-expression (excess) of GNMT from happening in the first place, we need to:
1) avoid chronic consumption of methionine – presumably by eating a diet that is not high in methionine to begin with, but perhaps also by fasting periodically to bring down the body’s methionine levels(?), and
2) consume enough glycine, which may help to prevent the formation of too much GNMT – you did not say this explicitly, but I am guessing you might believe this based on what you wrote(?).
In any event, I have a related question which perhaps you could answer briefly here but that I imagine might be a topic of future articles for you and Matt (and you may already have some that I have missed, so feel free to post links to them here). The question is how do we go about strengthening the immune system so that it can fight off the cancer cells better to begin with? What sorts of diets, foods, supplements, or other health practices strengthen the immune system?
I think the greatest immune system enhancer is a high metabolic rate/high body temperature. Of course, this tends to fall with age at which point nearly all degenerative diseases become more likely. But with a higher metabolic rate you’ll see higher immune cell counts, greater enzyme activity, and basically everything that a fever does but on an ongoing 24-7 basis and without negative symptoms. And of course, the metabolic rate is influenced by countless factors, amino acids and inflammation being but two examples.
Now I’m not sure I follow your reasoning! So let me try to clarify my own thinking. In fact, my theory on the development of cancer is not original; as I noted, it is really quite a mainstream view in the cancer research field. In any body in which a cancer arises, the renegade cells–having mutated in an environment characterized by being stimulated to divide repetitively due to chronic cellular damage, as happens in a chronic inflammatory environment, and now operating as completely separate organisms with different genetics than the host’s own body–undergo selection pressure based on the immunological and biochemical environment in which they develop. The “fittest” that survive to grow into dangerous tumors are therefore the ones best adapted to that environment. If the environment is methionine-loaded and glycine-deficient (really two sides of the same coin), the successful tumor cell clone will not likely be one that wastes metabolic energy maintaining the metabolic pathways that regenerate and recycle methionine. Rather, they will be the cells that waste methionine (since there’s always plenty around). On the other hand, with the environment being chronically glycine-poor, they will be cells that can maximally produce glycine. The easiest way to arrive at this metabolic plan is to have GNMT unregulated, ie. not responsive to the shut-off signal of MeTHF. This could be accomplished by a mutant GNMT that does not respond to the shut-off signal of MeTHF, or even simply by the lack of MeTHF, because MTHFR–the enzyme that makes it, as part of the methionine recharge pathway-may not be operational. It need not have to do with the actual amount of GNMT around. In fact, different tumors that arise likely get to this point in different ways. The point is, the “successful” tumor cell clone is maximally efficient in thriving in an environment in which methionine is abundant and glycine is rare. The very finding that so many human cancers behave this way is evidence–in my view–that the common condition which breeds cancer is indeed methionine-loaded and glycine-poor.
Now you might say that this does not quite add up, as the increased activity of GNMT will use up all the glycine being made. However, if you look at the product of GNMT–sarcosine–it can be turned back into glycine and the tumor cells may be selected to optimize this pathway. (This was one of the arguments of the Sreekumar paper on prostate cancer in 2009 that I referred to. They actually demonstrated higher quantities of glycine and sarcosine generated by prostatic cancers.)
Now, on to glycine and methionine utilization: Both these amino acids are critically needed to make both proteins and DNA: The actual synthesis of the purine DNA bases adenine and guanine uses the glycine molecule as a building block; and the methylation of DNA bases requires methionine. Methionine is also required for the initiation of the synthesis of all proteins, as well for the synthesis of polyamines, which are critical molecules is the actual structure of the chromosomes. Therefore, the idea that glycine and methionine are preferentially utilized by the most rapidly proliferating cells, and that conversely, drugs which inhibit such utilization are most effective in impairing such rapid proliferation, is really a no-brainer.
Now of course the bottom line is what all of this means in a situation in which a cancer has already developed. The use of chemotherapy is always a balancing act between damaging the cancer cells and damaging normal cells. Typically, chemotherapeutic drugs are antimetabolites which preferentially target rapidly dividing cells. Hence, during a course of chemotherapy in which glycine is antagonized, glycine supplementation may be counterproductive. However, during periods of remission (or cure: It’s often hard to tell the difference), I cannot see any reason not to maintain a healthy balance of methionine and glycine. If the diet is typically one which has too much methionine and not enough glycine, that should be corrected. It seems most reasonable to me that cancers would be less likely to recur in a healthy environment–especially for the immune system–with adequate glycine to guard against a state of chronic inflammation.
I have gone on rather long, but I think I managed to address both your questions and those of hazmatt below.
By the way, as an additional follow-up, I did find 3 studies showing that glycine does inhibit tumor growth:
1) https://www.landesbioscience.com/journals/cbt/amin2-2.pdf – “Dietary Glycine Inhibits Angiogenesis During Wound Healing and Tumor Growth” (This would seem to imply that maybe it is best NOT to supplement too much glycine during wound healing.)
2) http://carcin.oxfordjournals.org/content/20/11/2075.short – “Dietary glycine prevents the development of liver tumors caused by the peroxisome proliferator WY-14,643”
3) http://carcin.oxfordjournals.org/content/20/5/793.short – “Dietary glycine inhibits the growth of B16 melanoma tumors in mice”
What does this imply for those with MTHFR mutations?
Probably nothing. As I suggested in my comments after my previous post, the slightly reduced ability of the common MTHFR variants I would not expect to matter, as methionine is usually so overabundant. The popular concern over such the possible negative consequences of such mutations is overblown, in my view, to say the least. It is rooted in the idea that “undermethylation” is the problem underlying many cancers and other chronic illnesses, whereas the opposite is really the widespread problem. It is also worth noting from an evolutionary point of view, that the high prevalence of such of MTHFR mutations in human populations worldwide is testimony to their general lack of ill effect on human health.
You responded! That is so cool! :) So- if I eat a lot of muscle meats (I do) largely from beef and sometimes chicken, does that need to be balanced with glycine and if so can I just eat a ton of gelatin with the meats? Do you think eating the broth from the chicken with the chicken would balance it out, (kindof like the vitamin e present in walnuts seems intrinsically paired with the PUFAs there) or do you think more glycine supplementation via a straight source would be better to balance?
If you like the natural foods that balance out all the excess methionine–like gelatin and bone broth–go for it! But just make sure that you eat the balanced protein every day, and 8 grams is pretty substantial. That’s how much glycine I put in each serving of sweetamine, and that’s the equivalent of about 16 4-oz. servings of Jell-o.
Another recent study that shows higher concentrations of glycine inhibited cancer cell proliferation.
http://www.cell.com/cell-reports/abstract/S2211-1247(14)00347-7
Thanks for the references to studies that show glycine inhibiting tumor growth, Martin. Re: the last one on this list of papers, the B16 melanoma line is a routine transplantable tumor in mice that a number of my colleagues have worked with for years. One of them has repeated the published evidence you cite, i.e., he was absolutely unable to get B16 melanomas to grow in glycine-supplemented mice.
That leads me to another important point in regard to the work of Jain et al. (and others), who tend to scare off the public re: glycine supplementation with studies on cultured cell lines derived from human cancers. Not only are these tumor cells removed from the original scene of the crime (a human body) and grown under artificial conditions, but the artificial conditions are even more methionine-loaded and glycine-deficient than the human bodies which harbored their genesis in the first place!
Specifically, Jain et al. maintained and tested these cells in a typical tissue culture medium (called RPMI 1640), which contains methionine at levels 3-6 times higher than normal human blood plasma (RPMI = 100 micromolar; normal human plasma: 16-30 micromolar) and glycine levels below the (glycine-deficient, I maintain) normal range (RPMI = 133 micromolar; normal human plasma: 170 – 330 micromolar.
Of course, you may reasonably ask why they do this, and the answer is quite simple: The tissue culture conditions established for growing cancer cells in vitro is optimized for the growth of cancer cells! Therefore, all the experiments done on these cultured cells reinforce the ignorance of these conditions which actually breed cancer, i.e., too much methionine and not enough glycine.
This also brings up the question that Sarah posted on October 1 about glycine supplementation in the presence of active cancer. I can only say that the best environment to stop cancer from growing would be a healthy environment that is not glycine-deficient and methionine-loaded. True, I am not a medical doctor and would give no medical advice, but remember that glycine supplementation is not a drug strategy in any way: The only point in taking supplemental glycine is to make up what is missing from the typical (omnivorous but bone and cartilage-free) diet we consume nowadays.
So are you saying that cancer cells specifically use more glycine because they have adapted to eliminating more methionine, or that all cells in a cancer-prone individual have probably adapted to eliminating more methionine because cancer prone individuals have too much?
“Antagonizing glycine uptake and its mitochondrial biosynthesis preferentially impaired rapidly proliferating cells.”
Also, what does the above quote mean to you?
While your above explanation makes sense of this:
“This analysis identified glycine consumption and expression of the mitochondrial glycine biosynthetic pathway as strongly correlated with rates of proliferation across cancer cells.”
Sort of…
It doesn’t make sense of this:
?Antagonizing glycine uptake and its mitochondrial biosynthesis preferentially impaired rapidly proliferating cells.
I’m quite familiar with the Jain paper, but not so familiar that I can put the quotes in context by heart! Please cite the pages from which those quotes are taken, so I can put them in context and give you an intelligent answer.
http://m.sciencemag.org/content/336/6084/1040.abstract
I see, you don’t have the full paper. However, I think I addressed your questions adequately in my looooong response to Martin Tornberg, above.
Yea man, you don’t have to answer my question, just looking for clarification. The question I had was taken from the abstract, which I linked to and the person who originally asked the question about cancer linked to.
Never mind, I think you adequately answered it here:
“Therefore, the idea that glycine and methionine are preferentially utilized by the most rapidly proliferating cells, and that conversely, drugs which inhibit such utilization are most effective in impairing such rapid proliferation, is really a no-brainer.
Now of course the bottom line is what all of this means in a situation in which a cancer has already developed.”
Joel – I have a general question about glycine. Is there any benefit in taking glycine several times per day with meals that contain methionine (such as beef, lamb etc) or does just one dose in the morning have the same benefits? Thanks.
In my experience it does not matter, because after 2 or 3 days (of taking 8 grams per day, once in the morning), the blood levels of glycine reach a fairly steady state. You can always experiment to see what works best for you.
Thanks Dr.
I just found out today that (another) friend has cancer. It is bladder cancer. I have not found out what exact type of cancer it is yet.
I know that you are not a medical doctor but can you comment on the usage of glycine in someone who already has an active cancer?
Are their particular kinds of cancer (adenocarcinoma’s for example) that glycine therapy would have the potential to work better for?
Sarah, please see my long comment from yesterday, when I addressed this issue. Essentially, I do not advocate “glycine therapy”, because glycine is not medicine; just food. The whole point of glycine supplementation is complete one’s nutrition by adding back the glycine that is usually missing from the typical omnivorous but bone and cartilage-free diet. Whether one has an active cancer or not, it’s always good to have balanced nutrition, unless of course, one’s doctor prescribes a particular nutritional program to accompany a treatment program.
I just began adding gelatin to my morning coffee (the Great Lakes powdered beef sourced kind), and I notice that I tend to feel tight in the chest and I get more mucous. Do you think I am having a histamine reaction to it? I know gelatin is relatively high in histamine. Does this hurt me at all to supplement with it, and will the reaction eventually go away?
Gelatin actually has no histamine in it–you might be thinking of the amino acid histidine. Your body, however, will generate histamine if you are having an allergic reaction, which is certainly possible. (I commented after my last post re: beef and pork collagen allergies not being rare, especially among those who may have had collagen injections for cosmetic purposes.) If you are having an allergic reaction, it will get worse with continued consumption–not better. The good news is that Great Lakes also sells hydrolyzed collagen, so even if you are allergic to the whole collagen, the hydrolyzed kind, having had the allergenic protein structure destroyed, will give you the same benefit without the allergenicity.
Elsewhere on the web, there are many sites that say that gelatin from slow-cooked bone broth is very high in histamine. It’s the slow-cooking that causes the increase in histamine, at least that’s what they say.
Do you disagree with this?
This doesn’t have to do with the article, but I was wondering why I can’t find 180 diabetes anywhere. I would love to read the book, my husband has just been diagnosed with diabetes.
Thought I should mention, I wouldn’t just “love” to read the book, I feel a true necessity to read since my husband’s diagnosis! I have email Dr. Garrett Smith.
I hope to one day resurrect that book after it has been revised. Maybe next year. What was the diagnosis based on? A high fasting glucose test? I would start by getting a glucose meter and monitor fasting and postmeal glucose levels to establish a baseline and see what’s really going on.
Type 2 diabetes is one of those common conditions now known to result from “metabolic inflammation”. In fact, there was a clinical trial published in 2008 that showed improvement among diabetics with glycine supplementation. http://www.ncbi.nlm.nih.gov/pubmed'term=(Cruz%20M%5BAuthor%20-%20First%5D)%20AND%20glycine%5BTitle%5D
Here in Argentina it may be different how they measure it but it was because of high fasting blood glucose: 424mg, the reference value should be between 70 and 110mg. And the glucose in his urine was 37,8g/lt. He was also showing all the symptoms of diabetes: fatigue, excessive thirst so consequently frequent urination, numb finger tips, temporary loss of vision (only once or twice), REALLY rapid weight loss, loss of appetite. Of course they recommended???.LOW CARB!!!! Lucky him I screamed NOOOOOO, and said if anything will lower the fat in your diet and replace it with carbs. I will see where I can get a glucose meter. Any recommendations would be helpful, I know you’ve worked with diabetes patients.
Wow. That’s really REALLY high. To the point that suggests that he might be producing insufficient insulin.
Yes! I know, I’m actually scared out of my wits, afraid he is going to die of a stroke or heart attack at any moment. I wish there was something we could do that is an alternative to insulin injections and low carb, he really wants some sort of alternative and eventually to be able to live a more or less normal lifestyle.
If he’s not producing adequate insulin, he should probably be on it. That doesn’t mean his diet should be low-carb though.
I’m not vegan, but are there any non- gelatin sources of glycine? I think scallops are fareky high in glycine? But gelatin in jelly or bone broth seem to be the most sited sources of glycine. Any other food stuffs? Thanks in advance!
As far as I know, the richest natural source of glycine is silk, which actually has twice as much glycine as gelatin. However, I don’t think silk is too digestible. But if there is a richer source, I’ll eat my tie! Seriously, vegetable proteins are generally more glycine-rich and methionine poor than animal proteins.
So does that mean beans or legumes are more glycine rich and methionine poor?
Not necessarily: Soy and most other legumes, yes; lima beans, no. Also, mushrooms are high in methionine. Other legumes are generally OK.
Wanted to mention that I noticed on http://nutritiondata.self.com/facts/cereal-grains-and-pasta/5676/2 that amaranth has about the best glycine to methionine ratio of anything but gelatin.
I developed knee pain a couple of years ago and have been taking MSM daily which seems to have helped significantly. Now I’m reading about the dangers of excess methionine and have begun supplementing with glycine. And now that I am paying attention to methionine I see that MSM is touted to ensure you are getting enough methionine. If the mechanism whereby MSM works is by increasing methionine, I’m obviously fighting that with the glycine. On the other hand, if the increase in methionine is simply a byproduct of taking MSM, glycine could be having a protective effect while still allowing for the benefits of MSM. Any thoughts on this combination? Thanks much!
Funny you should mention MSM, Geoff, as I’ve been taking MSM as well for a couple of years now! Long before I discovered the methionine/glycine connection, I had developed pain in one knee, and started taking a glucosamine/chondroitin supplement. In a few weeks, the pain went away, so I have kept taking it. More recently (about a year ago), I changed to glucosamine/chondroitin supplement that also has MSM. It hasn’t hurt me in any way, so I still take it. However, MSM cannot replace methionine, as it is a very far downstream metabolite, like taurine (which I also include in my sweetamine supplement). The problem with excess methionine is the excess methylation capacity, which requires glycine to get rid of. So, no worries about taking MSM, but pay not attention to the fad of keeping methylation capacity up: Almost all of us have more than enough of that!
My take on ScienceMag is that it’s Big Pharma owned. Check out the board members of the AAAS (ScienceMag is the official mag for that group)… all the bios I peeked at were pharma-related. Not actual scientists. Just sayin.
Would you be able to help me understand the role and relationship of the mineral sulphur? This is another mineral said to be extremely important for glutathione production. I’m trying to understand if there is a negative effect of having excessive sulphur, whether from supplementation or eating tons of brassica.
You explained that consuming tons of methionine supplements in hope of increasing glutathione was akin to smoking to cure anemia. I’m wondering if consuming copious amounts of sulpher could also be detrimental?
Hi Dr. Brind,
Firstly i would like to thank you for posting so much scientifically backed detail information on collagen, and the general deficiency in dietary glycine.
My question deviates a bit from Glycine/Methionine balance. It is about Glycine itself.
My partner just finished a tough year with radiation surgery and chemotherapy for Colorectal cancer. He is currently ‘all clear’. But chemo has left a very frustrating side-effect: peripheral neuropathy. It got worseafter he finished his 12 course chemo. It is now about 9 weeks after his last session and he has tingling and numbness in his feet all the way above his knee, and in both his hands numbness. Oncologist says in most people it goes away, but some its permanent.
Glycine is an inhibitory neurotransmitter. Can you explain what that would mean and if it may help reverse/mitigate his neuropathy. Would Glycine help this do you think?
Thank you.
Is high glycine indicative of cancer? My glycine is over 500 with a top range of 325. I also have 4 other amino acids that are slightly elevated. I can’t seem to find any doctor who knows how to interpret my results and I’ve talked to many, including an endocrinologist.
Thanks!
Hi, I would like to enquire as to whether the logic of the safety of glycine supplementation also applies to sarcosine? As there is concern in certain circles that supplementing with sarcosine will increase the risk of prostate cancer or increase the growth or metastasis of existing cancer
Thanks for your help
Regards
Peter Rooks
Peter, this website is dead. The last comments were posted 2-3 years ago. Hopefully you can find an answer on a more reliable and updated site.
I have opted to treat my advanced prostate cancer as holisticaly as possible. As such I am now 100 % plant based diet wise and religiously practising intermittent fasting. ….only intake food 12 to 8 pm.
Obviously “bought in” to methionine feeds cancer. Key supplements are high dose melatonin,beta glucan,45 mg. Vit. K2, Mod. Citrus Pectin and IP6.
High Intensity Exercise every other day.
Have mers to bone upon diagnosis but after carefully reviewing treatments (probably foolishly) have decided to go this alone and let cards fall where they may. Always thought no cancer for me with strict attention to my health (now age 73). Thought I was doing the right things but learned too late that avoiding red meat didnt hold down my high methionine diet of strictly fish and chicken even though heavy on cruciferous and lots of other healthy vegetables. So, with that basic history and my desire to “starve” my methionine dependant cancer I am here for guidance from the msny wiser than me minds I have begun to follow. Please, any comments and my major question …. is, as I believe, glycine something that will help me based on my brief history presented since I am 100 % committed to feeling that cancer can be slowed or stopped by proper diet and exercise. Craig
Glycine is used to get rid of excess methionine. The key term here I think is excess. If you have a very low methionine diet then glycine should not make much of a difference but for those of us eating more methionine then glycine can help clear it out. That is at least my understanding of it.