21 replies to this topic

[Sith]

Greetings everyone, 

 

I was wondering whether hydrolysed collagen would be a more life extension compatible protein. My reasoning for this is that hydrolysed collagen is deficient in Methionine and Tryptophan and is higher in glycine and proline. 
 

So, would hydrolysed collagen still carry the health implications of other protein sources? Can it be compatible with life extension? 

 

Before some of you say low-protein does not equate to life extension, please do your research. Thanks. 

[Oakman]

I'm guessing you'd need to do an N=1 study to find out. Here they don't think much of it for anything other than hair, nails, and skin,...

 

"Supplement companies selling hydrolyzed collagen will tout it’s remarkable health benefits.  These benefits mainly include hair and nail support and joint benefits.  Numerous studies support the benefits of hydrolyzed collagen for hair, nails, and joints, however, I believe these benefits do not out weight the negative effects hydrolyzed collagen has on protein utilization.  What good is nice hair and nails, when you have zero muscle mass and look like skinny, malnourished, person? You’ll notice that these websites that promote hydrolyzed collagen as a good, healthy product, never mention that it has a biological value and PDCAA of ZERO and may decrease the efficiency of other high-quality proteins.  You’ll also never see them tell you that it comes from pig skins as well."

 

That may be a bit overstating the case, I say. My daily dose of Hydrolyzed Collagen I take is less than 5 grams. Is that going to dilute my other protein intake THAT much? Unlikely. So to answer your question, I don't think I'd want to live exclusively on HC, but as an additon for skin, hair, etc., I don't have a problem with it. 

[Heisok]

I think they are presenting a scare angle by the snarky pig comment. , even if some of their positions might be true. Little do they really know, Hydrolyzed Collagen is also made from, Bovine (cattle group) , Chicken and Marine sources. (They surely know this though.  

 

I do not know about Life Extension, but I do not doubt that there are other benefits.

 

My N=1 for Collagen Peptides is related to knee pain which was from banging my knee very hard against a wall. It was around the inner, upper outside the actual joint. The pain improved very little, and after about 6 weeks, I wondered if I was stuck with it. I started taking a Collagen Peptide for other reasons (possible stomach lining benefits, and as a possible prebiotic.)  Did not even consider the knee pain. Within a few weeks, I realized the pain was almost completely gone with no limitations to it's use. I still take from about 5 to 18 grams per day depending on the amount of gelatin produced from cooking whatever protein source I am eating. If it has a lot of cartlidge, I get a lot. If it is mostly muscle and fat, I add more collagen.  

 

 

A source of information, and the author seems to provide plenty of references:  https://fixyourgut.c...as-a-prebiotic/

 

 

This is what was posted by Aconita in another thread. "

"Molecular weight is the main factor in hydrolyzed collagen, when it is too high it dissolves poorly tending to form clumps and taste is kind of well detectable, in the other hand when the molecular weight is low enough it ready dissolves in water and there is virtually no taste. When the latter is experienced you know the product is good at least.:

Edited by Heisok, 18 June 2017 - 06:05 PM.

[brosci]

Fwiw, I've found this brand to have the mildest taste of the hydrolyzed gelatin's I've tried so far.

 

https://naturalforce...lagen-peptides/

 

I've tried the Vital Proteins brand (including their marine peptides), Bulletproof brand, and Great Lakes.  It seems like there's bound to be some crossover in sourcing materials for these different companies.

[Sith]

Thanks for all the answers, but I think I may have given the wrong impression. My question was whether hydrolysed collagen was obstructive towards longevity? 

 

My reasoning for this is the higher dietary protein intake due to supplementing with hydrolysed collagen. Would this still increase mTOR despite being deficient in leucine and other BCAAs? And would it impact on longevity, given that Methionine and Tryptophan are absent?

[brosci]

Thanks for all the answers, but I think I may have given the wrong impression. My question was whether hydrolysed collagen was obstructive towards longevity? 

 

My reasoning for this is the higher dietary protein intake due to supplementing with hydrolysed collagen. Would this still increase mTOR despite being deficient in leucine and other BCAAs? And would it impact on longevity, given that Methionine and Tryptophan are absent?

From what I understand, the benefits of restricting methionine / tryptophan is largely from the reduction in IGF1 rather than mTOR (which is only briefly raised in skeletal muscle following post-workout amino acid consumption?)  Interestingly, muscle mass + strength is a large predictor of longevity (with particularly increased odds of experiencing "extreme longevity.")

 

https://www.ncbi.nlm...les/PMC3337929/

https://www.ncbi.nlm...les/PMC4035379/

https://www.ncbi.nlm...pubmed/26791164

etc.

 

Also relevant:

)

 

In this article, glycine was mentioned to increase lifespan of animal models, where your best source of glycine would be hydrolyzed collagen:

http://www.fasebj.or...upplement/528.2

 

I believe this is largely the mechanism:

https://www.westonap...-good-and-evil/

 

"When the supply of methionine exceeds that needed for methylation, the excess is metabolized mainly in the liver and the pathways shown in panel B predominate. Glycine accepts the extra methyl groups, while choline and betaine recycle part of the extra homocysteine. These processes all result in the accumulation of dimethylglycine, part of which is lost in the urine.6 Vitamin B6 and glycine assist in the conversion of part of the extra homocysteine to cysteine and then to glutathione, which is the master antioxidant and detoxifier of the cell, and a key regulator of protein function. When the flux through this latter pathway exceeds the capacity for glutathione synthesis, the excess cysteine is converted to taurine and sulfate. Thus, B vitamins, choline, betaine and glycine all cooperate with methionine to allow optimal methylation and synthesis of glutathione. When methionine is provided in the absence of these partners, methylation and glutathione synthesis fall by the wayside and homocysteine accumulates to potentially toxic levels. It may also be the case that if only glycine is limiting, the capacity to absorb extra methyl groups diminishes and rogue methylations occur."

 

The author of that paper posted a recent article:

https://chrismasterj...athione-status/

 

"I would experiment with up to 10 to 20 grams of collagen if you have a reason to believe that glycine could be limiting for you, but that’s just a best guess."

 

He goes on to mention:

 

"If you have an MTHFR polymorphism that decreases MTHFR activity, you are likely to be wasting excess glycine into the urine, and you may be a good candidate for someone who could benefit from more glycine in the diet beyond what you would usually get."

 

The last time I checked my blood labs while supplementing gelatin and BCAAs, my IGF1 was 76 ng/mL (low, but ideal) and homocysteine was 7.4 umol/L (low, but ideal.)  I have the ++ C677T MTHFR polymorphism.  Ymmv.

Edited by brosci, 19 June 2017 - 12:57 AM.

[Sith]

 

Thanks for all the answers, but I think I may have given the wrong impression. My question was whether hydrolysed collagen was obstructive towards longevity? 

 

My reasoning for this is the higher dietary protein intake due to supplementing with hydrolysed collagen. Would this still increase mTOR despite being deficient in leucine and other BCAAs? And would it impact on longevity, given that Methionine and Tryptophan are absent?

From what I understand, the benefits of restricting methionine / tryptophan is largely from the reduction in IGF1 rather than mTOR (which is only briefly raised in skeletal muscle following post-workout amino acid consumption?)  Interestingly, muscle mass + strength is a large predictor of longevity (with particularly increased odds of experiencing "extreme longevity.")

 

https://www.ncbi.nlm...les/PMC3337929/

https://www.ncbi.nlm...les/PMC4035379/

https://www.ncbi.nlm...pubmed/26791164

etc.

 

Also relevant:

)

 

In this article, glycine was mentioned to increase lifespan of animal models, where your best source of glycine would be hydrolyzed collagen:

http://www.fasebj.or...upplement/528.2

 

I believe this is largely the mechanism:

https://www.westonap...-good-and-evil/

 

"When the supply of methionine exceeds that needed for methylation, the excess is metabolized mainly in the liver and the pathways shown in panel B predominate. Glycine accepts the extra methyl groups, while choline and betaine recycle part of the extra homocysteine. These processes all result in the accumulation of dimethylglycine, part of which is lost in the urine.6 Vitamin B6 and glycine assist in the conversion of part of the extra homocysteine to cysteine and then to glutathione, which is the master antioxidant and detoxifier of the cell, and a key regulator of protein function. When the flux through this latter pathway exceeds the capacity for glutathione synthesis, the excess cysteine is converted to taurine and sulfate. Thus, B vitamins, choline, betaine and glycine all cooperate with methionine to allow optimal methylation and synthesis of glutathione. When methionine is provided in the absence of these partners, methylation and glutathione synthesis fall by the wayside and homocysteine accumulates to potentially toxic levels. It may also be the case that if only glycine is limiting, the capacity to absorb extra methyl groups diminishes and rogue methylations occur."

 

The author of that paper posted a recent article:

https://chrismasterj...athione-status/

 

"I would experiment with up to 10 to 20 grams of collagen if you have a reason to believe that glycine could be limiting for you, but that’s just a best guess."

 

He goes on to mention:

 

"If you have an MTHFR polymorphism that decreases MTHFR activity, you are likely to be wasting excess glycine into the urine, and you may be a good candidate for someone who could benefit from more glycine in the diet beyond what you would usually get."

 

The last time I checked my blood labs while supplementing gelatin and BCAAs, my IGF1 was 76 ng/mL (low, but ideal) and homocysteine was 7.4 umol/L (low, but ideal.)  I have the ++ C677T MTHFR polymorphism.  Ymmv.

 

 

Thanks! This is great information. I have always been confused between protein consumption and individual amino acid consumption and which is more important to general longevity. I guess the question is still up in the air mostly.

[Sith]

Any more opinions? 

[GoingPrimal]

I try to take a source of glycine daily, to try to even out my protein consumption. Most muscle meats are high in methionine and lacking in glycine, so I try to consume some source of glycine. I regularly take betaine (trimethylglycine) for weight lifting purposes and liver detoxification, and usually take about 6 grams of hydrolyzed collagen, though I feel that homemade bone broth is best.

 

I do believe we over-consume methionine and under-consume glycine, and that balancing these out is beneficial to longevity.

[floweryriddle]

Pushing this thread a last time. I also recently started taking Hydrolysed Collagen and am very interested in this as well. 

This is the product I started taking based on recommendations: https://www.amazon.c...rds=great lakes

 

@GoingPrimal from which particular sources are you consuming glycine? 

[Nate-2004]

"Supplement companies selling hydrolyzed collagen will tout it’s remarkable health benefits.  These benefits mainly include hair and nail support and joint benefits.  Numerous studies support the benefits of hydrolyzed collagen for hair, nails, and joints, however, I believe these benefits do not out weight the negative effects hydrolyzed collagen has on protein utilization.  What good is nice hair and nails, when you have zero muscle mass and look like skinny, malnourished, person? You’ll notice that these websites that promote hydrolyzed collagen as a good, healthy product, never mention that it has a biological value and PDCAA of ZERO and may decrease the efficiency of other high-quality proteins.  You’ll also never see them tell you that it comes from pig skins as well."

 

That's a very thoughtless statement that assumes you're not getting your protein from any other source.

 

Disclaimer: I'll say up front that I don't have any references for this because there are none, it's just purely hypothesis based on my experience and based on what Aconita (a user on this board) has stated regarding his own opinion about it. I believe he linked some research.

 

In my own experience I've only noticed positive benefits from hydrolyzed collagen based on timing. I think it is more important when you take it and not so important that you take it. For one thing it bonds easily with other types of protein that aren't included so it is best taken on an empty stomach 30 mins before a meal and I believe hypothetically, that the best time to do that is in the days following an extended fast in conjunction with a 16/8 intermittent fasting routine. So I would break a 36 hr fast with it, then each day of 16/8 break the fast with the collagen, wait 30 mins to an hour, then re-feed with whatever you want, preferably good fats, protein and an excellent smoothie containing blueberries (these lower the spike in blood sugar he has other videos demonstrating this with science). 

 

All this in addition to maybe some topical forms of assistance with collagen production only during the time restricted feeds are also a good idea. By the way on that link I'd keep anything with vitamin c to a post workout period. So after you shower, with a wet face, put the matrixyl 3000 formulation on your face.  I've yet to figure out how to time it right with the hydrolyzed collagen though.  Matrixyl 3000 adds the peptides to your face that is common to damaged collagen, your body responds to these peptides by trying to make more. If you're well supplied with the materials to make it, it should all work out in a net positive way. The reason I suggest fasting or extended is for the autophagy which affects skin as well.  You also get a surge in growth hormone with a drop in IGF-1. This just makes for a more ripe environment to get best results I think. Again, this is all just hypothesis, sorry no real references other than the above. Search Aconita's posts on skin and collagen I think he has links.

 

I'm still getting used to 36 hour fasts twice a week and lately the refeed days have been a little calorie heavy but I've only lost fat % and maintained my muscle which is great. My skin so far as I can tell looks better than ever. I wouldn't keep putting myself through this fasting thing if I didn't think it helped my skin and didn't have the potential to help with my essential tremor given the boost in BDNF.

 

Longevity is another matter entirely and I would probably say that using hydrolyzed collagen as a primary protein source is ill advised. That said, you could cycle it in as a primary source on some days. I don't think you need that much protein every day. If you stuck with just veggies, fruits and unsaturated fats and took the hydrolyzed collagen on just one or two days of the week you'd be fine. It's more of a timing issue in my opinion. You could get the benefits just by cycling it with other protein sources at different points in the day or different points in the week.

Edited by Nate-2004, 27 June 2017 - 03:09 PM.

[Oakman]

 

"Supplement companies selling hydrolyzed collagen will tout it’s remarkable health benefits.  These benefits mainly include hair and nail support and joint benefits.  Numerous studies support the benefits of hydrolyzed collagen for hair, nails, and joints, however, I believe these benefits do not out weight the negative effects hydrolyzed collagen has on protein utilization.  What good is nice hair and nails, when you have zero muscle mass and look like skinny, malnourished, person? You’ll notice that these websites that promote hydrolyzed collagen as a good, healthy product, never mention that it has a biological value and PDCAA of ZERO and may decrease the efficiency of other high-quality proteins.  You’ll also never see them tell you that it comes from pig skins as well."

 

That's a very thoughtless statement that assumes you're not getting your protein from any other source.

 

....

 

Just for the record, I didn't say this!  > They did.

[Nate-2004]

 

 

 

 

 

....

Just for the record, I didn't say this!  > They did.

 

 

Haha I know. I tried to edit my response to clarify that.

 

Also just more to add on the mTOR angle. A lot of the fasting thing is about mTOR and autophagy, so the original poster was curious about specific types of protein like tryptophan and methionine. I've often been curious about mTOR activation with hydrolyzed collagen which contains glycine and hydroxyproline and other aminos and peptides. I don't know if these activate mTOR or not. For the longest time I've thought that given how glycine improves sleep quality (so does fasting), and given that your body sort of regenerates during high quality sleep, that taking the collagen right before bed was optimal. I still would try that as well on some nights, but not every night, just to see. I think it's more important to get it in there without other forms of protein than anything else. That's when it's most likely going to get to where it needs to be. That said, not sure where the research is on that. 

[Oakman]

I like how you think nate! Your thoughts show some well integrated hypotheses based on broad knowledge. I try to setup similar integrated experiments and I find too much 'internet data' disruptive to resolving clear thought (enter notropics regimen for concentration hah!).  That being said, your collagen plan has great potential, though... if it works as designed.  I too have come to the conclusion that PM away from food collagen is likely better used for its intended purpose, so take it and hyraloric acid  before bed..... although I'm not doing it breaking 36hr fasts (!)  which sound better still. The hard thing is to stick with these plans long enough to determine possible efficacy one way or the other!

[mccoy]

 

 

Also just more to add on the mTOR angle. A lot of the fasting thing is about mTOR and autophagy, so the original poster was curious about specific types of protein like tryptophan and methionine. I've often been curious about mTOR activation with hydrolyzed collagen which contains glycine and hydroxyproline and other aminos and peptides. I don't know if these activate mTOR or not. For the longest time I've thought that given how glycine improves sleep quality (so does fasting), and given that your body sort of regenerates during high quality sleep, that taking the collagen right before bed was optimal. I still would try that as well on some nights, but not every night, just to see. I think it's more important to get it in there without other forms of protein than anything else. That's when it's most likely going to get to where it needs to be. That said, not sure where the research is on that. 

 

 

AFAIK, mTOR is a nutrient sensor, all nutrients, although some Leucine must be present as a signal which ultimately leads mTOR on the lysosome body, where it can start its anabolic business. ALL aminoacids are sensed, although Leu has a predominant role.

 

I've read some studies on nutritional geometry where they measured  mTOr activation (phosporylation ratio) in lab rats hepatocites in relation to nutritional geometry, and it turns out that an high protein/Carbs ratio boosts its activation.

 

The conceptual ancestral framewrok though is that mTOR is a sensor of the abundance of nutrients, all nutrients. If glucose and fats are lacking energy is lacking, AMPK is activated which inhibits mTOR.

 

My bottom line is that if  glycine and hydroxyproline contribute significantly to the abundance of amminoacids, if enough Leucine is present, if energy is present, mTOR will be upregulated. So glycine and hydroxyproline supplements may trigger mTOR overactivation in suitable conditions.

[Sith]

 

 

 

Also just more to add on the mTOR angle. A lot of the fasting thing is about mTOR and autophagy, so the original poster was curious about specific types of protein like tryptophan and methionine. I've often been curious about mTOR activation with hydrolyzed collagen which contains glycine and hydroxyproline and other aminos and peptides. I don't know if these activate mTOR or not. For the longest time I've thought that given how glycine improves sleep quality (so does fasting), and given that your body sort of regenerates during high quality sleep, that taking the collagen right before bed was optimal. I still would try that as well on some nights, but not every night, just to see. I think it's more important to get it in there without other forms of protein than anything else. That's when it's most likely going to get to where it needs to be. That said, not sure where the research is on that. 

 

 

AFAIK, mTOR is a nutrient sensor, all nutrients, although some Leucine must be present as a signal which ultimately leads mTOR on the lysosome body, where it can start its anabolic business. ALL aminoacids are sensed, although Leu has a predominant role.

 

I've read some studies on nutritional geometry where they measured  mTOr activation (phosporylation ratio) in lab rats hepatocites in relation to nutritional geometry, and it turns out that an high protein/Carbs ratio boosts its activation.

 

The conceptual ancestral framewrok though is that mTOR is a sensor of the abundance of nutrients, all nutrients. If glucose and fats are lacking energy is lacking, AMPK is activated which inhibits mTOR.

 

My bottom line is that if  glycine and hydroxyproline contribute significantly to the abundance of amminoacids, if enough Leucine is present, if energy is present, mTOR will be upregulated. So glycine and hydroxyproline supplements may trigger mTOR overactivation in suitable conditions.

 

 

I like this answer!
 

Though a protein source deficient in leucine (and methionine and tryptophan), in a high carb dietary environment would prevent over-expression of mTOR. Is this logic correct? 

 

I have always thought of Leucine as the amino acid predominantly responsible for the sustained upregulation of mTOR.

[brosci]

 

 

 

 

Also just more to add on the mTOR angle. A lot of the fasting thing is about mTOR and autophagy, so the original poster was curious about specific types of protein like tryptophan and methionine. I've often been curious about mTOR activation with hydrolyzed collagen which contains glycine and hydroxyproline and other aminos and peptides. I don't know if these activate mTOR or not. For the longest time I've thought that given how glycine improves sleep quality (so does fasting), and given that your body sort of regenerates during high quality sleep, that taking the collagen right before bed was optimal. I still would try that as well on some nights, but not every night, just to see. I think it's more important to get it in there without other forms of protein than anything else. That's when it's most likely going to get to where it needs to be. That said, not sure where the research is on that. 

 

 

AFAIK, mTOR is a nutrient sensor, all nutrients, although some Leucine must be present as a signal which ultimately leads mTOR on the lysosome body, where it can start its anabolic business. ALL aminoacids are sensed, although Leu has a predominant role.

 

I've read some studies on nutritional geometry where they measured  mTOr activation (phosporylation ratio) in lab rats hepatocites in relation to nutritional geometry, and it turns out that an high protein/Carbs ratio boosts its activation.

 

The conceptual ancestral framewrok though is that mTOR is a sensor of the abundance of nutrients, all nutrients. If glucose and fats are lacking energy is lacking, AMPK is activated which inhibits mTOR.

 

My bottom line is that if  glycine and hydroxyproline contribute significantly to the abundance of amminoacids, if enough Leucine is present, if energy is present, mTOR will be upregulated. So glycine and hydroxyproline supplements may trigger mTOR overactivation in suitable conditions.

 

 

I like this answer!
 

Though a protein source deficient in leucine (and methionine and tryptophan), in a high carb dietary environment would prevent over-expression of mTOR. Is this logic correct? 

 

I have always thought of Leucine as the amino acid predominantly responsible for the sustained upregulation of mTOR.

 

If I recall, there was a recent Peter Attia interview (I believe he's working on a book on longevity) where he mentioned supplementing Leucine around exercise since the activation was so short-lived and there was a difference between activating mTOR in skeletal muscle around intense training (mTORC1 or MTORC2?) via supplementation (in the context of 16-20h of fasting/d?) vs a chronic dietary intake of carbohydrates and proteins via a western diet model.

 

https://www.ncbi.nlm...les/PMC3156598/

 

"Previous observations in yeast suggested that the branched-chain amino acids (BCAAs) leucine, isoleucine, and valine might be potential candidates in promoting survival [11]. We recently demonstrated that long-term dietary supplementation with a specific BCAA-enriched amino acid mixture (BCAAem) increased average lifespan of male mice [12]. This was accompanied by increased mitochondrial biogenesis and sirtuin 1 (SIRT1) expression and by up-regulated ROS defense system, with reduced oxidative damage, both in cardiac and skeletal muscles of middle aged mice"

Edited by brosci, 29 June 2017 - 02:10 PM.

[mccoy]

 

 

 

Though a protein source deficient in leucine (and methionine and tryptophan), in a high carb dietary environment would prevent over-expression of mTOR. Is this logic correct? 

 

I have always thought of Leucine as the amino acid predominantly responsible for the sustained upregulation of mTOR.

 

 

Actually, I don't know. As far as local upregulation in muscle tissues is concerned, literature insists on Leucine signaling (but it would just start the process) but as far as general regulation is concerned, all aminoacids seem to be sensed by mTOR, thru the Rag GTpases. This article for example, coauthored by David Sabatini, who discovered mTOR and was shortlisted for the Nobel prize a few years ago (maybe he's going to receive the award in future) speaks just of aminoacids sensing in general and never of Leucine.

 

Regulation of mTORC1 by amino acids

 mtorC-aminoacids.JPG   68.53KB   1 downloads

 

On the other hand, in this other more recent article, always coauthored by Sabatini, Leucine is described as a necessary signal to activate mTOr. In my abysmal ignorance, I construe the info available in the following way:

 

1. mTORC1 is mainly nutrient sensor. All nutrients, It senses, thru various mechanisms, when the level of nutrient is such that proliferation and growth is the optimal response for survival.
2. mTORC1 is bound to the lysosome in the presence of a minimum amount of Leucine. This aminoacid rules the beginning of mTORC1 activation. Leucine is abundant in nearly all foods, plant-based and animal protein (especially so the latter) and  I evidently has been taken as the favourite input for triggering mTOR activity, and is sensed by the Sestrin2 sub-sensor.

Sestrin2 is a leucine sensor for the mTORC1 pathway

 

 

So, my bottomline is that, if the minimum threshold of Leucine is present and sensed by Sestrin2, then mTORC1 is bound to the lysosome and becomes sensible to the abundance of all aminoacids. Once bound to the lysosome, it will be upregulated only if the Rheb GTpase is active that is, Akt phosphorylation will inhibit the TSC complex, which si a brake to rheb, which is the second mainswitch which will activate mTORC1 (to phosporylate akt, there must be enough glucose/glycogen and oxygen otherwiseAMPk will inhibit it).

 

 Fig-1-The-mTOR-signaling-pathway-The-key-signaling-pathways-that-regulate-mTORC1-and (1).png   297.43KB   1 downloads

[mccoy]

If I recall, there was a recent Peter Attia interview (I believe he's working on a book on longevity) where he mentioned supplementing Leucine around exercise since the activation was so short-lived and there was a difference between activating mTOR in skeletal muscle around intense training (mTORC1 or MTORC2?) via supplementation (in the context of 16-20h of fasting/d?) vs a chronic dietary intake of carbohydrates and proteins via a western diet model.

 

 

https://www.ncbi.nlm...les/PMC3156598/

 

"Previous observations in yeast suggested that the branched-chain amino acids (BCAAs) leucine, isoleucine, and valine might be potential candidates in promoting survival [11]. We recently demonstrated that long-term dietary supplementation with a specific BCAA-enriched amino acid mixture (BCAAem) increased average lifespan of male mice [12]. This was accompanied by increased mitochondrial biogenesis and sirtuin 1 (SIRT1) expression and by up-regulated ROS defense system, with reduced oxidative damage, both in cardiac and skeletal muscles of middle aged mice"

 

 

Brosci yes, I've studied those affirmations by Peter Attia, mainly expressed in the podcast with Rhonda Patrick, with Chris Kesser and maybe in some other occasions.

 

The bodybuilding literature is replete with the use of Leucine and BCAAs supplements to upregulate mTORC1, the risk there I believe being that the spike in the blood serum may give the triggering signal in other tissues different from the skeletal muscle tissues. Sure enough, with the quantities of BCAAs used by bodybuilders, mTOR activity will be overamplified in the whole system and not just in the muscles, promoting too much proliferation and cancer cells propagation. Conversely, if BCAAs are used only before or during strenuos workouts and at alternate days, then there is a reasonable probability that mainly muscle tissue will be stimulated. Muscle biopsies have been taken after BCAAs ingestion+ exercise, but I doubt that contemporary biopsies of hepatocites and other organs have been taken, so we really don't know.

I tried BCAAs a few times, then discontinued their use because it is not cautious in my reasoned opinion.

I would suggest BCAAs only for those who are really hard-gainers, or those who suffer sarcopenia, or those who have difficulties in recovering after an injury or an illness.

Also, BCAAs are too expensive. I would rather eat Leucine-rich food instead. Also, BCAAs would add to those already present in Whey protein isolates or hydrolized which bodybuilders take abundantly, plus the huge amounts of food they ingest. mTORc overamplification in the whole body would then be a sure thing.

 

I read your article and a related article from the same authors, it seems genuine, in that they did that experiment on 30 mice plus 30 mice control, the BCAAs supplemented mice on the average lived longer (higher median age). Since the article you cited is maybe a little confused and reports are contradictory (CRed mice live longer with less BCAAs), more literature is needed. Some other similar publications have been heavily sponsored by the protein industry. Also, the economical interests here are huge, given the retail price of BCAAs and I would be very cautious before accepting the literature results on the almost miracolous effects of BCAAs as true.

Edited by mccoy, 02 July 2017 - 11:39 AM.

[floweryriddle]

I have nothing constructive to add but just wanted to say that the discussion here is fantastic. I learned a ton of new things out of something that seemed like a simple question. Thanks a ton [emoji106]

[aribadabar]

He goes on to mention:

 

"If you have an MTHFR polymorphism that decreases MTHFR activity, you are likely to be wasting excess glycine into the urine, and you may be a good candidate for someone who could benefit from more glycine in the diet beyond what you would usually get."

 

What does he mean by that?

 What is the point of taking extra glycine if it only passes through you ("wasting") and peeing it out? You megadose glycine in a hope that SOME of it can be utilized before being expelled?

[aribadabar]

To whoever marked my post ill-informed - note that there are QUESTION MARKS, not full stops, at the end of each of my sentences.