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The Metabolic Capacity For Glycine Biosynthesis Does Not Satisfy The Need For Collagen Synthesis

paymanz

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A weak link in metabolism: the metabolic capacity for glycine biosynthesis does not satisfy the need for collagen synthesis.

In a previous paper, we pointed out that the capability to synthesize glycine from serine is constrained by the stoichiometry of the glycine hydroxymethyltransferase reaction, which limits the amount of glycine produced to be no more than equimolar with the amount of C 1 units produced. This constraint predicts a shortage of available glycine if there are no adequate compensating processes. Here, we test this prediction by comparing all reported fl uxes for the production and consumption of glycine in a human adult. Detailed assessment of all possible sources of glycine shows that synthesis from serine accounts for more than 85% of the total, and that the amount of glycine available from synthesis, about 3 g/day, together with that available from the diet, in the range 1.5-3.0 g/day, may fall significantly short of the amount needed for all metabolic uses, including collagen synthesis by about 10 g per day for a 70 kg human. This result supports earlier suggestions in the literature that glycine is a semi-essential amino acid and that it should be taken as a nutritional supplement to guarantee a healthy metabolism.
 
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fyo

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Re: A weak link in metabolism: the metabolic capacity for glycine biosynthesis does not satisfy the need for collagen sy

>fall significantly short of the amount needed for all metabolic uses, including collagen synthesis by about 10 g per day

Even more for people under metabolic stress, particularly for the gut, which is largely collagen, and prone to breakdown under stress.
 

BingDing

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Re: A weak link in metabolism: the metabolic capacity for glycine biosynthesis does not satisfy the need for collagen sy

Good post. One teaspoon of glycine is 4g, added to milk is a good way to take it.

And yet another essential metabolic pathway that requires a methyl donor. I'm keeping track!
 
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Re: A weak link in metabolism: the metabolic capacity for glycine biosynthesis does not satisfy the need for collagen sy

BingDing said:
Good post. One teaspoon of glycine is 4g, added to milk is a good way to take it.

And yet another essential metabolic pathway that requires a methyl donor. I'm keeping track!
:lol: what are you seeing in this?
 

BingDing

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Re: A weak link in metabolism: the metabolic capacity for glycine biosynthesis does not satisfy the need for collagen sy

Such_Saturation said:
BingDing said:
Good post. One teaspoon of glycine is 4g, added to milk is a good way to take it.

And yet another essential metabolic pathway that requires a methyl donor. I'm keeping track!
:lol: what are you seeing in this?

Just that methyl donors per se don't cause cancer.
 
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Re: A weak link in metabolism: the metabolic capacity for glycine biosynthesis does not satisfy the need for collagen sy

BingDing said:
Such_Saturation said:
BingDing said:
Good post. One teaspoon of glycine is 4g, added to milk is a good way to take it.

And yet another essential metabolic pathway that requires a methyl donor. I'm keeping track!
:lol: what are you seeing in this?

Just that methyl donors per se don't cause cancer.

Is that really all :cool:
 

johns74

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Jun 17, 2014
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Re: A weak link in metabolism: the metabolic capacity for glycine biosynthesis does not satisfy the need for collagen sy

Is lack of glycine the main usual problem that blocks collagen synthesis?

Or are there other things and nutrients one needs to pay attention to?
 

paymanz

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Re: A weak link in metabolism: the metabolic capacity for glycine biosynthesis does not satisfy the need for collagen sy

johns74 said:
Is lack of glycine the main usual problem that blocks collagen synthesis?

Or are there other things and nutrients one needs to pay attention to?

vitamin c,manganese,silicon,copper,zinc,proline,co2 and red ligth
trace element bromine also have a role.
 

sm1693

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Re: A weak link in metabolism: the metabolic capacity for glycine biosynthesis does not satisfy the need for collagen sy

I have been doing a lot of experimenting recently with this collagen synthesis theory.

The vitamin C and other effective nutrients I get from whole fruit seems distinctly to heal the gut, whereas, pasteurized juice (all kinds) appears to have no effect on gut healing.

I suppose this points to the oxidation of nutrients being quite negative towards health. I have read all Peat has written on oxidation, and to be honest, it is quite difficult to decipher from his writing how the information should be put into real life practice.

He says un-pasteurized juice is better than pasteurized, but I haven't seen much emphasis put on it. And since it is very difficult to get ahold of un-pasteurized juice, the vast majority of RP'ers end up going with the cheap and easy pasteurized juice.
 

Parsifal

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paymanz said:
post 83184
johns74 said:
Is lack of glycine the main usual problem that blocks collagen synthesis?

Or are there other things and nutrients one needs to pay attention to?

vitamin c,manganese,silicon,copper,zinc,proline,co2 and red ligth
trace element bromine also have a role.
Where did Ray talked about silicon? I thought that silicon is just like glass basically?
 
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paymanz

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Parsifal said:
post 119036
paymanz said:
post 83184
johns74 said:
Is lack of glycine the main usual problem that blocks collagen synthesis?

Or are there other things and nutrients one needs to pay attention to?

vitamin c,manganese,silicon,copper,zinc,proline,co2 and red ligth
trace element bromine also have a role.
Where did Ray talked about silicon? I thought that silicon is just like glass basically?


ray never talked about that but if you look at pubmed or other sources you find studies showing essentiality of silicon for connective tissue health.
 
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YuraCZ

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Parsifal said:
post 119036
paymanz said:
post 83184
johns74 said:
Is lack of glycine the main usual problem that blocks collagen synthesis?

Or are there other things and nutrients one needs to pay attention to?

vitamin c,manganese,silicon,copper,zinc,proline,co2 and red ligth
trace element bromine also have a role.
Where did Ray talked about silicon? I thought that silicon is just like glass basically?
Your body needs ORGANIC silica as well as ORGANIC sulfur for nice and healthy skin, nails, hairs etc..(those micronutrients are not found in food anymore basically) There is a big difference between type of micronutrient and how its utilised in the human body.. Btw balance between those micronutrients is also important. For example you need copper for collagen synthesis as well as sulfur or zinc, vit C etc.. and because they are antagonists. So for example too much vitC, sulfur, zinc etc.. can deplete copper and your collagen synthesis is ****88 and vise versa Too much copper will deplete sulfur, vit C, zinc as well as bioflavonoids rutin and hesperidin(they are especially important for strong capillaries, blood vessels etc..) so your collagen synthesis will be ****88 as well...
 
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Parsifal

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YuraCZ said:
post 119135
Parsifal said:
post 119036
paymanz said:
post 83184
johns74 said:
Is lack of glycine the main usual problem that blocks collagen synthesis?

Or are there other things and nutrients one needs to pay attention to?

vitamin c,manganese,silicon,copper,zinc,proline,co2 and red ligth
trace element bromine also have a role.
Where did Ray talked about silicon? I thought that silicon is just like glass basically?
Your body needs ORGANIC silica as well as ORGANIC sulfur for nice and healthy skin, nails, hairs etc..(those micronutrients are not found in food anymore basically) There is a big difference between type of micronutrient and how its utilised in the human body.. Btw balance between those micronutrients is also important. For example you need copper for collagen synthesis as well as sulfur or zinc, vit C etc.. and because they are antagonists. So for example too much vitC, sulfur, zinc etc.. can deplete copper and your collagen synthesis is f***ed and vise versa Too much copper will deplete sulfur, vit C, zinc as well as bioflavonoids rutin and hesperidin(they are especially important for strong capillaries, blood vessels etc..) so your collagen synthesis will be f***ed as well...
Interesting, thanks, but it seems hard to know what the food that you eat really contain, looking on websites like Cronometer seems not really precise. By the way isn't there silica in nettle and sulfur in garlic? Why do you say that these nutrients are not found in food anymore?
 
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tara

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YuraCZ said:
post 119135
Your body needs ORGANIC silica as well as ORGANIC sulfur for nice and healthy skin, nails, hairs etc..(those micronutrients are not found in food anymore basically
Gee, where does all that hydrogen sulphide come from, if not from the organic suphur in the eggs, onions, garlic, etc we eat? :lol:
Though I guess if you restrict diet too much you can avoid getting enough.
 
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Amazoniac

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Not Uganda
Guru, I don't know why your work isn't more popular, I'm still impressed by the thoughtful approach.

For those that didn't (and won't) read, the main pathway for synthesis of glycine relies on the enzyme that at the same time adds to the system methyl groups accepted by folate (#3), these are two different needs. If you have an excess of glycine or increased requirement for methyl groups, you can degrade glycine and put it to other uses through the folate cycle (that you is all familiar with) and dispose what's not desired (#11); but the opposite, to allow more glycine synthesis, you can't do anything useful with the excess methyl groups without upsetting the balance (#4) and the disposal (#12) is insufficient given the usual glycine deficit; this becomes limiting and it's their constraint. The image is useful:

upload_2019-7-16_20-1-12.png

A summary of their calculations:

upload_2019-7-16_20-4-21.png
Check out the article.​

Extra bits:

"Collagen is the protein that characterizes the animal world, as it is the material that allows multicellular flexibility. It appeared with the origin of animal life in the Precambrian explosion (Aouacheria et al. 2006) and its history thus spans the same time period as that of animals, around 580 million years (Li et al. 1998). It is the most abundant protein in the human body and constitutes more than a quarter of the total protein (Waterlow 2006)."

Gelatin, stress, longevity
"Gelatin (the cooked form of collagen) makes up about 50% of the protein in an animal, but a much smaller percentage in the more active tissues, such as brain, muscle, and liver. 35% of the amino acids in gelatin are glycine, 11% alanine, and 21% proline and hydroxyproline."

¿​

"The high content of glycine in collagen (one-third of the amino acid residues) implies an important requirement for the availability of this amino acid to support a wealthy turnover of collagen, high enough to avoid problems of accumulation of undesirable chemical modifications (glycation and others), as a protein-deficient diet induces decreased turnover of protein, especially collagen (Gibson et al. 2002)."

"It was widely believed in the past that collagen turnover is very slow, with a life-span of several years for the molecule, but today it is recognized that it is a very significant proportion of the whole daily protein turnover (Waterlow 2006)."

"It might appear that experimental studies of collagen turnover and glycine production in rats or other small animals would definitively resolve the question. Unfortunately, however, the problem is greatly complicated by allometric scaling. A 70 kg human has 350 times the mass of a 200 g rat, but neither skeletal mass nor metabolic capacity increase in proportion to body mass. Skeletal mass is proportional to the 1.1 power of body mass (Reynolds and Karlotski 1977), so a human has about 350^1.1, i.e. about 630, times the skeletal mass of a rat, implying about 630 times as much collagen. On the other hand, metabolic capacity increases as the 0.75 power of body mass (Kleiber 1947) and so a human has only 350^0.75, or 81, times the metabolic capacity of a rat. As a result, collagen-related problems are typically found in large animals, not in small ones. These problems accumulate with age, and are especially acute in large animals that live for many years. All of this means that very little information about glycine requirements can be obtained by studying small laboratory animals with short lifetimes."
 
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