Can autophagy reverse collagen glycation?

[sloopnoob]

Most research says it is an irreversible process, one research says autophagy Advanced glycation end products (AGEs), I also read that Matrixyl 3000 could reverse it.
Calling collagen and autophagy experts @Cope @Lifeisgood72

 

[Deleted member 5634]

How do you plan to reach autophagy OP?

 

[sloopnoob]

How do you plan to reach autophagy OP?

fasting 3-5 days every 2-3 weeks

 

[thickdickdaddy27]

idk about reverse but carnosine is legit for inhibiting the process

 

[JustBeCurry]

source?

 

[Deleted member 5634]

fasting 3-5 days every 2-3 weeks

My experience is yes, but this amount of fasting is going to crush your sex drive and muscle building capacity, also extremely difficult a 3 day fast is already difficult.

 

[sloopnoob]

crush your sex drive and muscle building capacity

dont care much about muscles and sex drive rn, I have good muscle foundation so regaining what I will lose won't take more than 3 weeks at most and I don't have a gf so dc about sex drive. Skin is utmost priority rn

 

[sloopnoob]

idk about reverse but carnosine is legit for inhibiting the process

almost zero sugars,alpha lipoic acid ,carnosine ,blueberry ,green tea, vitamin c, quercetin, ginger, autophagy + exercise, all these things can inhibit it I don't have to worry about inducing more glycation since I have taken care of that already I want to reverse the damage already caused to my skin

 

[sloopnoob]

one research says autophagy Advanced glycation end products (AGEs)

I meant one research says autophagy removes Advanced glycation end products (AGEs)

 

[Cope]

The study on Autophagy was in vitro but it seems legit.

Do you have a link to the study on Matrixyl 3000?

 

[Chintuck22]

The study on Autophagy was in vitro but it seems legit.

Do you have a link to the study on Matrixyl 3000?

Oh wow no way! Enlighten us once with your vast knowledge @Cope

 

[.*my*.]

Autofagy?

Autofagy?

 

[Cope]

Oh wow no way! Enlighten us once with your vast knowledge @Cope

There are a few hypotheses regarding potential mechanisms that repair glycated proteins. Indeed, there are two intracellular anti-glycation systems that could restore the glycated proteins to their initial form. However, these mechanisms only act on Amadori products and cannot change AGEs. The first of these systems, known as transglycation, separates the carbohydrate portion from the glycated protein and transfers it to an intracellular nucleophile, made up of free amino acids, in a non-enzymatic process. Removing this portion allows the protein to regain its original shape. It is important to note that these nucleophile agents, which include glutathione and carnosine, have an anti-glycation effect. Other molecules, such as pyridoxamine and taurine, combat glycation through different molecular processes. The second repair mechanism uses fructosamine-3-kinase, an enzyme that catalyzes the repair of glycation intermediaries like fructoselysines. The fructosamine-3-kinase enzyme thus limits the formation of glycated hemoglobin in erythrocytes.

However, glycated intracellular proteins are not eliminated by the cell. They remain and may concentrate in and damage cells and tissues. The accumulation of intracellular glycation triggers a series of malfunctions that may end in cellular apoptosis. Extracellular glycated products can also be broken down by proteases. Their elimination through the kidneys is directly dependent on renal function and as a result, in chronic kidney failure, glycated blood components accumulate in the blood and tissues. Indeed, the concentration of plasma AGEs is up to forty times higher in patients on renal dialysis than in healthy patients. In addition, as previously discussed, the remodeling enzymes of the extracellular matrix are less effective in degrading glycated proteins; one example of this phenomenon being the reduced effectiveness of matrixins on glycated collagen. This may partially explain the loss of biomechanical properties in soft tissues like the skin.

 

[Chintuck22]

There are a few hypotheses regarding potential mechanisms that repair glycated proteins. Indeed, there are two intracellular anti-glycation systems that could restore the glycated proteins to their initial form. However, these mechanisms only act on Amadori products and cannot change AGEs. The first of these systems, known as transglycation, separates the carbohydrate portion from the glycated protein and transfers it to an intracellular nucleophile, made up of free amino acids, in a non-enzymatic process. Removing this portion allows the protein to regain its original shape. It is important to note that these nucleophile agents, which include glutathione and carnosine, have an anti-glycation effect. Other molecules, such as pyridoxamine and taurine, combat glycation through different molecular processes. The second repair mechanism uses fructosamine-3-kinase, an enzyme that catalyzes the repair of glycation intermediaries like fructoselysines. The fructosamine-3-kinase enzyme thus limits the formation of glycated hemoglobin in erythrocytes.

However, glycated intracellular proteins are not eliminated by the cell. They remain and may concentrate in and damage cells and tissues. The accumulation of intracellular glycation triggers a series of malfunctions that may end in cellular apoptosis. Extracellular glycated products can also be broken down by proteases. Their elimination through the kidneys is directly dependent on renal function and as a result, in chronic kidney failure, glycated blood components accumulate in the blood and tissues. Indeed, the concentration of plasma AGEs is up to forty times higher in patients on renal dialysis than in healthy patients. In addition, as previously discussed, the remodeling enzymes of the extracellular matrix are less effective in degrading glycated proteins; one example of this phenomenon being the reduced effectiveness of matrixins on glycated collagen. This may partially explain the loss of biomechanical properties in soft tissues like the skin.

Geniunely 'mirin, good job champ, amazing !!

 

[sloopnoob]

Do you have a link to the study on Matrixyl 3000?

there was no study, only claims. That is why I didn't take it at face value. One such claim being this

 

[sloopnoob]

However, glycated intracellular proteins are not eliminated by the cell.

Do glycated intracellular proteins have any superficial impact?

 

[Deleted member 3990]

If glycation of proteins and the resulting damage is your main concern, so be it. Ending up taking thousands of supplements

 

[sloopnoob]

source?

for what exactly? Matrixyl 3000 reversing it is just a claim, I haven't found any data backing it up.
https://ncnskincare.com/blog/we-use-all-three-matrixyl-peptides/ this website says " Matrixyl 3000 (Palmitoyl Terapeptide) will do this as well but it also inhibits and reverses glycation damage. This added benefit can make this a better choice as an anti aging skin care product for some people. "

Autophagy helping with removal of AGE:

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onlinelibrary.wiley.com

 

[sloopnoob]

Ending up taking thousands of supplements

The question was about not eating anything at all, let alone taking thousands of supplements.

 

[Cope]

there was no study, only claims. That is why I didn't take it at face value. One such claim being this View attachment 851087

I can't find any scientific journal or study stating this, weird.

Do glycated intracellular proteins have any superficial impact?

I think so. Glycosaminoglycans consist of chondroitin sulfate and hyaluronic acid. The intent of certain peptides like GHK-Cu is to stimulate glycosaminoglycans synthesis.

 

[Chintuck22]

Don't restrict calories or fast, this will lower the activity of the mTOR/pi3k/ATK pathways as insulin is vital for the activation of these pathways, fasting and lowering caloric intake will also decrease both insulin and leptin within the body, leptin is the hormone that is released when you have eaten past the point of satiation, my findings suggest that leptin is a potent agonist to osteogenic genotypes, essentially it induces bone formation, remodeling, and mineral disposition, it also increases IGF-1 levels, which is what we want.

 

[Deleted member 773]

Idk but I’m doing a week long fast in December. I did one for 3 and 1/2 days in November and it was easy AF.

 

[sloopnoob]

Idk but I’m doing a week long fast in December. I did one for 3 and 1/2 days in November and it was easy AF.

I've had 3 weddings in family this month and another in a few days, I can't fast coz of all the buffet rn but will do an extended fast after I'm done with that

 

[Deleted member 2205]

Don't restrict calories or fast, this will lower the activity of the mTOR/pi3k/ATK pathways as insulin is vital for the activation of these pathways, fasting and lowering caloric intake will also decrease both insulin and leptin within the body, leptin is the hormone that is released when you have eaten past the point of satiation, my findings suggest that leptin is a potent agonist to osteogenic genotypes, essentially it induces bone formation, remodeling, and mineral disposition, it also increases IGF-1 levels, which is what we want.

He is literally trying to lower those very pathways because it is too late for that born formation or remodeling to happen