Dr. Luc (Luke) van Loon

We used intrinsically labeled protein, for example, also to show that the glycine or that the amino acids actually show up in collagen.

So yes, collagen can be used and is a good source of glycine and proline, but does it further increase connective protein synthesis when compared to a high-quality dairy protein or a different protein?

So far, we haven't seen any evidence for that.

But of course, again, it's just a matter of the amount.

If you give twice the amount of collagen, which has the same essential amino acids, then half the amount of, for example, egg or dairy protein, you might actually see exactly the same response.

But there's a lot of studies that still need to be done to figure this one out.

So the amino acids, I mean, so like I said, collagen contains...

like any other protein, a lot of amino acids, and particularly the amino acids glycine and proline.

And of course, those amino acids are going to be used to synthesize proteins, whether that's connective protein or whether that's myofibular protein.

So yes, I mean, this is just a protein source which has a lot of glycine and proline.

So yeah, why not?

Why not?

But from a complete constitution, it doesn't have as much as a balanced amino acid profile as most animal or higher quality animal derived proteins.

But that doesn't mean that, I mean, I think, I mean, this is something that I think we, so in muscle, I think that the availability of the amino acids is not restricting the increase after physical activity.

Because after physical activity, we see the connective tissue protein synthesis rates go up.

but it doesn't seem to depend on the amount of protein or collagen that you provide.

So I think there it's not limiting, at least not in the first few hours after exercise.

Maybe in a longer time frame?

I don't know.

That's a possibility.