[{"from": "human", "value": "What can you tell me about this molecule? [C][C@H1][Branch1][O][C][N][C@@H1][Ring1][Branch1][C][=Branch1][C][=O][O][O]"}, {"from": "gpt", "value": "The molecule is a major component of the protein collagen. Hydroxyproline is produced by hydroxylation of the amino acid proline and is, therefore, a post-translationally modified amino acid. Hydroxyproline and proline play key roles for collagen stability. In particular, they permit the sharp twisting of the collagen helix. Hydroxyproline is found in few proteins other than collagen. The only other mammalian protein which includes hydroxyproline is elastin. For this reason, hydroxyproline content has been used as an indicator to determine collagen and/or gelatin amount in tissue or biological samples.  Increased serum and urine levels of hydroxyproline have been found in Paget's disease  Hydroxyproline (Hyp) content in biological fluids is used as a parameter of collagen catabolism, especially bone resorption or tissue degradation. Bedridden and elderly individuals show significantly elevated serum levels of hydroxyproline in comparison to normal, active individuals  Elevated levels of urinary hydroxyproline are also indicative of muscle damage  Increased reactive oxygen species (ROS) are also known to accelerate collagen degradation. Hydroxyproline levels increase in cases of depression and stress  (A3486, A3487, A3488, A3489)."}]