A comparison of lysyl hydroxylation in various types of collagen from type VI Ehlers-Danlos syndrome fibroblasts.
Type I, type III, and type V collagens were isolated from type VI Ehlers-Danlos syndrome fibroblasts. Five different alpha chains were separated and their degrees of prolyl and lysyl hydroxylations were determined. Lysyl hydroxylation in all collagen types was low in the mutant fibroblasts compared to age-matched controls, with no significant change in prolyl hydroxylation. The degrees of lysyl hydroxylation in type I, type III, and type V collagens were 52%, 73%, and 76% of controls, respectively.
D000328:Adult; D003094:Collagen / Q000378:metabolism*; D004535:Ehlers-Danlos Syndrome / Q000378:metabolism*; D005347:Fibroblasts / Q000378:metabolism; D006801:Humans; D006900:Hydroxylation; D008239:Lysine / Q000378:metabolism*; D008875:Middle Aged; D011347:Procollagen / Q000378:metabolism; D011392:Proline / Q000378:metabolism
D011347:Procollagen; D003094:Collagen; D011392:Proline; D008239:Lysine