Abstract
Type I, type III, and type V collagens were isolated from type VI Ehlers-Danlos syndrome fibroblasts. Five different α 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 S2 0/o, 73 0/o, and 76'0/o of controls, respectively.
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