Collagen synthesis in cultured skin fibroblasts from a patient with osteogenesis imperfecta was studied. Approximately 2 fold accumulation of collagen in the cell layer was found. The slower mobility of proα1 (I) and proα2 (I) as well as α1 and α2 (I) polypeptide on sodium dodecylsulfate-polyacrylamide gel electrophoresis was detected, indicating that abnormal posttranslational modification could be present in type I procollagen in patient fibroblasts. The degrees of hydroxylation and subsequent glycosylation of lysine residues in the affected collagen were elevated 1.5 and 1.4 fold, respectively. There were no significant changes in the relative content of type III to type I collagen nor the incorporation of mannose into the carboxyterminal propeptide of proα1 (I) and proα2 (I). These results indicate that the patient produces an over-modified type I procollagen which is responsible for the clinical features and has a collagen abnormality already reported in type II osteogenesis imperfecta.
|Number of pages||4|
|Journal||Journal of Dermatology|
|Publication status||Published - 1994 Jan 1|
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