期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1972
卷号：69
期号：10
页码：2899-2903
DOI：10.1073/pnas.69.10.2899
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Cell culture studies were performed on members of a family in which two sisters, ages 9 and 12, have a similar disorder characterized clinically by severe scoliosis, joint laxity and recurrent dislocations, hyperextensible skin, and thin scars. The skin collagen from the sisters was markedly deficient in hydroxylysine, but other amino acids were present in normal amounts. Hydroxylysine in collagen from fascia and bone was reduced to a lesser extent. Since the most likely explanation for the hydroxylysine deficiency was a reduction in enzymatic hydroxylation of lysine residues in protocollagen, we measured the activity of lysyl-protocollagen hydroxylase in crude lysates of cultured skin fibroblasts. Enzyme activities in the two affected children were 14 and 10% of controls, whereas the activity was about 60% of normal in the mother, a pattern most consistent with autosomal recessive inheritance. The mutant enzyme demonstrated the same cofactor requirements as that from normal cells. Deficiency of lysyl-protocollagen hydroxylase is the first inborn error of human collagen metabolism to be defined at the biochemical level.
