LYSYL HYDROXYLATION IN COLLAGENS FROM HYPERPLASTIC CALLUS AND EMBRYONIC BONES

被引：15

作者：

LEHMANN, HW ^{[1
]}

BODO, M ^{[1
]}

FROHN, C ^{[1
]}

NERLICH, A ^{[1
]}

RIMEK, D ^{[1
]}

NOTBOHM, H ^{[1
]}

MULLER, PK ^{[1
]}

机构：

[1] UNIV MUNICH,INST PATHOL,W-8000 MUNICH 2,GERMANY

来源：

BIOCHEMICAL JOURNAL | 1992年 / 282卷

关键词：

D O I：

10.1042/bj2820313

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Tissue from two patients with osteogenesis imperfecta suffering from a hyperplastic callus was studied. Although collagen type I from the compact bone and the skin and fibroblast cultures of these patients showed normal lysyl hydroxylation, collagen types I, II, III and V from the callus tissue were markedly overhydroxylated. Furthermore, the overhydroxylation of lysine residues covered almost equally the entire alpha-1(I) collagen chain, as demonstrated by the analysis of individual CNBr-derived peptides. In addition, collagen type I was isolated from femoral compact bone of 33 individuals who died between the 16th week of gestational age and 22 years. Lysyl hydroxylation rapidly decreased in both collagen alpha-1(I) and alpha-2(I) chains during fetal development, and only little in the postnatal period. The transient increase in lysyl hydroxylation and the involvement of various collagen types in callus tissue argue for a regulatory mechanism that may operate in bone repair and during fetal development.

引用

页码：313 / 318

页数：6

共 30 条

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