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. 1992 Mar 1;282(Pt 2):313–318. doi: 10.1042/bj2820313

Lysyl hydroxylation in collagens from hyperplastic callus and embryonic bones.

H W Lehmann 1, M Bodo 1, C Frohn 1, A Nerlich 1, D Rimek 1, H Notbohm 1, P K Müller 1
PMCID: PMC1130780  PMID: 1546948

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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