PMID: 9164823Jun 1, 1997Paper

Alteration in the extent of collagen I hydroxylation, isolated from femoral heads of women with a femoral neck fracture caused by osteoporosis

Calcified Tissue International
J KöwitzJ Mach

Abstract

The aim of this study was to investigate the extent of lysyl and prolyl hydroxylation of collagen I in osteoporosis and compare it with collagen I from "bone healthy" individuals. Collagen I was isolated from femoral heads of osteoporotic women, from women suffering from osteoarthrosis of the hip, and from healthy women 60-85 years of age. The femoral heads were dissected into compact and trabecular bone of the neck region and from trabecular bone of the head region, and collagen I was extracted by limited pepsin digestion. The amino acid analysis of individual alpha-chains showed a remarkably higher degree of hydroxylation of lysine residues both in the alpha1(I)- and in the alpha2(I)-chains in osteoporotic bone compared with osteoarthrotic and "normal" bone, whereas the prolyl hydroxylation was nearly unchanged. The lysyl overhydroxylation was observed in the compact as well as in the trabecular bone of osteoporotic femoral heads. These biochemical alterations may play a crucial role in the pathogenesis of osteoporosis.

Citations

Jan 12, 2002·Journal of Biomedical Materials Research·Junro YamashitaC Mauli Agrawal
Dec 13, 2005·Osteoporosis International : a Journal Established As Result of Cooperation Between the European Foundation for Osteoporosis and the National Osteoporosis Foundation of the USA·S Viguet-CarrinP D Delmas
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