Post-translational modifications in the collagen of human osteoporotic femoral head.
No detailed biochemical analysis has been made of the possible compositional changes in the collagen relating to the fragility of osteoporotic bone. We report for the first time significant changes in the compositional properties of the collagen. The major differences were observed in the post-translational modifications, namely, in the hydroxylation of lysine residues and the nature of the stabilizing cross-links of the collagen fibre. The increase in hydroxylation was greater in the head region compared to the neck region of the femoral head, whilst the decrease in the intermediate cross-links was greater in the neck region. Clearly, the collagen is altered in osteoporosis and it is important that these changes are recognised in studies of bone metabolism in osteoporosis since they may play a role in the pathogenesis of the disease.
Bailey
A J
AJ
Department of Veterinary Medicine, University of Bristol, Langford, UK.
Wotton
S F
SF
Sims
T J
TJ
Thompson
P W
PW
D000328:Adult; D000368:Aged; D000596:Amino Acids / Q000032:analysis; D001842:Bone and Bones / Q000378:metabolism*; D003094:Collagen / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D005260:Female; D005269:Femur / Q000378:metabolism*; D006801:Humans; D006900:Hydroxylation; D006901:Hydroxylysine / Q000032:analysis; D066298:In Vitro Techniques; D008297:Male; D010024:Osteoporosis / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D012016:Reference Values
D000596:Amino Acids; D006901:Hydroxylysine; D003094:Collagen