Biochemical changes in the collagen of human osteoporotic bone matrix.
Although it is known that collagen imparts mechanical strength to bone no detailed biochemical analysis has been made of osteoporotic bone collagen. We report for the first time significant changes in the properties of the collagen. Analysis of collagen types revealed little change in the proportion of Type III collagen, but in some cases there was a significant loss of the Type VI. However, the major differences were observed in the post-translational modifications, namely, in the stabilizing cross-links and the hydroxylation of the collagen. These changes indicated a higher turnover in the head region compared to the neck region of the femoral head and are consistent with the susceptibility of the neck region to fracture. Clearly, the collagen is altered in osteoporosis and these changes 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
D000368:Aged; D000369:Aged, 80 and over; D001857:Bone Matrix / Q000378:metabolism* / Q000648:ultrastructure; D003094:Collagen / Q000737:chemistry* / Q000378:metabolism*; D005260:Female; D006801:Humans; D006900:Hydroxylation; D008239:Lysine / Q000378:metabolism; D008297:Male; D008854:Microscopy, Electron; D008855:Microscopy, Electron, Scanning; D008875:Middle Aged; D010024:Osteoporosis / Q000378:metabolism* / Q000473:pathology; D012016:Reference Values
D003094:Collagen; D008239:Lysine