Properties of collagen in OIM mouse tissues.
The deletion of the alpha2 chain from type I collagen in the oim mouse model of osteogenesis imperfecta has been shown to result in a significant reduction in the mechanical strength of the tail tendon and bone tissue. However, the exact role of the alpha2 chain in reducing the mechanical properties is not clear. We now report that the stabilizing intermolecular cross-links in bone are significantly reduced by 27%, thereby contributing to the loss of tensile strength and the change in stress-strain profile. We also report that, in contrast to previous studies, the denaturation temperature of the triple helical molecule and the intact fibers are 2.6 degrees and 1.9 degrees C higher than the corresponding tail tendon collagen from wild-type mice. The increase in hydroxyproline content accounts, at least in part, for the increase in denaturation temperature. The alpha2 chain clearly plays an important part in stabilizing the type I collagen triple helix and fiber packing, but further studies are required to determine the precise mechanism.
Sims
T J
TJ
Division of Molecular and Cellular Biology, University of Bristol, Bristol, United Kingdom.
Miles
C A
CA
Bailey
A J
AJ
Camacho
N P
NP
D000818:Animals; D002113:Calcification, Physiologic / Q000502:physiology; D024042:Collagen Type I / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D003432:Cross-Linking Reagents / Q000032:analysis; D004195:Disease Models, Animal; D005260:Female; D006901:Hydroxylysine / Q000032:analysis / Q000378:metabolism; D008297:Male; D051379:Mice; D008817:Mice, Mutant Strains; D010013:Osteogenesis Imperfecta / Q000235:genetics* / Q000378:metabolism / Q000503:physiopathology; D011489:Protein Denaturation; D013623:Tail; D013710:Tendons / Q000737:chemistry / Q000378:metabolism; D013718:Tensile Strength; D013977:Tibia / Q000737:chemistry / Q000378:metabolism
D024042:Collagen Type I; D003432:Cross-Linking Reagents; D006901:Hydroxylysine