Knott L, Whitehead C C, Fleming R H, Bailey A J
Division of Molecular and Cellular Biology, University of Bristol, U.K.
Biochem J. 1995 Sep 15;310 ( Pt 3)(Pt 3):1045-51. doi: 10.1042/bj3101045.
No detailed biochemical analysis has been carried out of the compositional changes in the collagen matrix of avian bone in relation to increased bone fragility in osteoporosis. We have shown that osteoporosis in avian bone is certainly not just a simple loss of apatite and collagen, but involves significant changes in the biochemistry of the collagen molecule and consequently in the physical properties of the fibre. The decreased mechanical strength and the change in the thermal stability can be directly related to changes in post-translational modifications, i.e. lysine hydroxylation and the intermolecular cross-link profile. The increased hydroxylation and change in cross-linking are consistent with increased turnover of the collagen, possibly in an attempt to initiate a repair mechanism which, in fact, leads to an acceleration in the increase in fragility of the bone. Clearly there are post-translational modifications of the newly synthesized collagen in avian osteoporosis, and these changes may play a role in the pathogenesis of the disease.
尚未针对骨质疏松症中禽类骨骼胶原基质成分变化与骨脆性增加之间的关系进行详细的生化分析。我们已经表明，禽类骨骼中的骨质疏松症肯定不只是磷灰石和胶原蛋白的简单流失，而是涉及胶原分子生化性质的显著变化，进而影响纤维的物理性质。机械强度降低和热稳定性变化可直接与翻译后修饰的变化相关，即赖氨酸羟基化和分子间交联谱。羟基化增加和交联变化与胶原蛋白更新率增加一致，这可能是试图启动一种修复机制，但实际上却导致骨脆性增加加速。显然，在禽类骨质疏松症中，新合成的胶原蛋白存在翻译后修饰，这些变化可能在该疾病的发病机制中起作用。
