James V J, Delbridge L, McLennan S V, Yue D K
School of Physics, University of New South Wales, Kensington, Australia.
Diabetes. 1991 Mar;40(3):391-4. doi: 10.2337/diab.40.3.391.
Extensive investigations of the solubility and fluorescence of collagen fibers in diabetes have revealed that there are significant changes in their physical properties. These changes are associated with increased cross-link formation. We used X-ray diffraction to study these changes in human extensor tendons at a molecular level in relation to both aging and diabetes. Our results indicate that diabetes induces significant alterations in the ultrastructure of collagen in the lateral packing of the molecules and the axial structure of the specimen. These changes can be induced in normal tendon by incubation in ribose and glucose-6-phosphate but are different from those associated with the normal process of aging.
对糖尿病患者胶原纤维的溶解性和荧光性进行的广泛研究表明,其物理性质发生了显著变化。这些变化与交联形成增加有关。我们利用X射线衍射在分子水平上研究了人类伸肌腱中与衰老和糖尿病相关的这些变化。我们的结果表明,糖尿病会导致分子侧向堆积和标本轴向结构中胶原蛋白超微结构的显著改变。在正常肌腱中,通过在核糖和6-磷酸葡萄糖中孵育可诱导这些变化,但这些变化与正常衰老过程中相关的变化不同。