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Age-related changes on the surface of vitreous collagen fibrils.

机译:玻璃体胶原原纤维表面的年龄相关变化。

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摘要

PURPOSE. To determine whether aging vitreous collagen fibrils undergo ultrastructural changes that might underlie vitreous liquefaction and posterior vitreous detachment. METHODS. Vitreous collagen fibrils from 21 human subjects (age range, 3-89 years) and from bovine eyes were isolated on electron microscopy grids. Cupromeronic blue labeling in the presence of 0.3 M MgCl(2) and immunogold labeling for collagen types II and IX were analyzed by transmission electron microscopy. RESULTS. Aging was associated with marked changes on the surface of human vitreous collagen fibrils, including an exponential loss of type IX collagen along with its chondroitin sulfate side-chains (half-life, 11 years) and a fourfold increase in the exposure of type II collagen. CONCLUSIONS. Despite being a minor component of vitreous collagen fibrils, type IX collagen, probably by virtue of its chondroitin sulfate side-chains, shields type II collagen from exposure on the fibril surface. With aging, this shielding diminishes, resulting in the surface exposure of "sticky" type II collagen and thus predisposing the vitreous collagen fibrils to fusion. These changes could underlie vitreous liquefaction and weakening of vitreoretinal adhesion.
机译:目的。要确定老化的玻璃体胶原原纤维是否经历了超微结构变化,可能是玻璃液化和玻璃体后脱离的基础。方法。在电子显微镜格栅上分离了来自21位人类受试者(年龄范围3-89岁)和牛眼的玻璃状胶原纤维。通过透射电子显微镜分析了存在0.3 M MgCl(2)的铜铬蓝标记和II型和IX型胶原的免疫金标记。结果。衰老与人类玻璃体胶原纤维表面的显着变化有关,包括IX型胶原及其硫酸软骨素侧链的指数损失(半衰期为11年),以及II型胶原的暴露量增加了四倍。结论。尽管是玻璃体胶原蛋白纤维的次要成分,IX型胶原蛋白(可能是由于其硫酸软骨素侧链)仍能保护II型胶原蛋白,使其不暴露于原纤维表面。随着年龄的增长,这种屏蔽作用减弱,导致“粘性” II型胶原蛋白在表面暴露,从而使玻璃状胶原蛋白原纤维易于融合。这些变化可能是玻璃化液化和玻璃体视网膜粘连减弱的基础。

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