Ponce Aldo, Sorensen Christopher, Takemoto Larry
Division of Biology, Kansas State University, Manhattan, KS 66506, USA.
Mol Vis. 2006 Aug 10;12:879-84.
At high protein concentrations found in the lens, short-range order of lens proteins results in a medium of relatively constant protein density and refractive index that minimizes scattering of light. During aging and cataractogenesis of the lens, formation of high molecular weight aggregates causes fluctuations in this protein density, resulting in light scattering and a concomitant decrease in transparency, with eventual lens opacification. This review summarizes what is known about the molecular nature of short-range order, both in the normal and cataractous lens, then hypothesizes that part of this order involves heterologous crystallin interactions that may be necessary for the maintenance of lens transparency. A summary of past and possible future experimental approaches will be reviewed that can be used to ascertain the existence of these interactions and their possible changes during lens opacification.
在晶状体中发现的高蛋白浓度下,晶状体蛋白的短程有序结构形成了一种蛋白质密度和折射率相对恒定的介质,从而使光散射最小化。在晶状体老化和白内障形成过程中,高分子量聚集体的形成导致这种蛋白质密度发生波动,进而引起光散射并使透明度随之降低,最终导致晶状体混浊。本综述总结了正常晶状体和白内障晶状体中短程有序结构的分子本质的已知情况,然后推测这种有序结构的一部分涉及异源性晶状体蛋白相互作用,这可能是维持晶状体透明度所必需的。将回顾过去以及未来可能的实验方法总结,这些方法可用于确定这些相互作用的存在以及它们在晶状体混浊过程中可能发生的变化。