突变型（R116C）和野生型αA晶状体蛋白与肌动蛋白的差异结合。
Differential binding of mutant (R116C) and wildtype alphaA crystallin to actin.
作者信息
Brown Zachery, Ponce Aldo, Lampi Kirsten, Hancock Lynn, Takemoto Larry
机构信息
Division of Biology, Kansas State University, Manhattan 97239, USA.
出版信息
Curr Eye Res. 2007 Dec;32(12):1051-4. doi: 10.1080/02713680701769989.
Abstract
PURPOSE
Quantitate the interaction of mutant (R116C) and wildtype human alphaA crystallins with actin.
METHODS
AlphaA crystallins, expressed in a recombinant system, were purified, followed by passage through an actin affinity column.
RESULTS
Binding of mutant alphaA crystallin was significantly less than binding of wildtype alphaA crystallin.
CONCLUSIONS
The R116C mutation of alphaA crystallin found in human cataracts binds less to the cytoskeletal component actin. Since both alphaA crystallin and actin are necessary for proper development of the lens, decreased binding of the mutant protein to actin may perturb normal differentiation processes of lens cells which are necessary for transparency.
摘要
目的
定量分析突变型（R116C）和野生型人αA晶状体蛋白与肌动蛋白的相互作用。
方法
在重组系统中表达的αA晶状体蛋白经纯化后，通过肌动蛋白亲和柱。
结果
突变型αA晶状体蛋白的结合显著少于野生型αA晶状体蛋白的结合。
结论
在人类白内障中发现的αA晶状体蛋白的R116C突变与细胞骨架成分肌动蛋白的结合较少。由于αA晶状体蛋白和肌动蛋白对于晶状体的正常发育都是必需的，突变蛋白与肌动蛋白结合的减少可能会扰乱晶状体细胞正常的分化过程，而这一过程对于晶状体的透明度是必需的。
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