Hsp27 suppresses the formation of inclusion bodies induced by expression of R120GαB-crystallin, a cause of desmin-related myopathy
Hsp27 suppresses the formation of inclusion bodies induced by expression of R120GαB-crystallin, a cause of desmin-related myopathy
复制标题
DOI：
10.1007/s00018-003-3024-9
复制
发表时间：
2003-06-01
影响因子：
8
通讯作者：
Kato, K
中科院分区：
文献类型：
--
作者：
Ito, H;Kamei, K;Kato, K
在一个患有结蛋白相关肌病的家系中发现了小热休克蛋白(SHSP)α-晶体蛋白R120G突变。在这项研究中，我们鉴定了在哺乳动物细胞中瞬时表达的R120GalphaB晶体蛋白的特征。此外，我们还研究了这个突变的α-晶体蛋白与另一种具有代表性的SHSP-Hsp27的相互作用。在HeLa细胞中，瞬时表达的R120GalphaB-晶状体蛋白主要存在于不溶组分中，而野生型α-晶状体蛋白主要存在于可溶组分中。在免疫荧光研究中，我们发现15%-25%的R120GalphaB-晶体蛋白表达细胞含有多个胞浆包涵体，其中Hsp27也定位于其中。当R120GalphaB-晶状体蛋白和Hsp27在HeLa细胞中瞬时共表达时，R120GalphaB-晶状体蛋白在可溶组分中的含量高于单独表达R120GalphaB-晶状体蛋白。此外，共表达减少了包涵体的形成，表明Hsp27是R120GalphaB-晶状体蛋白的分子伴侣。
The R120G mutation in the small heat shock protein (sHSP) alphaB-crystallin has been identified in a family suffering from desmin-related myopathy. In this study, we characterized the features of transiently expressed R120GalphaB-crystallin in mammalian cells. In addition, we examined interactions of this mutant alphaB-crystallin with Hsp27, another representative sHSP. In HeLa cells, transiently expressed R120GalphaB-crystallin was mainly fractionated in the insoluble fraction, although wild-type alphaB-crystallin was predominantly found in the soluble fraction. In immunofluorescence studies, we found 15-25% of R120GalphaB-crystallin-expressing cells to contain multiple cytosolic inclusion bodies, in which Hsp27 was also localized. When R120GalphaB-crystallin and Hsp27 were transiently co-expressed in HeLa cells, the amount of R120GalphaB-crystallin in the soluble fraction was greater than with expression of R120GalphaB-crystallin alone. Moreover, co-expression resulted in reduced formation of inclusion bodies, suggesting that Hsp27 acts as a molecular chaperone for R120GalphaB-crystallin.