Suppr超能文献

在成年哺乳动物晶状体上皮细胞中含有α8-连接蛋白(MP70)的间隙连接表明需要重新评估其在晶状体中的作用。

Gap junctions containing alpha8-connexin (MP70) in the adult mammalian lens epithelium suggests a re-evaluation of its role in the lens.

作者信息

Dahm R, van Marle J, Prescott A R, Quinlan R A

机构信息

Department of Biochemistry, Medical Sciences Institute, University of Dundee, Dundee, DD1 4HN, UK.

出版信息

Exp Eye Res. 1999 Jul;69(1):45-56. doi: 10.1006/exer.1999.0670.

Abstract

A missense mutation in one of the three lens connexins, alpha8-connexin, has been recently shown to be the genetic basis of the zonular pulverant lens cataract. This connexin had been considered to be expressed only in lens fibre cells. The present studies show that alpha8-connexin is also expressed in the lens epithelial cell layer. For this study, the distribution of gap junctions in the adult bovine lens has been investigated by confocal immunofluorescence microscopy using antibodies against alpha8-connexin (MP70) and alpha1-connexin (Cx43). In addition to the anticipated localisation of alpha8-connexin to the broad faces of lens fibre cells as reported in other species, alpha8-connexin was also found colocalized with alpha1-connexin at plaques in the lateral epithelial-epithelial plasma membranes of the bovine lens. These data suggest that mixed alpha8-connexin/alpha1-connexin plaques are between epithelial cells at their apico-lateral plasma membranes, rather than between epithelial and fibre cells. Indeed, freeze fracture analyses of the epithelial-fibre cell interface failed to reveal gap junctions connecting the epithelium and the underlying fibre cells. Importantly, microdissection and subsequent immunoblotting of lens epithelium samples confirmed the immunolocalisation results. The data suggest mature mammalian lens epithelial cells could form either heteromeric, heterotypic and/or mixed homomeric-homotypic gap junctional complexes with unique physiological properties, an important point when considering the role of epithelial cell connexins in cataractogenesis.

摘要

最近研究表明,三种晶状体连接蛋白之一的α8-连接蛋白中的一个错义突变是带状粉末状晶状体白内障的遗传基础。这种连接蛋白一直被认为仅在晶状体纤维细胞中表达。目前的研究表明,α8-连接蛋白也在晶状体上皮细胞层中表达。在本研究中,使用抗α8-连接蛋白(MP70)和抗α1-连接蛋白(Cx43)抗体,通过共聚焦免疫荧光显微镜研究了成年牛晶状体中缝隙连接的分布。除了如在其他物种中报道的α8-连接蛋白预期定位于晶状体纤维细胞的宽面外,还发现α8-连接蛋白与α1-连接蛋白在牛晶状体外侧上皮-上皮质膜的斑块中共定位。这些数据表明,混合的α8-连接蛋白/α1-连接蛋白斑块位于上皮细胞顶端-外侧质膜之间,而不是上皮细胞与纤维细胞之间。事实上,对上皮-纤维细胞界面的冷冻断裂分析未能揭示连接上皮细胞和下方纤维细胞的缝隙连接。重要的是,对晶状体上皮细胞样本进行显微切割并随后进行免疫印迹,证实了免疫定位结果。数据表明,成熟的哺乳动物晶状体上皮细胞可以形成具有独特生理特性的异聚体、异型和/或混合同聚体-同型缝隙连接复合物,这在考虑上皮细胞连接蛋白在白内障发生中的作用时是一个重要观点。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验