Cx30.2可与其他心脏缝隙连接蛋白形成异质间隙连接通道
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Cx30.2 can form heteromeric gap junction channels with other cardiac connexins
背景与目的
因为心脏中的大多数细胞共同表达多种连接蛋白，我们研究了转染细胞中连接蛋白30.2与连接蛋白40、连接蛋白43或连接蛋白45之间的异质相互作用。
方 法
双标记免疫荧光显微镜观察表明，连接蛋白30.2与每个共同表达的连接蛋白广泛共定位在端膜上。当Triton x-100溶解连接子从共表达细胞中亲和纯化时，连接蛋白30.2与连接蛋白40、连接蛋白43或连接蛋白45一起被分离出来。
结 果
连接蛋白30.2与连接蛋白40、连接蛋白43和连接蛋白45的共同表达并不能显著降低总连接电导。在共表达连接蛋白30.2和连接蛋白43或连接蛋白45的细胞中，缝隙连接通道在单独的连接蛋白之间表现出电压依赖性的门控特性。与之形成对照的是，当与连接蛋白40共同表达时，连接蛋白30.2主导电压依赖性。
结 论
我们的数据表明，连接蛋白30.2可以与其他心脏连接蛋白形成异质体，并且在共同表达这些连接蛋白的心脏区域，这种混合通道的形成将影响缝隙连接的门控特性。
原始文献摘要
Gemel J1, Lin X, Collins R, et al. Cx30.2 can form heteromeric gap junction channels with other cardiac connexins. Biochem Biophys Res Commun. 2008 May 2;369(2):388-94. doi: 10.1016/j.bbrc.2008.02.040. Epub 2008 Feb 20.
Abstract:Since most cells in the heart co-express multiple connexins, we studied the possible heteromeric interactions between connexin30.2 and connexin40, connexin43 or connexin45 in transfected cells.Double label immunofluorescence microscopy showed that connexin30.2 extensively co-localized with each co-expressed connexin at appositional membranes. When Triton X-100 solubilized connexons were affinity purified from co-expressing cells, connexin30.2 was isolated together with connexin40, connexin43, or connexin45. Co-expression of connexin30.2 with connexin40,connexin43, or connexin45 did not significantly reduce total junctional conductance. Gap junction channels in cells co-expressing connexin30.2 with connexin43 or connexin45 exhibited voltage-dependent gating intermediate between that of either connexin alone. In contrast, connexin30.2 dominated the voltage dependence when co-expressed with connexin40. Our data suggest that connexin30.2 can form heteromers with the other cardiac connexins and that mixed channel formation will influence the gating properties of gap junctions in cardiac regions that co-express these connexins.
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