Department of Cardiology, The First Affiliated Hospital, Shantou University Medical College, 57 Changping Road, 515041, Shantou, People's Republic of China.
Mol Biol Rep. 2010 Apr;37(4):1685-91. doi: 10.1007/s11033-009-9584-5. Epub 2009 Jun 21.
Gap junctions (GJs), collections of multiple intercellular channels between neighboring cells, are specialized channels facilitating intercellular electrical and chemical communication. GJs are important for synchronizing coupling and coordinated contraction in the heart, and are crucial regulators of heart gene transcription, cardiac development, and protection of ischemic cardiomyocytes through second messenger communication. Identification of proteins that interact with Connexin43 (Cx43), the predominant protein in cardiac GJs, may contribute to the understanding of GJ functional regulation. Using a yeast two-hybrid system, we identified Caveolin-3 (Cav3) as a new Cx43-interacting protein. This interaction was confirmed by co-immunoprecipitation and co-localization experiments. CX43 interacts with Cav3, suggesting that Cav3 may participate in the functional regulation of GJs.
缝隙连接(GJ)是相邻细胞之间的多个细胞间通道的集合,是促进细胞间电和化学通讯的特化通道。GJ 对于心脏的同步耦联和协调收缩很重要,并且通过第二信使通讯,是心脏基因转录、心脏发育和缺血性心肌细胞保护的重要调节剂。鉴定与间隙连接蛋白 43(Cx43)相互作用的蛋白质可能有助于理解 GJ 的功能调节。我们使用酵母双杂交系统鉴定出 Caviolin-3(Cav3)是 Cx43 的一种新的相互作用蛋白。通过共免疫沉淀和共定位实验证实了这种相互作用。CX43 与 Cav3 相互作用,表明 Cav3 可能参与 GJ 的功能调节。