Calmodulin binds to chick lens gap junction protein in a calcium-independent manner.
Calmodulin binds to chick lens gap junction protein in a calcium-independent manner.
复制标题
钙调蛋白以不依赖于钙的方式与鸡晶状体间隙连接蛋白结合。
DOI：
10.1126/science.6280283
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发表时间：
1982
期刊：
影响因子：
--
通讯作者：
Maisel,H
中科院分区：
文献类型：
--
作者：
Welsh,MJ;Aster,JC;Ireland,M;Alcala,J;Maisel,H
合成了一种具有生物化学活性的钙调素-四甲基罗丹明异硫氰酸酯偶联物（CaM-RITC）。当与鸡透镜切片一起孵育时，该缀合物在无钙存在下结合于透镜纤维细胞的表面膜。透镜切片与透镜的间隙连接蛋白的抗体一起孵育完全阻断了缀合物与细胞膜的结合，而来自未免疫动物的血清或其它透镜蛋白的抗体仅略微降低了结合。通过凝胶覆盖程序，发现125 I标记的钙调素结合差距连接蛋白的透镜，也在钙非依赖性的方式。这些结果支持了钙调素可能与活细胞中的间隙连接相互作用并调节间隙连接的概念。
A biochemically active conjugate of calmodulin and tetramethylrhodamine isothiocyanate (CaM-RITC) was synthesized. When incubated with sections of chick lens, this conjugate bound to the surface membranes of lens fiber cells in the presence of absence of calcium. Incubation of lens sections with antibodies to gap junction protein of lens completely blocked the binding of the conjugate to cell membranes, whereas serum from nonimmunized animals or antibodies to other lens proteins reduced the binding only slightly. By means of a gel overlay procedure,125I-labeled calmodulin was found to bind to the gap junction protein of lens, also in a calcium-independent manner. These results support the concept that calmodulin may interact with and regulate gap junctions in living cells.