Calmodulin binds to chick lens gap junction protein in a calcium-independent manner.
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 others 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.
D000818:Animals; D002118:Calcium / Q000378:metabolism*; D002135:Calcium-Binding Proteins / Q000378:metabolism*; D002147:Calmodulin / Q000378:metabolism*; D002645:Chickens; D017630:Connexins; D005136:Eye Proteins / Q000378:metabolism*; D007365:Intercellular Junctions / Q000378:metabolism*; D007908:Lens, Crystalline / Q000378:metabolism* / Q000648:ultrastructure; D008565:Membrane Proteins / Q000378:metabolism*
D002135:Calcium-Binding Proteins; D002147:Calmodulin; D017630:Connexins; D005136:Eye Proteins; D008565:Membrane Proteins; D002118:Calcium