Function of a novel calcium-binding protein, visinin.

我们于1985年报道了visinin的分子量为24 kDa，是一种视锥细胞特异性蛋白。我们已经分离了visinin cDNA和其编码的蛋白质。我们还检测了visinin和抗visinin血清对蛙杆外节鸟苷酸环化酶活性的影响。用抗visinin血清从鸡视网膜神经元cDNA文库中分离Visinin cDNA。核苷酸序列分析表明，visinin具有三个E-F手形结构，是一种钙结合蛋白。Visinin蛋白在E.大肠杆菌具有钙结合活性.免疫印迹和免疫组化结果表明，visinin只存在于鸡视网膜锥体和松果体细胞中.从E.表达visinin的大肠杆菌和抗visinin血清对蛙r6 d外段鸟苷酸环化酶活性无影响.松果体培养物中的视素含量在光照下诱导增加4-8倍，而在黑暗中则无此作用.这些数据表明，visinin可能通过钙代谢参与视网膜锥细胞和松果体细胞的光转导。

We reported in 1985 that visinin is 24kDa and a cone specific protein. We have isolated visinin cDNA and characterized the encoded protein. We also examined the effect of visinin and anti-visinin serum on guanylate cyclase activity from frog rod outer segments.1. Visinin cDNA was isolated from chick retinal lambdagtll cDNA library, using anti-visinin serum. The nucleotide sequence revealed that visinin has three E-F hand structure and is a calcium binding protein. Visinin protein expressed in E. Coli exhibited Ca binding activity.2. Western blot and immunohistochemistry using an epitope-selected visinin antibody demonstrated that visinin exist only in the retinal cone and pinealocytes in chick.3. Visinin isolated from E. coli in which visinin was expressed and anti-visinin serum did not affect the activity of guanylate cyclase from frog r6d outer segments.4. The amounts of visinin in the pineal organ culture induced 4-8 folds in the light, but not in the dark.5. These data suggest that visinin may be involved in phototransduction in the retinal cone cell and pinealocytes through calcium metabolism.