Function of a novel calcium-binding protein, visinin.

1985年我们报道了Visinin全长24 kDa，是一种锥体特异性蛋白。我们已经分离到visinin基因，并对其编码蛋白进行了鉴定。我们还检测了粘附素和抗粘附素血清对蛙杆外节鸟苷环化酶活性的影响。用抗Visinin血清从鸡视网膜lambdagtll基因文库中分离到Visinin基因。核苷酸序列分析表明，Visinin具有三个E-F手型结构，是一种钙结合蛋白。结论：1.在大肠杆菌中表达的Visinin蛋白具有钙结合活性。免疫印迹和免疫组织化学显示，在鸡的视网膜锥体和松果体细胞中，仅存在视黄素。从表达Visinin和抗Visinin血清的大肠杆菌中分离的Visinin不影响青蛙R6d外节段鸟苷环化酶的活性。松果体培养中Visinin的含量在光照条件下诱导4-8倍，而在黑暗条件下不诱导。这些数据表明，Visinin可能通过钙代谢参与视网膜锥体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.