S-modulin-like proteins in the retina.

在青蛙视网膜中，我们先前纯化了s -调素样蛋白s26。在本项目中，我们检查了(1)氨基酸序列，(2)组织定位，(3)s26的功能。此外，还研究了其他组织中发现的s -调素样蛋白的可能功能。(1) s26的氨基酸序列与S-modulin相同66%。令人惊讶的是，s26显示出77%的同源性，与鸡视网膜中视锥特异性钙结合蛋白visinin具有更高的同源性。(2)抗体产生s26特异性肽，染色青蛙视网膜的感光层。正信号在云层中的确切位置正在确定中。(3) s26的功能似乎与S-modulin相同。这一结论来自于s26在高钙浓度下抑制视紫红质磷酸化的发现，就像s -调节蛋白一样。(4)在大脑中发现了许多s -调质样蛋白，但其功能尚不清楚。我们检查了其中的7种蛋白质，发现所有7种蛋白质都显示出与s -调节蛋白相似的作用。这一发现有力地表明，这些蛋白在磷酸化反应中起钙依赖性调节作用。

In the frog retina, we previously purified an S-modulin-like protein, s26. In the present project, we examined (1) the aminoacid sequence, (2) the tissue localization and (3) the function of s26. In addition, the possible function of S-modulin-like proteins found in other tissues are studied.(1) The amino acid sequence of s26 is 66% identical to S-modulin. Surprisingly, s26 shows 77% identity, a higher homology to visinin, a cone specific calcium-biding protein in chick retina.(2) The antibody raised to a peptide specific to s26 stained a photoreceptor layr of the frog retina.The exact location of the positive signal in the layr is now in progress.(3) The function of s26 seems to be the same as that of S-modulin. This conclusion was drawn from the finding that s26 inhibited rhodopsin phosphorylation at high calcium concentrations as S-modulin does.(4) Many S-modulin-like proteins have been found in brain, but their functions are titally unknown. We examined 7 of these proteins and found that all of the 7 proteins tested showed a similar effect as S-modulin.This finding strongly suggests that these proteins function as a calciumdependent regulator of a phoshorylation reaction.