1991 Fiscal Year Final Research Report Summary
Function of a novel calcium-binding protein, visinin.
| Project/Area Number |
02454135
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
General pharmacology
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| Research Institution | Osaka University |
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Principal Investigator |
MIKI Naomasa Osaka University Medical School Professor, 医学部, 教授 (40094445)
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| Co-Investigator(Kenkyū-buntansha) |
TANIURA Hideo Osaka University Medical School, 医学部, 医員
OSUGI Takeshi Osaka University Medical School Assis. Prof., 医学部, 助手 (50176880)
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| Project Period (FY) |
1990 – 1991
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| Keywords | visinin / cDNA Cloning / retina / pineal / light / calcium / guanylate cyclase |
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| Research Abstract |
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.
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