1994 Fiscal Year Final Research Report Summary
Lens protein related disufide bond and complex
| Project/Area Number |
05671474
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
Ophthalmology
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| Research Institution | Showa University |
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Principal Investigator |
IIJIMA Takeru Showa University School of Medicine Assistant professor, 医学部, 助教授 (10053951)
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| Project Period (FY) |
1993 – 1994
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| Keywords | Cataract / GSH / Mixed disulfide / Thilate anion / Lens pretein / Amino acid / ICR rat / ^<14>C-cystine |
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| Research Abstract |
The study was designed to investigate the formation of mixed disulfide of protein in the rat lens. We compared the accumulation of ^<14>C-cystine, ^3H-leucine, ^<14>C-glycine and ^<35>S-methionine in inherited cataractous rat lens (ICR/f) during cataractogenisis with Wistar strain rat. The accumulation of ^<14>C-cystine in water insoluble protein (WIP) of lens were increased, especially in lens recognized cataract. The radioactivity accumulated into the WIP were released by incubating with 2-mercaptoethanol, dithiothretol and reduced gluthathione.
It was assumed that the accumulation of ^<14>C-cystine were related to the formation of protein-disulfide of lens protein.
The accumulation of ^<14>C-cystine in water insoluble protein of cataract lens induced by stretozotocin were increased, but in transparent lens.
This result was not accepted in the cataract lens induced for maleic acid disulfide ester.
From this result, it seems that formation of lens protein disulfide and thiolate anion is not formed for a short time like in vitro cataract but for a long time like senile it.
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