Regulation of H^+-pump in Stomach by Protein Phosphorylation
| Project/Area Number |
09680608
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Functional biochemistry
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| Research Institution | HOKKAIDO UNIVERSITY |
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Principal Investigator |
IMAGAWA Toshiaki Grad.School of Sci., Hokkaido Univ., Asso.Pro., 大学院・理学研究科, 助教授 (20142177)
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| Project Period (FY) |
1997 – 1998
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| Project Status |
Completed (Fiscal Year 1998)
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| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,900,000)
Fiscal Year 1998: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 1997: ¥3,000,000 (Direct Cost: ¥3,000,000)
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| Keywords | H^+, K^+-ATPase / c-SRC / tyrosine kinase / protein Kinase C / protein phosphatase 1 / tyrosine phosphatase / stomach / acid secretion / H,K-ATPase / H^+,K^+-ATPase / プロトンポンプ / PKC / 壁細胞 / リン酸化 |
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| Research Abstract |
We identified the intrinsic tyrosine kinase and serine kinase, which phosphorylate Tyr^7 and Tyr^<10> and Ser^<27> in the alpha subunit of pig stomach H^+, K^+-ATPase as an c-SRC like protein tyrosine kinase and PKC alpha and BETAII, respectively. We found that an protein phosphatase 1 in the H+, K+-ATPase preparation dephosphorylate the phosphorylated Ser^<27> in alpha subunit of H^+, K^+-ATPase. We purified the protein tyrosine phosphatase, which specifically dephosphorylate the phosphorylated Tyr^7 and Tyr^<10>. The purified preparation contained two major proteins, whose molecular mass were about l40kDa and 65kDa.The amino terminal amino acid sequence analysis of these proteins revealed that the 65kDa protein was a pig serum albumin and the l40kDa protein might be a new protein tyrosine phosphatase. Using a glutathione S transferase fusion protein with the N-terminal domain of the a subunit of H^+, K^+-ATPase, we found the stomach-specific 35kDa protein interacted with this fusion protein.
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Report
(3 results)
Research Products
(8 results)
