2000 Fiscal Year Final Research Report Summary
Structure, function and regulation of the Na^+/H^+ exchanger
| Project/Area Number |
11680650
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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 | National Cardiovascular Center Research Institute |
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Principal Investigator |
WAKABAYASHI Shigeo Department of Molecular Physiology National Cardiovascular Center Research Institute Senior Investigator, 循環分子生理部, 室長 (70158583)
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| Project Period (FY) |
1999 – 2000
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| Keywords | Na^+ / H^+ exchanger / membrane topology / mutagevesis / Volume regulation / Calcineurin-homologous protein / lithium ion |
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| Research Abstract |
Mammalian Na^+/H^+ exchanger (NHE) is a ubiquitous plasma membrane transporter that regulates intracellular pH and cell volume, and epithelial absorption of Na^+ and bicarbonate in kidney and intestine. During 2 years, we studied about structure-function and regulatory mechanism of NHE, and obtained following results.
1. We discovered that one of exchanger-binding proteins, calcineurin-homologous protein (CHP) is an essential cofactor for physiological activity of multiple exchanger isoforms (JBC, 2001, in press).
2. Based on cysteine accessibility analysis, we presented a novel topology model of NHE1 (JBC, 2000).
3. We identified critical amino acid residues important for plasma membrane expression of NHE1 and found that second mutations at several positions rescued surface expression of NHE1 (FEBS letters, 2000).
4. We found that Li^+ ion is an activator of NHE isoforms NHE1 and NHE2, and tyrosine kinase may be involved in this activation process (Pflugers Archiv. 2000).
5. We found that the extracellular loop is responsible for different volume sensitivity of NHE1 and NHE2 (submitted).
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Research Products
(14 results)
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[Publications] Anzai, N., Suzuki, N., Izumida, I., Saito, J., Wakabayashi, S., Shigekawa, M., and Kawahara, K.: "Hyperosmolality increases expression of a Na^+/H^+ exchanger isoform NHE1, but not NHE4 in cultured rat kidney inner medullary collecting duct."In "Control and Diseases of Sodium Dependent Transport Proteins and Ion Channels", edited by Y.Suketa et al. Elsevier Publishers. 129-131 (2000)
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