1996 Fiscal Year Final Research Report Summary
Molecular Mechanism in Mobilization of Proton Pump to Apical Cell Membrane of Gastric Parietal Cells
| Project/Area Number |
06454149
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
General physiology
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| Research Institution | University of Occupational and Environmental Health |
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Principal Investigator |
KAWAMURA Masaru Univ. of Occup and Environ. Health, School of Medicine, Professor, 医学部, 教授 (00049066)
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| Co-Investigator(Kenkyū-buntansha) |
OHNO Koki Univ. of Occup and Environ. Health, School of Medicine, Professor, 医学部, 教授 (30049085)
TAKEDA Kazuo Univ. of Occup and Environ. Health, School of Medicine, Assistant Professor, 医学部, 講師 (70131927)
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| Project Period (FY) |
1994 – 1996
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| Keywords | H^+ / K^+-ATPase / Na^+ / K^+-ATPase / chimera / oocyte |
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| Research Abstract |
The molecular mechanism involved in targeting of proton pump molecules to apical cell membrane of gastric parietal cells was studied. The Na-pump that is restricted basolaterally was examined in contrast.
1. Assembly of the alpha-and beta-subunits is pre-requisite for targeting of the alpha-subunit to cell membranes. The disulfide-bonded loops in the extracellular domain of the beta-subunit and N-terminal domain of the alpha-subunit are involved in the assembly.
2. The beta-subunit is interchangable between proton-and Na-pumps with respect to assembly with the alpha-subunit, but resulting hibrids are functionally inactive.Chimeric beta-subunits were constructed in order to assign specific site (s) of each beta-subunit. The specific sites are distributed in the extracellular domain of the beta-subunit.
3. The first disulfide-bonded loop (L_1) in the extracellular domain is one of the specific sites. The 148th amino acid residue within L_1 is especially important.
4. These results are summarized in our review.
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