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Study of the low molecular weight GTP binding proteins in amylase exocytosis of parotid acini in vitro.

Research Project

Project/Area Number 06672016
Research Category

Grant-in-Aid for General Scientific Research (C)

Allocation TypeSingle-year Grants
Research Field Surgical dentistry
Research InstitutionHealth Sciences University of Hokkaido

Principal Investigator

OKUMURA Kazuhiko  1st Dept.Oral & Maxillofacial Surg. Assist.Prof., 歯学部, 講師 (60194510)

Co-Investigator(Kenkyū-buntansha) TOMIOKA Keiko  1st Dept.Oral & Maxillofacial Surg.Staff, 歯学部, 助手 (10227613)
Project Period (FY) 1994 – 1995
Project Status Completed (Fiscal Year 1995)
Budget Amount *help
¥1,900,000 (Direct Cost: ¥1,900,000)
Fiscal Year 1995: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 1994: ¥1,000,000 (Direct Cost: ¥1,000,000)
Keywordsexocytosis / low mr GTP binding proteins / Parotid / secretory granule membranes / rho proteins / 低分子量GTP結合蛋白質
Research Abstract

The trimeric GTP binding protein plays it as information and/or transformation factor on the plasma membranes. But existence of low molecular weight GTP binding protein which expressed in cytosol fraction. Futhermore, it is inserted in the secretory granule membranes in secretory cell and as member of constitution. So, low molecular weight GTP binding protein in parotid acinar cell exists in secretory granule membranes, and is which associated with amylase secretion. We examined whether playd it. Secretory granules of rat parotid glands were isolated by percoll-gradient centrifuges as described by Hopfer et al. We report here that at least 21ow molecular GTP-binding proteins (21 kD-25 kD) are associated with the plasma membrane and secretory granule membranes from rat parotid acini by [32 [-GTP overlay assay.
Results
1. The secretory granules isolated by rat parotid tissues. Western blotting analysis of the rho proteins. The rho protein A and B localized the plasma menbranes and secretory granule membranes as molecular weight at 21 kD.
2. Inactivation of rho p21 of parotid acini by ADP-rybosiltransferase C3 resulted in the inhibited release of amylase, suggesting that amylase secretion was mediated by rho p21.

Report

(3 results)
  • 1995 Annual Research Report   Final Research Report Summary
  • 1994 Annual Research Report

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Published: 1994-04-01   Modified: 2016-04-21  

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