| Project/Area Number |
59480099
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
General physiology
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| Research Institution | Kansai Medical University |
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Principal Investigator |
TASHIRO Yutaka Kansai Medical University, School of Medicine, 医学部, 教授 (40077558)
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| Co-Investigator(Kenkyū-buntansha) |
YOSHIMORI Tamotsu Kansai Meidical University, School of Medicine, 医学部, 助手 (60191649)
YAMAMOTO Akitsugu Kansai Meidical University, School of Medicine, 医学部, 助手 (30174775)
MASAKI Ryuichi Kansai Meidical University, School of Medicine, 医学部, 助手 (70140283)
OMORI Koichiro Kansai Meidical University, School of Medicine, 医学部, 助教授 (80094465)
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| Project Period (FY) |
1984 – 1986
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| Project Status |
Completed (Fiscal Year 1986)
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| Budget Amount *help |
¥6,700,000 (Direct Cost: ¥6,700,000)
Fiscal Year 1986: ¥1,200,000 (Direct Cost: ¥1,200,000)
Fiscal Year 1985: ¥1,200,000 (Direct Cost: ¥1,200,000)
Fiscal Year 1984: ¥4,300,000 (Direct Cost: ¥4,300,000)
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| Keywords | ( <Na^+> , <K^+> )ATPase / hepatocyte / exocrine pancreatic cell / parotide acinar cell / cell polarity / 生合成 / プロセッシング |
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| Research Abstract |
We purified holo( <Na^+> , <K^+> )ATPase from canine and rat kidney outer medulla and prepared monospecific antibody against the ATPase. We investigated the distribution of the ATPase in canine hepatocytes, rat exocrine pancreatic cells and rat parotid cells, and also biosynthesis and processing of the ATPase in rat kidney.
1) In canine hepatocytes, ( <Na^+> , <K^+> )ATPase was found not only on the sinusoid-lateral surface but also on the bile canalicular surface and the surface density on the latter was 2.5 times higher than that on the former.
2) In the exocrine pancreatic cells, the ATPase was found on the luminal surface of not only acinar cells but also ductal cells, and we suggested that the ATPase actively participates in the formation of the pancreatic fluids.
3) In the parotid acinar cells, a small but significant amount of ( <Na^+> , <K^+> )ATPase was found on the luminal surface. In the duct cells, however, the ATPase was distributed exclusively on the basal plasma membrane, especially on the well developed basal infoldings.
4) Biosynthesis of the ATPase in rat kidney was investigated by labeling with <^(35)S> -Met and it was revealed that the <beta> subunit (38K) was cotranslationally glycosylated in the ER to form the 50 K high-mannose type glycoprotein and then converted to the 54 K complex type glycoprotein. The molecular weight of the <alpha> subunit (95 K) did not change throughout the intracellular transport and processing.
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