1992 Fiscal Year Final Research Report Summary
Modulation of ectoenzyme-gene expression in volving reformation of bile-canalicular structures in rat primary cultured hepatocytes
Project/Area Number |
02670304
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Research Category |
Grant-in-Aid for General Scientific Research (C)
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Allocation Type | Single-year Grants |
Research Field |
Gastroenterology
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Research Institution | Tottori University |
Principal Investigator |
IKAWA Shiro Division of Chemistry, Institute of Steroid Research, Tottori University School of Medicine, Professor, 医学部, 教授 (70032183)
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Co-Investigator(Kenkyū-buntansha) |
KOHARA Hiromi Division of Chemistry, Institute of Steroid Research, Tottori University School, 医学部, 助手 (40032221)
MURA Tetsuo Division of Chemistry, Institute of Steroid Research, Tottori University School, 医学部, 講師 (80093631)
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Project Period (FY) |
1990 – 1992
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Keywords | Primary cultured of rat hepatocytes / Bile canalicular reformation / Cell membrane polarity / Bile canalicular ectoenzyme / Taurocholate binding assay / Bile acid carrier protein / Labeling of bile acid carrier protein |
Research Abstract |
The isolated hepatocytes membranes and bile-canalicular structures are damaged by collagenase digestion. These damages, however, are almost completely repaired when the hepatocytes are cultured as monolayers for only 24hr. Moreover, we found that the suppressive effects of insulin on bile-canalicule reformation or alkaline phosphatase induction by dexamethasone were due to decrease and the suppression of synthesis of alkaline mRNA, not to enhacement of its degradation. However, the relation to this enzyme induction is still unknown. Therefore, further studies are necessary for the regulatory gene of this enzyme and the characterization of the transmitter molecules and/or effector molecules involved in transcription and their interaction with genetic structure. On the other hand, the bile acid binding protein checked by [^<14>C]taurocholate is distributed mainly on the surface of the bile canalicule. This binding protein from rat liver plasma membrane was fractionated by Sephacryl S-200 column ; molecular weight is 100kD, 60kD and 48kD, respectively. This binding protrin (100kD) was mainly found from sinusoidsite. This is in accordance with intracellular for bile acid transport.
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