合成ペプチドによる抗コネクシン32抗体の作製とそれを用いた肝細胞 Gap Junction の研究
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概要
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Gap junctions are specialized membrane channels comprised of 6 connexin molecules and play an important role in intercellular communication between cells in contact. Connexin 32(Cx 32) has been isolated as the major hepatocyte gap junction protein. To study the changes of gap junctions in hepatocytes under various pathologic conditions, we developed a polyclonal antibody against synthetic peptides of the intracytoplasmic domain of the Cx 32 molecule. The specificity of the antibody was confirmed by immunoelectronmicroscopy and Western blot analysis. In order to examine the relation between Cx32 expression and hepatocyte proliferation, immunofluorescent examination of Cx32 in nomal and regenerating liver of rat and mouse was performed. Normal rat and mouse hepatocytes showed around 10 dot-like positive stainings on the cell membrane, however, staining of Cx 32 gradually decreased and almost disappeared in accordance with stage of DNA syn- thesis in regenerating liver of both rat and mouse. Northern blot analysis revealed that a decrease of Cx32 mRNA had already occurred before DNA synthesis. Sequential changes in the staining of Cx 32 in cultured hepatocytes after plating were also examined. The Cx32 positive dots gradually decreased in number and disappeared at 24hr after plating. We examined the effects of the antibody on intercellular communication by microinjection of the antibody and Lucifer Yellow in couplet he- patocytes. The results demonstrated that the injection of antibody inhibited intercellular communi- cation between couplet hepatocytes, suggesting the importance of the intracytoplasmic domain of Cx 32 for regulation of gap junction function.
- 札幌医科大学の論文
- 1991-12-01
札幌医科大学 | 論文
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