Role of cell surface H+-ATP synthase on adipocyte differentiation
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概要
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The H<SUP>+</SUP>-ATP synthase has been found in all energy transducing membranes such as mitochondria and chloroplasts, and catalyzes the synthesis of ATP with the energy that derives from electron transfer in the respiratory or photosynthetic electron transport chains. Recent studies, however, have shown that some of its subunits localize in the plasma membrane of neoplastic, endothelial, and hepatic cells. Moreover, it has been proposed that the enzyme may be a receptor for ligands such as angiostatin and apolipoprotein A-1 in endothelial and hepatic cells, respectively. Along the same line, Moser et al. and we showed that cell surface H<SUP>+</SUP>-ATP synthase is active in ATP synthesis and small molecular substances targeting F1 subunit complex of H<SUP>+</SUP>-ATP synthase, inhibit proliferation, migration, and tube formation in Matrigel of HUVECs, suggesting that the activity of cell surface H<SUP>+</SUP>-ATP synthase contributes to regulation of angiogenesis. In addition to these findings, we recently found that the expression of the cell surface H<SUP>+</SUP>-ATP synthase complex was markedly increased during adipocyte differentiation and that the treatment of differentiated 3T3-L1 adipocytes with H<SUP>+</SUP>-ATP synthase inhibitors leads to the decrease in the cytosolic lipid droplet accumulation. The present results show that cell surface H<SUP>+</SUP>-ATP synthase has a previously unsuspected role on lipid metabolism. This paper briefly reviews the recent evidence for a role of cell surface H<SUP>+</SUP>-ATP synthase on lipid metabolism in adipocytes.
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