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Papers In Press, published online ahead of print November 1, 2004
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Department of Biochemistry, Cell Biology and Metabolism, Nagoya City University, Graduate School of Medical Sciences, Nagoya, Aichi 467-8601
Corresponding Author: syokoyam{at}med.nagoya-cu.ac.jp
Mechanism for assembly of high density lipoprotein (HDL) with cellular lipid by ATP binding cassette transporter A1 (ABCA1) and helical apolipoprotein was investigated in hepatocytes. Both HepG2 cells and mouse primary culture hepatocytes produced HDL with apolipoprotein A-I (apoA-I) whether endogenously synthesized or exogenously provided. Probucol, an ABCA1 inactivator, inhibited these reactions, as well as the reversible binding of apoA-I to HepG2. Primary-cultured heaptocytes of ABCA1-deficient mice also lacked the HDL-production regardless of the presence of exogenous apoA-I. HepG2 cells secreted apoA-I into the medium even when ABCA1 was inactivated by probucol, but it was all in a free form as HDL production is inhibited. When a lipid-free apoA-I-specific monoclonal antibody, 725-1E2, was present in the culture medium, production of HDL was suppressed, whether with endogenous or exogenously added apoA-I, while the antibody did not influence HDL already produced by HepG2 cells. We concluded that the main mechanism for HDL assembly by endogenous apoA-I in the HepG2 cells is an autocrine-like reaction in which apoA-I is secreted and then interact with cellular ABCA1 to generate HDL.{
Revised on November 1, 2004
Accepted on October 28, 2004
On the hepatic mechanism of HDL assembly by the ABCA1/apoA-I pathway
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