Potential involvement of dissociated apoA-I in the ABCA1-dependent cellular lipid release by HDL

Okuhira, Keiichiro; Tsujita, Maki; Yamauchi, Yoshio; Abe-Dohmae, Sumiko; Kato, Koichi; Handa, Tetsurou; Yokoyama, Shinji

doi:10.1194/jlr.m300257-jlr200

Cited by 56 publications

(49 citation statements)

References 48 publications

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“…Finally, we attempted to inactivate free apoA-I in the medium by trapping it using a monoclonal antibody to lipid-free apoA-I, 725-1E2 (15). As shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Probucol was kindly provided by Daiichi Pharmaceutical Co. LDL was isolated by sequential ultracentrifugation, and control and probucol-containing LDL were prepared by the method previously described (9). A monoclonal antibody (IgG) against lipid-free apoA-I, 725-1E2, was among the antibodies provided by Daiichi Pure Chemicals (Tokyo, Japan) and characterized in our laboratory as described previously (15). Mouse IgG was purchased from Chemicon International and used as a nonspecific control for 725-1E2.…”

Section: Apolipoprotein Lipoprotein and An Anti-apoa-i Monoclonal Amentioning

confidence: 99%

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On the hepatic mechanism of HDL assembly by the ABCA1/apoA-I pathway

Tsujita

Abe-Dohmae

et al. 2005

Journal of Lipid Research

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The mechanism for the assembly of HDL with cellular lipid by 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 hepatocytes of ABCA1-deficient mice also lacked 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 was 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, and the antibody did not influence HDL already produced by HepG2 cells. We conclude that the main mechanism for HDL assembly by endogenous apoA-I in HepG2 cells is an autocrine-like reaction in which apoA-I is secreted and then interacts with cellular ABCA1 to generate HDL. -Tsujita, M., C-A. Wu, S. AbeDohmae, S. Usui, M. Okazaki, and S. Yokoyama. On the hepatic mechanism of HDL assembly by the ABCA1/apoA-I pathway. J. Lipid Res. 2005. 46: 154-162.

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“…Finally, we attempted to inactivate free apoA-I in the medium by trapping it using a monoclonal antibody to lipid-free apoA-I, 725-1E2 (15). As shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

Section: Apolipoprotein Lipoprotein and An Anti-apoa-i Monoclonal Amentioning

confidence: 99%

On the hepatic mechanism of HDL assembly by the ABCA1/apoA-I pathway

Tsujita

Abe-Dohmae

et al. 2005

Journal of Lipid Research

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“…Finally, it was shown that a monoclonal antibody specific for lipid-free apoA-I selectively inhibited the ABCA1-dependent part of cell cholesterol release to HDL and that ABCA1-dependent binding to cells took place in HDL apoprotein but not HDL lipid (102). In that paper, kinetic analysis of the data indicated that apoA-I has affinity for HDL as high as that for the cellular surface, and spoA-I could still be transferred from HDL to the cell surface (Fig.…”

Section: How Does Hdl Remove Cell Cholesterol?mentioning

confidence: 99%

“…In hepatocytes (60), apoA-I is supplied from an authentic source in addition to extracellular origins, and produces HDL by the same mechanism in an autocrine manner. A monoclonal antibody selective against lipid-free apoA-I, 725-1E2, blocked the production of HDL in both cases (60,102).…”

Section: Autocrine Reaction For Hdl Biogenesismentioning

confidence: 99%

ABCA1 and Biogenesis of HDL

Yokoyama

2006

JAT

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“…In particular, cholesterol-overloaded macrophages, one of the foremost players in atherosclerosis progression (28,29), primarily efflux excess cholesterol through an ABCA1-dependent mechanism (30,31). The main extracellular recipient of ABCA1-mediated cholesterol release is lipid-free apoA-I (32,33), and minimal lipidation of apoA-I greatly reduces its ABCA1-mediated cholesterol release efficiency (34 -37).…”

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confidence: 99%

Impact of Self-association on Function of Apolipoprotein A-I

Jayaraman

Abe-Dohmae

Yokoyama

et al. 2011

Journal of Biological Chemistry

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Background: Self-association is an intrinsic property of exchangeable apolipoproteins but an under-explored feature of the major protein of good cholesterol, apolipoprotein A-I. Result: Different degrees of apolipoprotein A-I self-association exhibit distinct in vitro lipid remodeling and cellular lipid release efficiencies. Conclusion: Self-association of apolipoprotein A-I modulates the biogenesis of high density lipoprotein. Significance: This is the first study to demonstrate that self-association of apolipoprotein A-I attunes key steps in reverse cholesterol transport.

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Potential involvement of dissociated apoA-I in the ABCA1-dependent cellular lipid release by HDL

Cited by 56 publications

References 48 publications

On the hepatic mechanism of HDL assembly by the ABCA1/apoA-I pathway

On the hepatic mechanism of HDL assembly by the ABCA1/apoA-I pathway

ABCA1 and Biogenesis of HDL

Impact of Self-association on Function of Apolipoprotein A-I

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