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

Tsujita, Maki, Wu, Cheng-Ai, Abe-Dohmae, Sumiko, Usui, Shinichi, Okazaki, Mitsuyo, Yokoyama, Shinji·2005·Journal of Lipid Research
DOI 10.1194/jlr.m400402-jlr200
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Fig. 1 Apolipoprotein-mediated lipid release from HepG2 cell. Cells were incubated for 16 h with minimum essential medium Eagle 𝛂 modification (MEM𝛂 ) containing 0.02% BSA and the indicated concentration of apolipoprotein A-I (apoA-I) or apoA-II. Cellular lipid released into the conditioned medium was extracted by organic solvent and analyzed by colorimetric enzymatic assay for cholesterol and choline-phospholipid as described. The values represent means ± SEM for three determinations. Open circles, exogenous human apoA-I; open squares, exogenous human apoA-II.
Fig. 1 Apolipoprotein-mediated lipid release from HepG2 cell. Cells were incubated for 16 h with minimum essential medium Eagle 𝛂 modification (MEM𝛂 ) containing 0.02% BSA and the indicated concentration of apolipoprotein A-I (apoA-I) or apoA-II. Cellular lipid released into the conditioned medium was extracted by organic solvent and analyzed by colorimetric enzymatic assay for cholesterol and choline-phospholipid as described. The values represent means ± SEM for three determinations. Open circles, exogenous human apoA-I; open squares, exogenous human apoA-II.CC-BY · From the PDF
Fig. 2 Lipoprotein analysis of the culture medium of HepG2 cells by HPLC. Cells were incubated with MEM𝛂 containing 0.02% BSA with (B, D, F) or without (A, C, E) 10 𝛍 g/ml human apoA-I for 16 h. The conditioned medium of HepG2 cells (100 𝛍 l) was analyzed by the HPLC lipoprotein analysis system using two tandem gel-permeation columns (Lipopropak XL; 7.8 mm × 300 mm; Tosoh). The elution profile was monitored by an online assay system for total cholesterol (solid lines) and triacylglycerol (dotted lines). A and B: Whole conditioned medium. C and D: d > 1.063 g/ml fraction. E and F: d < 1.063 g/ml fraction. The eluting positions of human plasma VLDL, LDL, and HDL are indicated by arrows in A.
Fig. 2 Lipoprotein analysis of the culture medium of HepG2 cells by HPLC. Cells were incubated with MEM𝛂 containing 0.02% BSA with (B, D, F) or without (A, C, E) 10 𝛍 g/ml human apoA-I for 16 h. The conditioned medium of HepG2 cells (100 𝛍 l) was analyzed by the HPLC lipoprotein analysis system using two tandem gel-permeation columns (Lipopropak XL; 7.8 mm × 300 mm; Tosoh). The elution profile was monitored by an online assay system for total cholesterol (solid lines) and triacylglycerol (dotted lines). A and B: Whole conditioned medium. C and D: d > 1.063 g/ml fraction. E and F: d < 1.063 g/ml fraction. The eluting positions of human plasma VLDL, LDL, and HDL are indicated by arrows in A.CC-BY · From the PDF
Fig. 3 Analysis of lipoprotein generated by mouse primary culture hepatocytes. Primary culture hepatocytes of C57Bl/6 mice were harvested using the Hanks'-EDTA and collagenase two-medium method described in Materials and Methods. The cells were incubated in DMEM (high glucose)/BSA medium with or without human apoA-I for 16 h. The conditioned medium was separated by ultracentrifugation at a density 1.063 g/ml. The data represent means ± SEM of three determinations. Difference in HDL between control and apoA-I ( + ) is significant by P < 0.005.
Fig. 3 Analysis of lipoprotein generated by mouse primary culture hepatocytes. Primary culture hepatocytes of C57Bl/6 mice were harvested using the Hanks'-EDTA and collagenase two-medium method described in Materials and Methods. The cells were incubated in DMEM (high glucose)/BSA medium with or without human apoA-I for 16 h. The conditioned medium was separated by ultracentrifugation at a density 1.063 g/ml. The data represent means ± SEM of three determinations. Difference in HDL between control and apoA-I ( + ) is significant by P < 0.005.CC-BY · From the PDF
Fig. 4 The effect of ABCA1 inactivation on the generation of HDL by hepatocytes as analyzed by HPLC. A-D: HepG2 cells. A: The conditioned medium of HepG2 cells after 16 h. B: The conditioned medium incubated with apoA-I (10 𝛍 g/ml) for 16 h. C: The conditioned medium of probucol-loaded HepG2 cells after 16 h. D: The conditioned medium of probucol-loaded HepG2 cells with apoA-I (10 𝛍 g/ml) for 16 h. E-F: Primary cultured hepatocytes. E: The conditioned medium of the hepatocytes isolated from an ABCA1deficient mouse after 16 h of incubation. F: The conditioned medium of the hepatocytes of an ABCA1-deficient mouse after incubation with apoA-I (10 𝛍 g/ml) for 16 h. G: The conditioned medium of the hepatocytes obtained from C57Bl/6 mice fed with control chow after 16 h of incubation. H: The conditioned medium of the hepatocytes obtained from C57Bl/6 mice fed with 0.5% probucolcontaining chow. The medium was analyzed by HPLC using two tandem gel-permeation columns (Lipopropak XL; 7.8 mm × 300 mm; Tosoh) to yield the lipoprotein profiles as described in the text. Solid lines represent cholesterol, dotted lines represent triglyceride, and dot-and-broken lines (in E and F) represent cholinephospholipid. Arrows with a solid line, a thick broken line, and a thin broken line indicate the eluting positions of plasma HDL, LDL, and VLDL, respectively. Pseudopeaks generated by the color of the medium caused baseline shifts in the analysis of the primary culture medium as the sensitivity of the monitoring lipid was increased. KO, knockout.
Fig. 4 The effect of ABCA1 inactivation on the generation of HDL by hepatocytes as analyzed by HPLC. A-D: HepG2 cells. A: The conditioned medium of HepG2 cells after 16 h. B: The conditioned medium incubated with apoA-I (10 𝛍 g/ml) for 16 h. C: The conditioned medium of probucol-loaded HepG2 cells after 16 h. D: The conditioned medium of probucol-loaded HepG2 cells with apoA-I (10 𝛍 g/ml) for 16 h. E-F: Primary cultured hepatocytes. E: The conditioned medium of the hepatocytes isolated from an ABCA1deficient mouse after 16 h of incubation. F: The conditioned medium of the hepatocytes of an ABCA1-deficient mouse after incubation with apoA-I (10 𝛍 g/ml) for 16 h. G: The conditioned medium of the hepatocytes obtained from C57Bl/6 mice fed with control chow after 16 h of incubation. H: The conditioned medium of the hepatocytes obtained from C57Bl/6 mice fed with 0.5% probucolcontaining chow. The medium was analyzed by HPLC using two tandem gel-permeation columns (Lipopropak XL; 7.8 mm × 300 mm; Tosoh) to yield the lipoprotein profiles as described in the text. Solid lines represent cholesterol, dotted lines represent triglyceride, and dot-and-broken lines (in E and F) represent cholinephospholipid. Arrows with a solid line, a thick broken line, and a thin broken line indicate the eluting positions of plasma HDL, LDL, and VLDL, respectively. Pseudopeaks generated by the color of the medium caused baseline shifts in the analysis of the primary culture medium as the sensitivity of the monitoring lipid was increased. KO, knockout.CC-BY · From the PDF
Fig. 5 Effect of probucol loading on apoA-I-mediated cellular lipid release from HepG2 cells and exchangeable binding apoA-I to HepG2 cells. A and B: Lipid release. HepG2 cells were incubated with either control LDL or probucol-containing LDL for 24 h. Cellular cholesterol and phospholipid release were measured after incubation for 16 h with various amounts of apoA-I. HDL-cholesterol (A) and HDL-phospholipid (B) were determined by an HPLC system. Open squares, control LDL-loaded cells; open circles, probucol-LDL loaded cells. C: ApoA-I binding. The indicated amounts of 125 I-apoA-I-incubated HepG2 cells were preloaded with control LDL or probucol-containing LDL for 2 h at 4 ° C. The cells were washed two times with ice-cold PBS, and the bound 125 I-apoA-I was displaced two times by 50 𝛍 g/ml nonlabeled apoA-I for 9 h. The difference in the total radioactivity after the first washing and after the second displacement was calculated as displaceable or exchangeable binding of apoA-I to the cells. Squares, binding to the cells loaded with control LDL; circles, binding to the cells loaded with probucol-containing LDL. Error bars indicate ± SEM.
Fig. 5 Effect of probucol loading on apoA-I-mediated cellular lipid release from HepG2 cells and exchangeable binding apoA-I to HepG2 cells. A and B: Lipid release. HepG2 cells were incubated with either control LDL or probucol-containing LDL for 24 h. Cellular cholesterol and phospholipid release were measured after incubation for 16 h with various amounts of apoA-I. HDL-cholesterol (A) and HDL-phospholipid (B) were determined by an HPLC system. Open squares, control LDL-loaded cells; open circles, probucol-LDL loaded cells. C: ApoA-I binding. The indicated amounts of 125 I-apoA-I-incubated HepG2 cells were preloaded with control LDL or probucol-containing LDL for 2 h at 4 ° C. The cells were washed two times with ice-cold PBS, and the bound 125 I-apoA-I was displaced two times by 50 𝛍 g/ml nonlabeled apoA-I for 9 h. The difference in the total radioactivity after the first washing and after the second displacement was calculated as displaceable or exchangeable binding of apoA-I to the cells. Squares, binding to the cells loaded with control LDL; circles, binding to the cells loaded with probucol-containing LDL. Error bars indicate ± SEM.CC-BY · From the PDF
Fig. 6 Analysis of apolipoproteins in the HPLC fractions of the HepG2 conditioned medium. The conditioned medium of HepG2 cells (A) and probucol-loaded HepG2 cells (B) was tested after 16 h of incubation. The medium was analyzed by HPLC and fractionated as described in the text. The upper panels show immunoblot analysis of the fractions for apoB and apoA-I, and the lower panels represent HPLC elution profiles of lipids (solid lines, cholesterol; dotted lines, choline-phospholipid). Positions of lanes in the immunoblot analysis are adjusted for the HPLC elution times. VLDL, LDL, and HDL indicate the eluting positions for plasma lipoproteins.
Fig. 6 Analysis of apolipoproteins in the HPLC fractions of the HepG2 conditioned medium. The conditioned medium of HepG2 cells (A) and probucol-loaded HepG2 cells (B) was tested after 16 h of incubation. The medium was analyzed by HPLC and fractionated as described in the text. The upper panels show immunoblot analysis of the fractions for apoB and apoA-I, and the lower panels represent HPLC elution profiles of lipids (solid lines, cholesterol; dotted lines, choline-phospholipid). Positions of lanes in the immunoblot analysis are adjusted for the HPLC elution times. VLDL, LDL, and HDL indicate the eluting positions for plasma lipoproteins.CC-BY · From the PDF
Fig. 7 Immunoblot analysis of apoA-I and ABCA1. A: ApoA-I in the conditioned medium of HepG2 cells was analyzed after preincubation with control LDL and probucol-containing LDL and subsequent incubation in the presence and absence of 10 𝛍 g/ml apoA-I for 16 h. B: Density distribution of apoA-I in the medium. ApoA-I was analyzed in density subfractions of the conditioned medium of HepG2 cells preincubated with 50 𝛍 g/ml control LDL (C) or probucol-containing LDL (P) for 24 h and then incubated for 16 h. The medium was fractionated by sequential ultracentrifugation for the VLDL/LDL fraction (d < 1.063 g/ml), the HDL fraction (1.063 < d < 1.21 g/ml), and the bottom fraction (d > 1.21 g/ml). Each fraction, corresponding to 10 𝛍 l of the original medium, was dialyzed and analyzed for apoA-I. C: ABCA1 in the plasma membrane of HepG2 cells prepared as described for A. D: Clearance of ABCA1 in HepG2 cells. The cells were preloaded with control or probucol-containing LDL, and ABCA1 was examined after incubation with 71 𝛍 M cycloheximide.
Fig. 7 Immunoblot analysis of apoA-I and ABCA1. A: ApoA-I in the conditioned medium of HepG2 cells was analyzed after preincubation with control LDL and probucol-containing LDL and subsequent incubation in the presence and absence of 10 𝛍 g/ml apoA-I for 16 h. B: Density distribution of apoA-I in the medium. ApoA-I was analyzed in density subfractions of the conditioned medium of HepG2 cells preincubated with 50 𝛍 g/ml control LDL (C) or probucol-containing LDL (P) for 24 h and then incubated for 16 h. The medium was fractionated by sequential ultracentrifugation for the VLDL/LDL fraction (d < 1.063 g/ml), the HDL fraction (1.063 < d < 1.21 g/ml), and the bottom fraction (d > 1.21 g/ml). Each fraction, corresponding to 10 𝛍 l of the original medium, was dialyzed and analyzed for apoA-I. C: ABCA1 in the plasma membrane of HepG2 cells prepared as described for A. D: Clearance of ABCA1 in HepG2 cells. The cells were preloaded with control or probucol-containing LDL, and ABCA1 was examined after incubation with 71 𝛍 M cycloheximide.CC-BY · From the PDF
Image 8
CC-BY · From the PDF
Fig. 8 Inhibition of HDL production by HepG2 cells by a monoclonal antibody against lipid-free apoA-I. A: HepG2 cells were incubated with 0.02% BSA-containing MEM𝛂 medium in the presence of 1 mg/ml monoclonal antibody 725-1E2 specific to lipid-free apoA-I and 10 𝛍 g/ml apoA-I for 16 h, and the medium was analyzed for its lipoprotein profile using HPLC with one gel-permeation column (Lipopropak XL; 7.8 mm × 300 mm; Tosoh). A-a: The medium of the cells by plain incubation. A-b: The medium of the cells incubated in the presence of apoA-I. A-c: The medium after incubation in the presence of control mouse IgG. A-d: The medium incubated in the presence of apoA-I and control IgG. A-e: The medium of the probucol (Pb)-preloaded cells. A-f: The medium of the cell preloaded with probucol after incubation in the presence of apoA-I. A-g: The medium of the cells incubated in the presence of the free apoA-I-specific antibody 725-1E2. A-h: The medium of the cells incubated with the antibody 725-1E2 in the presence of apoA-I. B: The conditioned medium of HepG2 cells was incubated for 16 h in the absence (B-a) and presence (B-b) of the antibody, and the lipoprotein profile was analyzed by HPLC. Solid lines, cholesterol; dotted lines, choline-phospholipid.
Fig. 8 Inhibition of HDL production by HepG2 cells by a monoclonal antibody against lipid-free apoA-I. A: HepG2 cells were incubated with 0.02% BSA-containing MEM𝛂 medium in the presence of 1 mg/ml monoclonal antibody 725-1E2 specific to lipid-free apoA-I and 10 𝛍 g/ml apoA-I for 16 h, and the medium was analyzed for its lipoprotein profile using HPLC with one gel-permeation column (Lipopropak XL; 7.8 mm × 300 mm; Tosoh). A-a: The medium of the cells by plain incubation. A-b: The medium of the cells incubated in the presence of apoA-I. A-c: The medium after incubation in the presence of control mouse IgG. A-d: The medium incubated in the presence of apoA-I and control IgG. A-e: The medium of the probucol (Pb)-preloaded cells. A-f: The medium of the cell preloaded with probucol after incubation in the presence of apoA-I. A-g: The medium of the cells incubated in the presence of the free apoA-I-specific antibody 725-1E2. A-h: The medium of the cells incubated with the antibody 725-1E2 in the presence of apoA-I. B: The conditioned medium of HepG2 cells was incubated for 16 h in the absence (B-a) and presence (B-b) of the antibody, and the lipoprotein profile was analyzed by HPLC. Solid lines, cholesterol; dotted lines, choline-phospholipid.CC-BY · From the PDF
Fig. 9 Effect of free apoA-I-specific monoclonal antibody on HDL production by HepG2 cells. A: Cholesterol and phospholipid in HDL in the medium of HepG2 cells incubated in the presence of the antibody 725-1E2 and apoA-I, based on HPLC analysis. The data represent means ± SEM of triplicate assays. B: Cholesterol and phospholipid in HDL in the medium of HepG2 cells incubated in the presence of the antibody 725-1E2 and apoA-I, based on ultracentrifugal analysis. Data represent means ± SEM of triplicate assays.
Fig. 9 Effect of free apoA-I-specific monoclonal antibody on HDL production by HepG2 cells. A: Cholesterol and phospholipid in HDL in the medium of HepG2 cells incubated in the presence of the antibody 725-1E2 and apoA-I, based on HPLC analysis. The data represent means ± SEM of triplicate assays. B: Cholesterol and phospholipid in HDL in the medium of HepG2 cells incubated in the presence of the antibody 725-1E2 and apoA-I, based on ultracentrifugal analysis. Data represent means ± SEM of triplicate assays.CC-BY · From the PDF

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Research works printed but not linked: 27

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Authors
Tsujita, M., Wu, C.-A., Abe-Dohmae, S., Usui, S., Okazaki, M., & Yokoyama, S.
Venue
Journal of Lipid Research
Publisher
Elsevier BV
Published
2005-01
Volume
46
Issue
1
Pages
154-162
ISSN
0022-2275
DOI
10.1194/jlr.m400402-jlr200
Cited by
67
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Language
en
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Tsujita, M., Wu, C.-A., Abe-Dohmae, S., Usui, S., Okazaki, M., & Yokoyama, S. (2005). On the hepatic mechanism of HDL assembly by the ABCA1/apoA-I pathway. Journal of Lipid Research. https://doi.org/10.1194/jlr.m400402-jlr200