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Regulated turnover of a cell surface-associated pool of newly synthesized apolipoprotein E in HepG2 cells

Schmitt, Matthias, Grand-Perret, Thierry·1999·Journal of Lipid Research
DOI 10.1016/s0022-2275(20)33337-x
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Fig. 1 Analysis of apoE and albumin secretion by HepG2 cells. HepG2 cells were radiolabeled with [ 35 S]methionine for 10 min and chased in the presence of unlabeled methionine for the times indicated. ApoE and albumin were immunoprecipitated from cell lysates (cellular) and culture supernatants (extracellular) and subjected to SDS-PAGE as described in Materials and Methods. (A) Phosphorimager analysis of representative SDS-PAGE gels. (B) Phosphorimager quantification of four independent experiments (means 6 SD). All apoE bands were quantified. The totals were calculated by addition of cellular and extracellular material. The amounts of apoE and albumin after the pulse were set to 100%.
Fig. 1 Analysis of apoE and albumin secretion by HepG2 cells. HepG2 cells were radiolabeled with [ 35 S]methionine for 10 min and chased in the presence of unlabeled methionine for the times indicated. ApoE and albumin were immunoprecipitated from cell lysates (cellular) and culture supernatants (extracellular) and subjected to SDS-PAGE as described in Materials and Methods. (A) Phosphorimager analysis of representative SDS-PAGE gels. (B) Phosphorimager quantification of four independent experiments (means 6 SD). All apoE bands were quantified. The totals were calculated by addition of cellular and extracellular material. The amounts of apoE and albumin after the pulse were set to 100%.CC-BY · From the PDF
Fig. 2 Transient accumulation of newly synthesized apoE on the cell surface. HepG2 cells were radiolabeled with [ 35 S]methionine for 10 min and chased in the presence of unlabeled methionine for the times indicated. After the chase, cells were biotinylated and treated with 200 m g/ml trypsin as described in Materials and Methods. ApoE was immunoprecipitated from cell lysates of trypsintreated and non-trypsin-treated cells as described in Materials and Methods. Samples were subjected to SDS-PAGE and quantified by phosphorimager analysis. The figure shows means 6 SD of three independent experiments. Trypsin-sensitive apoE was calculated as the difference between apoE immunoprecipitations of trypsintreated and non-trypsin-treated cells. The amount of apoE after the pulse was set to 100%.
Fig. 2 Transient accumulation of newly synthesized apoE on the cell surface. HepG2 cells were radiolabeled with [ 35 S]methionine for 10 min and chased in the presence of unlabeled methionine for the times indicated. After the chase, cells were biotinylated and treated with 200 m g/ml trypsin as described in Materials and Methods. ApoE was immunoprecipitated from cell lysates of trypsintreated and non-trypsin-treated cells as described in Materials and Methods. Samples were subjected to SDS-PAGE and quantified by phosphorimager analysis. The figure shows means 6 SD of three independent experiments. Trypsin-sensitive apoE was calculated as the difference between apoE immunoprecipitations of trypsintreated and non-trypsin-treated cells. The amount of apoE after the pulse was set to 100%.CC-BY · From the PDF
Fig. 3 Cell-associated apoE is localized predominantly on the cell surface. HepG2 cells were radiolabeled with [ 35 S]methionine for 48 h in RPMI-medium in the absence of serum. Afterwards, cells were treated with the indicated concentrations of trypsin as described in Materials and Methods. Cells were lysed and apoE was immunoprecipitated as described in Materials and Methods. The figure shows the phosphorimager analysis of a representative gel (upper panel) and the phosphorimager quantification of duplicate samples (means 6 SD; lower panel). Similar results were obtained when cells were radiolabeled in the presence of 10% fetal bovine serum.
Fig. 3 Cell-associated apoE is localized predominantly on the cell surface. HepG2 cells were radiolabeled with [ 35 S]methionine for 48 h in RPMI-medium in the absence of serum. Afterwards, cells were treated with the indicated concentrations of trypsin as described in Materials and Methods. Cells were lysed and apoE was immunoprecipitated as described in Materials and Methods. The figure shows the phosphorimager analysis of a representative gel (upper panel) and the phosphorimager quantification of duplicate samples (means 6 SD; lower panel). Similar results were obtained when cells were radiolabeled in the presence of 10% fetal bovine serum.CC-BY · From the PDF
Fig. 4 Heparin-sensitive binding of apoE to HepG2 cells. HepG2 cells were radiolabeled with [ 35 S]methionine for 15 min and chased in the presence of unlabeled methionine for 2 h. Chase media containing radiolabeled secreted proteins were incubated with unlabeled HepG2 cells ( 1 cells) in the presence or absence of heparin (10 m g/ml) as described in Materials and Methods. In parallel, chase media containing radiolabeled secreted proteins were incubated in empty wells of the culture dishes to assay non-specific binding ( 2 cells). Incubations were performed either at 4 8 C (upper panel) or at 37 8 C (lower panel) for the times indicated. Afterwards, apoE was immunoprecipitated from cell lysates and culture supernatants and subjected to SDS-PAGE as described in Materials and Methods. Samples were quantified by phosphorimager analysis (means 6 SD of three independent experiments). The amount of radiolabeled apoE applied to each well of unlabeled cells was set to 100%.
Fig. 4 Heparin-sensitive binding of apoE to HepG2 cells. HepG2 cells were radiolabeled with [ 35 S]methionine for 15 min and chased in the presence of unlabeled methionine for 2 h. Chase media containing radiolabeled secreted proteins were incubated with unlabeled HepG2 cells ( 1 cells) in the presence or absence of heparin (10 m g/ml) as described in Materials and Methods. In parallel, chase media containing radiolabeled secreted proteins were incubated in empty wells of the culture dishes to assay non-specific binding ( 2 cells). Incubations were performed either at 4 8 C (upper panel) or at 37 8 C (lower panel) for the times indicated. Afterwards, apoE was immunoprecipitated from cell lysates and culture supernatants and subjected to SDS-PAGE as described in Materials and Methods. Samples were quantified by phosphorimager analysis (means 6 SD of three independent experiments). The amount of radiolabeled apoE applied to each well of unlabeled cells was set to 100%.CC-BY · From the PDF
Fig. 5 Binding, deglycosylation, and degradation of apoE by HepG2 cells. HepG2 cells were radiolabeled with [ 35 S]methionine for 15 min and chased in the presence of unlabeled methionine for 2 h. Chase media containing radiolabeled secreted proteins were incubated with unlabeled HepG2 cells as described in Materials and Methods. Incubations were performed at 37 8 C for the times indicated. Afterwards, apoE was immunoprecipitated from cell lysates (bound apoE) and culture supernatants (unbound apoE) and subjected to SDS-PAGE as described in Materials and Methods. The upper panel shows the phosphorimager analysis of a representative SDS-PAGE gel. The middle panel shows the phosphorimager quantification of all bands of apoE, whereas the lower panel shows a quantification of the non-glycosylated, fastest migrating band of apoE (means 6 SD of three independent experiments). The amount of radiolabeled apoE applied to each well of unlabeled cells (left lane, input) was set to 100%.
Fig. 5 Binding, deglycosylation, and degradation of apoE by HepG2 cells. HepG2 cells were radiolabeled with [ 35 S]methionine for 15 min and chased in the presence of unlabeled methionine for 2 h. Chase media containing radiolabeled secreted proteins were incubated with unlabeled HepG2 cells as described in Materials and Methods. Incubations were performed at 37 8 C for the times indicated. Afterwards, apoE was immunoprecipitated from cell lysates (bound apoE) and culture supernatants (unbound apoE) and subjected to SDS-PAGE as described in Materials and Methods. The upper panel shows the phosphorimager analysis of a representative SDS-PAGE gel. The middle panel shows the phosphorimager quantification of all bands of apoE, whereas the lower panel shows a quantification of the non-glycosylated, fastest migrating band of apoE (means 6 SD of three independent experiments). The amount of radiolabeled apoE applied to each well of unlabeled cells (left lane, input) was set to 100%.CC-BY · From the PDF
Fig. 6 Inhibition of apoE degradation by lysosomotropic agents. HepG2 cells were radiolabeled with [ 35 S]methionine for 15 min and chased in the presence of unlabeled methionine for 2 h. Chase media containing radiolabeled secreted proteins were incubated with unlabeled HepG2 cells as described in Materials and Methods. Incubations were performed at 37 8 C for the times indicated. After 90 min of incubation, either 100 m m chloroquine or 1 m m NH4Cl was added to the samples as indicated. ApoE, apoA-I, and apoB were immunoprecipitated from cell lysates and culture supernatants and subjected to SDS-PAGE as described in Materials and Methods. The figure shows the phosphorimager quantification of two independent experiments (means 6 SD). All apoE bands were quantified. The amount of radiolabeled apoE applied to each well of unlabeled cells was set to 100%.
Fig. 6 Inhibition of apoE degradation by lysosomotropic agents. HepG2 cells were radiolabeled with [ 35 S]methionine for 15 min and chased in the presence of unlabeled methionine for 2 h. Chase media containing radiolabeled secreted proteins were incubated with unlabeled HepG2 cells as described in Materials and Methods. Incubations were performed at 37 8 C for the times indicated. After 90 min of incubation, either 100 m m chloroquine or 1 m m NH4Cl was added to the samples as indicated. ApoE, apoA-I, and apoB were immunoprecipitated from cell lysates and culture supernatants and subjected to SDS-PAGE as described in Materials and Methods. The figure shows the phosphorimager quantification of two independent experiments (means 6 SD). All apoE bands were quantified. The amount of radiolabeled apoE applied to each well of unlabeled cells was set to 100%.CC-BY · From the PDF
Fig. 7 Enhanced secretion and reduced degradation of apoE in the presence of human serum. HepG2 cells were radiolabeled with [ 35 S]methionine for 10 min and chased in the presence of unlabeled methionine for 2 h (upper panel) or 6 h (lower panel). ApoE was immunoprecipitated from cell lysates (cellular apoE) and culture supernatants (extracellular apoE) and subjected to SDS-PAGE as described in Materials and Methods. The figure shows the phosphorimager quantification of duplicate samples of a representative experiment (means 6 SD). All apoE bands were quantified. The degraded material (degraded apoE) represents the difference between the sum of cellular and secreted apoE after the chase and the amount of apoE after the pulse. The amount of apoE after the pulse was set to 100%.
Fig. 7 Enhanced secretion and reduced degradation of apoE in the presence of human serum. HepG2 cells were radiolabeled with [ 35 S]methionine for 10 min and chased in the presence of unlabeled methionine for 2 h (upper panel) or 6 h (lower panel). ApoE was immunoprecipitated from cell lysates (cellular apoE) and culture supernatants (extracellular apoE) and subjected to SDS-PAGE as described in Materials and Methods. The figure shows the phosphorimager quantification of duplicate samples of a representative experiment (means 6 SD). All apoE bands were quantified. The degraded material (degraded apoE) represents the difference between the sum of cellular and secreted apoE after the chase and the amount of apoE after the pulse. The amount of apoE after the pulse was set to 100%.CC-BY · From the PDF
Fig. 8 Influence of human serum on apoE interaction with the cell surface. (A) HepG2 cells were radiolabeled with [ 35 S]methionine for 10 min and chased in the presence of unlabeled methionine for 2 h. Chase medium was discarded and cells were washed with Dulbecco's PBS. Subsequently, cells were chased for another 2 h in RPMI medium in the presence or absence of 10% human serum either at 4 8 C or 37 8 C. ApoE was immunoprecipitated from culture supernatants and subjected to SDS-PAGE as described in Materials and Methods. The figure shows the phosphorimager quantification of two independent experiments (means 6 SD). All apoE bands were quantified. The amount of apoE after the pulse was set to 100%. (B) HepG2 cells were radiolabeled with [ 35 S]methionine for 15 min and chased in the presence of unlabeled methionine for 2 h (chase), either in the presence or absence of 10% human serum. Chase media containing radiolabeled secreted proteins were incubated for 90 min with unlabeled HepG2 cells as described in Materials and Methods (re-binding). The second chase was performed either in the presence or absence of 10% human serum. ApoE immunoprecipitation and detection were performed as described in (A). The amount of radiolabeled apoE applied to each well of unlabeled cells was set to 100%.
Fig. 8 Influence of human serum on apoE interaction with the cell surface. (A) HepG2 cells were radiolabeled with [ 35 S]methionine for 10 min and chased in the presence of unlabeled methionine for 2 h. Chase medium was discarded and cells were washed with Dulbecco's PBS. Subsequently, cells were chased for another 2 h in RPMI medium in the presence or absence of 10% human serum either at 4 8 C or 37 8 C. ApoE was immunoprecipitated from culture supernatants and subjected to SDS-PAGE as described in Materials and Methods. The figure shows the phosphorimager quantification of two independent experiments (means 6 SD). All apoE bands were quantified. The amount of apoE after the pulse was set to 100%. (B) HepG2 cells were radiolabeled with [ 35 S]methionine for 15 min and chased in the presence of unlabeled methionine for 2 h (chase), either in the presence or absence of 10% human serum. Chase media containing radiolabeled secreted proteins were incubated for 90 min with unlabeled HepG2 cells as described in Materials and Methods (re-binding). The second chase was performed either in the presence or absence of 10% human serum. ApoE immunoprecipitation and detection were performed as described in (A). The amount of radiolabeled apoE applied to each well of unlabeled cells was set to 100%.CC-BY · From the PDF
Fig. 9 The effect of isolated human LDL and HDL on apoE secretion and binding to HepG2 cells. (A) HepG2 cells were radiolabeled with [ 35 S]methionine for 10 min and chased in the presence of unlabeled methionine for 2 h in the presence or absence of either 10% human serum, 100 m g/ml isolated human LDL, or 10 m g/ml isolated human HDL. ApoE was immunoprecipitated from cell lysates (white bars) and culture supernatants (black bars) and subjected to SDS-PAGE as described in Materials and Methods. The figure shows the phosphorimager quantification of two independent experiments (means 6 SD). All apoE bands were quantified. The amount of apoE after the pulse was set to 100%. (B) HepG2 cells were radiolabeled with [ 35 S]methionine for 15 min and chased in the presence of unlabeled methionine for 2 h in the presence or absence of 10% human serum, 100 m g/ml isolated human LDL, or 10 m g/ml isolated human HDL. The obtained chase media containing radiolabeled secreted proteins were incubated for 90 min with unlabeled HepG2 cells as described in Materials and Methods. ApoE immunoprecipitation and detection were performed as described in (A). The amount of radiolabeled apoE applied to each well of unlabeled cells was set to 100%.
Fig. 9 The effect of isolated human LDL and HDL on apoE secretion and binding to HepG2 cells. (A) HepG2 cells were radiolabeled with [ 35 S]methionine for 10 min and chased in the presence of unlabeled methionine for 2 h in the presence or absence of either 10% human serum, 100 m g/ml isolated human LDL, or 10 m g/ml isolated human HDL. ApoE was immunoprecipitated from cell lysates (white bars) and culture supernatants (black bars) and subjected to SDS-PAGE as described in Materials and Methods. The figure shows the phosphorimager quantification of two independent experiments (means 6 SD). All apoE bands were quantified. The amount of apoE after the pulse was set to 100%. (B) HepG2 cells were radiolabeled with [ 35 S]methionine for 15 min and chased in the presence of unlabeled methionine for 2 h in the presence or absence of 10% human serum, 100 m g/ml isolated human LDL, or 10 m g/ml isolated human HDL. The obtained chase media containing radiolabeled secreted proteins were incubated for 90 min with unlabeled HepG2 cells as described in Materials and Methods. ApoE immunoprecipitation and detection were performed as described in (A). The amount of radiolabeled apoE applied to each well of unlabeled cells was set to 100%.CC-BY · From the PDF

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Metadata

Authors
Schmitt, M., & Grand-Perret, T.
Venue
Journal of Lipid Research
Publisher
Elsevier BV
Published
1999-01
Volume
40
Issue
1
Pages
39-49
ISSN
0022-2275
DOI
10.1016/s0022-2275(20)33337-x
Cited by
14
References
3
Language
en
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