Modulators of Protein Kinase C Affect SR-BI-Dependent HDL Lipid Uptake in Transfected HepG2 Cells
Figure 6
The protein kinase C inhibitor calphostin C reduces SR-BI-mediated DiI-HDL lipid uptake in HepG2 cells independently of SR-BI’s C-terminal tail. DiI-HDL lipid uptake (panels (a)-(c)) and eGFP fluorescence (panels (d) and (e)) were measured by flow cytometry. HepG2[eGFP-SR-BI] cells untreated or treated with 0.5 μM PMA, 7.5 μM chelerythrine chloride, 1 μM calphostin C, 300 nM BLT-1, individually or in combination as indicated panels (a) and (d). HepG2[eGFP-SR-BI-ΔC] cells untreated or treated with PMA, calphostin C, or BLT-1 either individually or in combination as indicated panels (b) and (e). Panel (c): untransfected HepG2 cells treated without or with PMA or calphostin C individually as above. The data represent average ± standard deviations of triplicate samples. compared to control by Student’s -test.
