
pmid: 20171215
A link between cellular uptake of high density lipoprotein (HDL) and regulation of sterol regulatory element‐binding protein‐1 (SREBP‐1) was investigated in vitro. HDL decreased nuclear SREBP‐1 levels as well as SREBP‐1 target gene expression in HepG2 and HEK293 cells. However, HDL did not repress an exogenously expressed, constitutively active form of SREBP‐1. HDL increased cellular cholesterol levels, and cellular cholesterol depletion by methyl‐β‐cyclodextrin abolished the effects of HDL. These results suggest that HDL inhibits the activation of SREBP‐1 through a cholesterol‐dependent mechanism, which may play an important role in regulating lipid synthetic pathways mediated by SREBP‐1.
Male, Transcriptional Activation, Cellular lipogenesis, High density lipoprotein, Hep G2 Cells, Lipid Metabolism, Gene Expression Regulation, Enzymologic, Rats, Rats, Sprague-Dawley, Cholesterol, Sterol regulatory element-binding protein-1, Animals, Humans, Fatty Acid Synthases, Lipoproteins, HDL, Promoter Regions, Genetic, Sterol Regulatory Element Binding Protein 1, Cells, Cultured, Stearoyl-CoA Desaturase, Acetyl-CoA Carboxylase
Male, Transcriptional Activation, Cellular lipogenesis, High density lipoprotein, Hep G2 Cells, Lipid Metabolism, Gene Expression Regulation, Enzymologic, Rats, Rats, Sprague-Dawley, Cholesterol, Sterol regulatory element-binding protein-1, Animals, Humans, Fatty Acid Synthases, Lipoproteins, HDL, Promoter Regions, Genetic, Sterol Regulatory Element Binding Protein 1, Cells, Cultured, Stearoyl-CoA Desaturase, Acetyl-CoA Carboxylase
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