Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10872052 | FEBS Letters | 2010 | 6 Pages |
Abstract
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.
Keywords
GAPDHSCD1SREBP-1RCTS1PACCMβCDSCAPFASNAFLDSREBP cleavage activating proteinCETPacetyl-CoA carboxylasefatty acid synthasenon-alcoholic fatty liver diseaseInsigendoplasmic reticulumhigh density lipoproteinmethyl-β-cyclodextrinSterol regulatory element-binding protein-1cholesteryl ester transfer proteininsulin-induced genecholesterolreverse cholesterol transportGlyglyburideglyceraldehyde-3-phosphate dehydrogenase
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Authors
Masaki Yoshida, Nagakatsu Harada, Keiko Yoshida, Tadahiko Nakagawa, Takaaki Shimohata, Kazuaki Mawatari, Akira Takahashi, Hiroshi Sakaue, Yutaka Nakaya,