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• W2066404731 endingPage "80" @default.
• W2066404731 startingPage "72" @default.
• W2066404731 abstract "Endoplasmic reticulum (ER) stress modulates gene expression and has been implicated in causing dyslipidemias. To determine if ER stress may contribute to hypoalphalipoproteinemia through suppression of apo A-I gene expression, human hepatoma cell line Hep G2 was treated with ER stress inducers and the changes in apo A-I gene expression were compared to albumin gene expression. HepG2 cells were treated with tunicamycin (TM) and thapsigargin (TG), two potent inducers of ER stress, and apo A-I and albumin protein levels, mRNA levels, and promoter activity were measured. ER stress was measured using the ER stress-responsive alkaline phosphatase assay and by Western blot quantitation of ER stress markers such as glucose-regulated protein-78 (GRP-78), phosphorylated Jun N-terminal kinase (phospho-JNK), total JNK, phosphorylated eukaryotic initiation factor 2 alpha (phospho eIF2α), and total eIF2α. TM and TG induced ER stress in HepG2 cells and reduced apo A-I and albumin secretion in a dose-dependent manner. Intracellular albumin levels increased in cells treated with TM and TG while intracellular apo A-I levels decreased. Albumin mRNA and albumin gene promoter activity were reduced in proportion to the decrease in albumin secreted while changes in the apo A-I mRNA levels and promoter activity were modest and did not account for the reduction in apo A-I secretion. These results indicate that apo A-I secretion is inhibited by ER stress possibly by affecting cellular degradation pathways. However, ER stress does not affect apo A-I secretion by regulating gene expression." @default.
• W2066404731 created "2016-06-24" @default.
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• W2066404731 date "2013-01-01" @default.
• W2066404731 modified "2023-10-18" @default.
• W2066404731 title "Endoplasmic reticulum stress in HepG2 cells inhibits apolipoprotein A-I secretion" @default.
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• W2066404731 doi "https://doi.org/10.1016/j.lfs.2012.11.001" @default.
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