ChREBP Rather Than SHP Regulates Hepatic VLDL Secretion.

ChREBP Rather Than SHP Regulates Hepatic VLDL Secretion.
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Niwa H, Iizuka K, Kato T, Wu W, Tsuchida H, Takao K, Horikawa Y, Takeda J,


Niwa H, Iizuka K, Kato T, Wu W, Tsuchida H, Takao K, Horikawa Y, Takeda J, (click to view)

Niwa H, Iizuka K, Kato T, Wu W, Tsuchida H, Takao K, Horikawa Y, Takeda J,

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Nutrients 2018 03 0710(3) pii E321
Abstract

The regulation of hepatic very-low-density lipoprotein (VLDL) secretion plays an important role in the pathogenesis of dyslipidemia and fatty liver diseases. VLDL is controlled by hepatic microsomal triglyceride transfer protein (MTTP).is regulated by carbohydrate response element binding protein (ChREBP) and small heterodimer partner (SHP). However, it is unclear whether both coordinately regulateexpression and VLDL secretion. Here, adenoviral overexpression of ChREBP and SHP in rat primary hepatocytes induced and suppressedmRNA, respectively. However,induction by ChREBP was much more potent than suppression by SHP. Promoter assays ofand the liver type pyruvate kinase gene revealed that SHP and ChREBP did not affect the transcriptional activity of each other.mRNA and protein levels of Shpmice were similar to those of wild-types; however, those of ChrebpShpand Chrebpmice were significantly much lower. Consistent with this, the VLDL particle number and VLDL secretion rates in Shpmice were similar to wild-types but were much lower in Chrebpand ChrebpShpmice. These findings suggest that ChREBP, rather than SHP, regulates VLDL secretion under normal conditions and that ChREBP and SHP do not affect the transcriptional activities of each other.

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