期刊
ARCHIVES OF PHYSIOLOGY AND BIOCHEMISTRY
卷 120, 期 5, 页码 216-227出版社
TAYLOR & FRANCIS LTD
DOI: 10.3109/13813455.2014.973418
关键词
Dyslipidemia; fatty acids; hepatokine; NAFLD; secretome
资金
- Center for Molecular Medicine Cologne [TV1]
- German Diabetes Center
- city of Hamburg (Norgenta GmbH) within LiDia project
The transcription factor sterol regulatory element binding protein (SREBP)-1c plays a pivotal role in lipid metabolism. In this report we identified the main phosphorylation sites of MAPK-families, i.e. p38 stress-activated MAPK (p38), ERK-MAPK (ERK) or c-JUN N-terminal protein kinases (JNK) in SREBP-1c. The major phosphorylation sites of p38, i.e. serine 39 and threonine 402, are identical to those we recently identified in the splice-variant SREBP-1a. In contrast, ERK and JNK phosphorylate SREBP-1c at two major sites, i.e. threonine 81 and serine 93, instead of one site in SREBP-1a. Functional analyses of the biological outcome in the human liver cell line HepG2 reveals SREBP-1c phosphorylation dependent alteration in lipid metabolism and secretion pattern of lipid transporting proteins, e. g. ApoE or ApoA1. These results suggest that phosphorylation of SREBP-1c by different MAPKs interferes with lipid metabolism and the secretory activity of liver cells.
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