Aspartate-β-hydroxylase suppresses nonalcoholic fatty liver progression by regulating AMPK phosphorylation and SREBP-1c expression.textMulla, Joud IssamcreatorHuang, Chiung-kueiAdvisorWands, JackReaderLi, JisuReaderBrown University. Department of Molecular Pharmacology, Physiology and Biotechnologysponsor2020, 44 p.born digitalThesis (Sc. M.)--Brown University, 2020thesesNAFLD affects more than one-quarter of adults worldwide with 60% in diabetic patients and 90% in obese people. Aspartate beta-hydroxylase (ASPH), an alpha-ketoglutarate dependent enzyme hydroxylase that has been linked to hepatocellular carcinoma, recently shown to suppress NAFLD progression by regulating AMPK phosphorylation and SREBP1c expression, which are important regulators in lipid and glucose metabolism. B6 mice have been successfully genetically modified with human ASPH gene. Using those transgenic mice, we demonstrated that human ASPH overexpression decreases liver weight in mice fed with a high-fat diet. Moreover; western blot shows that overexpression of ASPH in mice fed with high-fat diet play a role in lipid and glucose metabolism by activating AMPK phosphorylation and suppressing SREBP1c expression. ASPH overexpression reduces hepatic lipid accumulation as shown in the histology staining and lipid analysis. Our study indicates the potential of ASPH as a therapeutic target in NAFLD.LiverLiver--DiseasesGastroenterologyEnglishRPB2020072010.26300/xmhw-ve62In CopyrightCollection is open for research.