Phosphorylation of Acetyl-CoA Carboxylase by AMPK Reduces Renal Fibrosis and Is Essential for the Anti-Fibrotic Effect of Metformin | Zendy

Mardiana Lee | Zendy; Marina Katerelos | Zendy; Kurt Gleich | Zendy; Sandra Galić | Zendy; Bruce E. Kemp | Zendy; Peter F. Mount | Zendy; David A. Power | Zendy

Open Access

Phosphorylation of Acetyl-CoA Carboxylase by AMPK Reduces Renal Fibrosis and Is Essential for the Anti-Fibrotic Effect of Metformin

Author(s) -

Mardiana Lee,

Marina Katerelos,

Kurt Gleich,

Sandra Galić,

Bruce E. Kemp,

Peter F. Mount,

David A. Power

Publication year - 2018

Publication title -

journal of the american society of nephrology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 4.451

H-Index - 279

eISSN - 1533-3450

pISSN - 1046-6673

DOI - 10.1681/asn.2018010050

Subject(s) - ampk , phosphorylation , fibrosis , metformin , endocrinology , medicine , acetyl coa carboxylase , amp activated protein kinase , beta oxidation , lipid metabolism , kidney , chemistry , protein kinase a , pharmacology , pyruvate carboxylase , metabolism , biochemistry , diabetes mellitus , enzyme

Expression of genes regulating fatty acid metabolism is reduced in tubular epithelial cells from kidneys with tubulointerstitial fibrosis (TIF), thus decreasing the energy produced by fatty acid oxidation (FAO). Acetyl-CoA carboxylase (ACC), a target for the energy-sensing AMP-activating protein kinase (AMPK), is the major controller of the rate of FAO within cells. Metformin has a well described antifibrotic effect, and increases phosphorylation of ACC by AMPK, thereby increasing FAO.

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