Liver ACSM3 deficiency mediates metabolic syndrome via a lauric acid-HNF4α-p38 MAPK axis

EMBO J. 2024 Feb;43(4):507-532. doi: 10.1038/s44318-023-00020-1. Epub 2024 Jan 8.

Abstract

Metabolic syndrome combines major risk factors for cardiovascular disease, making deeper insight into its pathogenesis important. We here explore the mechanistic basis of metabolic syndrome by recruiting an essential patient cohort and performing extensive gene expression profiling. The mitochondrial fatty acid metabolism enzyme acyl-CoA synthetase medium-chain family member 3 (ACSM3) was identified to be significantly lower expressed in the peripheral blood of metabolic syndrome patients. In line, hepatic ACSM3 expression was decreased in mice with metabolic syndrome. Furthermore, Acsm3 knockout mice showed glucose and lipid metabolic abnormalities, and hepatic accumulation of the ACSM3 fatty acid substrate lauric acid. Acsm3 depletion markedly decreased mitochondrial function and stimulated signaling via the p38 MAPK pathway cascade. Consistently, Acsm3 knockout mouse exhibited abnormal mitochondrial morphology, decreased ATP contents, and enhanced ROS levels in their livers. Mechanistically, Acsm3 deficiency, and lauric acid accumulation activated nuclear receptor Hnf4α-p38 MAPK signaling. In line, the p38 inhibitor Adezmapimod effectively rescued the Acsm3 depletion phenotype. Together, these findings show that disease-associated loss of ACSM3 facilitates mitochondrial dysfunction via a lauric acid-HNF4a-p38 MAPK axis, suggesting a novel therapeutic vulnerability in systemic metabolic dysfunction.

Keywords: Acsm3; Lauric Acid; Metabolic Syndrome; Mitochondria Dysfunction; p38 MAPK Signaling Pathway.

MeSH terms

  • Animals
  • Coenzyme A Ligases / genetics
  • Coenzyme A Ligases / metabolism
  • Coenzyme A Ligases / pharmacology
  • Fatty Acids / metabolism
  • Humans
  • Lauric Acids*
  • Liver / metabolism
  • Metabolic Syndrome* / genetics
  • Metabolic Syndrome* / metabolism
  • Mice
  • p38 Mitogen-Activated Protein Kinases / genetics

Substances

  • lauric acid
  • p38 Mitogen-Activated Protein Kinases
  • Fatty Acids
  • ACSM3 protein, human
  • Coenzyme A Ligases
  • Lauric Acids