Adipose acyl-CoA synthetase-1 directs fatty acids toward beta-oxidation and is required for cold thermogenesis

Cell Metab. 2010 Jul 7;12(1):53-64. doi: 10.1016/j.cmet.2010.05.012.

Abstract

Long-chain acyl-CoA synthetase-1 (ACSL1) contributes 80% of total ACSL activity in adipose tissue and was believed to be essential for the synthesis of triacylglycerol. We predicted that an adipose-specific knockout of ACSL1 (Acsl1(A-/-)) would be lipodystrophic, but compared to controls, Acsl1(A-/-) mice had 30% greater fat mass when fed a low-fat diet and gained weight normally when fed a high-fat diet. Acsl1(A-/-) adipocytes incorporated [(14)C]oleate into glycerolipids normally, but fatty acid (FA) oxidation rates were 50%-90% lower than in control adipocytes and mitochondria. Acsl1(A-/-) mice were markedly cold intolerant, and beta(3)-adrenergic agonists did not increase oxygen consumption, despite normal adrenergic signaling in brown adipose tissue. The reduced adipose FA oxidation and marked cold intolerance of Acsl1(A-/-) mice indicate that normal activation of FA for oxidation in adipose tissue in vivo requires ACSL1. Thus, ACSL1 has a specific function in directing the metabolic partitioning of FAs toward beta-oxidation in adipocytes.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adipose Tissue, Brown / metabolism
  • Adrenergic Agonists / pharmacology
  • Animals
  • Coenzyme A Ligases / genetics
  • Coenzyme A Ligases / metabolism*
  • Cold Temperature*
  • Diet, Fat-Restricted
  • Fatty Acids / metabolism*
  • Mice
  • Mice, Knockout
  • Oxidation-Reduction
  • Thermogenesis*

Substances

  • Adrenergic Agonists
  • Fatty Acids
  • ACSL1 protein, mouse
  • Coenzyme A Ligases