Lipin1-Mediated Repression of Adipogenesis by Rutin

Am J Chin Med. 2016;44(3):565-78. doi: 10.1142/S0192415X16500312. Epub 2016 Apr 24.

Abstract

Rutin, also called rutoside or quercetin-3-O-rutinoside and sophorin, is a glycoside between the flavonol quercetin and the disaccharide rutinose. Although many effects of rutin have been reported in vitro and in vivo, the anti-adipogenic effects of rutin have not been fully reported. The aim of this study was to confirm how rutin regulates adipocyte related factors. In this study, rutin decreased the expressions of adipogenesis-related genes, including peroxisome proliferators, activated receptor [Formula: see text] (PPAR[Formula: see text], CCAAT/enhancer-binding protein [Formula: see text] (C/EBP[Formula: see text], fatty acid synthase, adipocyte fatty acid-binding protein, and lipoprotein lipase in 3T3-L1 cells. Rutin also repressed the expression of lipin1, which is an upstream regulator that controls PPAR[Formula: see text] and C/EBP[Formula: see text]. In addition, when 3T3-L1 was transfected with lipin1 siRNA to block lipin1 function, rutin did not affect the expressions of PPAR[Formula: see text] and C/EBP[Formula: see text]. These results suggest that rutin has an anti-adipogenic effect that acts through the suppression of lipin1, as well as PPAR[Formula: see text] and C/EBP[Formula: see text].

Keywords: 3T3-L1; Lipin1; Rutin; siRNA.

MeSH terms

  • 3T3 Cells
  • AMP-Activated Protein Kinases / physiology
  • Adipogenesis / drug effects*
  • Adipogenesis / genetics*
  • Animals
  • CCAAT-Enhancer-Binding Proteins / genetics
  • CCAAT-Enhancer-Binding Proteins / metabolism
  • Cell Differentiation / drug effects
  • Cell Differentiation / genetics
  • Cell Survival / drug effects
  • Cell Survival / genetics
  • Lipid Metabolism / drug effects
  • Lipid Metabolism / genetics
  • Mice
  • Nuclear Proteins / antagonists & inhibitors
  • Nuclear Proteins / physiology*
  • PPAR gamma / genetics
  • PPAR gamma / metabolism
  • Phosphatidate Phosphatase / antagonists & inhibitors
  • Phosphatidate Phosphatase / physiology*
  • Rutin / pharmacology*
  • Signal Transduction / drug effects
  • Signal Transduction / genetics

Substances

  • CCAAT-Enhancer-Binding Proteins
  • CEBPA protein, mouse
  • Nuclear Proteins
  • PPAR gamma
  • Rutin
  • AMP-Activated Protein Kinases
  • Lpin1 protein, mouse
  • Phosphatidate Phosphatase