Gallic acid induces GLUT4 translocation and glucose uptake activity in 3T3-L1 cells

FEBS Lett. 2010 Feb 5;584(3):531-6. doi: 10.1016/j.febslet.2009.11.092. Epub 2009 Dec 3.

Abstract

GLUT4, a 12 transmembrane protein, plays a major role in insulin mediated glucose transport in muscle and adipocytes. For glucose transport, the GLUT4 protein needs to be translocated to the plasma membrane from the intracellular pool and it is possible that certain compounds may be able to enhance this process. In the present work, we have shown that gallic acid can increase GLUT4 translocation and glucose uptake activity in an Akt-independent but wortmannin-sensitive manner. Further analysis suggested the role of atypical protein kinase Czeta/lambda in gallic acid mediated GLUT4 translocation and glucose uptake.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3T3-L1 Cells
  • Androstadienes / pharmacology
  • Animals
  • Biological Transport / drug effects*
  • Gallic Acid / pharmacology*
  • Glucose / metabolism*
  • Glucose Transporter Type 4 / metabolism*
  • Mice
  • Protein Kinase Inhibitors / pharmacology
  • Protein Transport / drug effects
  • Wortmannin

Substances

  • Androstadienes
  • Glucose Transporter Type 4
  • Protein Kinase Inhibitors
  • Gallic Acid
  • Glucose
  • Wortmannin