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This version published online on April 17, 2003
Molecular Endocrinology, doi:10.1210/me.2003-0057
Molecular Endocrinology Vol. 0, No. 2003 200300571-
doi:10.1210/me.2003-0057
Copyright © 2003 by the Endocrine Society.
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Submitted on February 17, 2003
Accepted on April 11, 2003

Inhibition of protein kinase C{beta}II increases glucose uptake in 3T3-L1 adipocytes through elevated expression of GLUT-1 at the plasma membrane

Remko R. Bosch1*, Merlijn Bazuine1, Michelle M. Wake1, Paul N. Span1, André J. Olthaar1, Annette Schürmann1, J. Antonie Maassen1, Ad R.M.M. Hermus1, Peter H.G.M. Willems1, and C. G.J. (Fred) Sweep1

1 Department of Chemical Endocrinology, University Medical Centre Nijmegen, The Netherlands; Department of Endocrinology, University Medical Centre Nijmegen, The Netherlands; Department of Molecular Cell Biology, Leiden University Medical Center, Leiden, The Netherlands; Department of Pharmacology, German Institute of Human Nutrition, Potsdam-Rehbrücke, Germany; Department of Biochemistry, University Medical Centre Nijmegen, The Netherlands

* To whom correspondence should be addressed. E-mail: R.Bosch{at}ace.umcn.nl.

The mechanism via which diacylglycerol-sensitive Protein Kinase Cs (PKCs) stimulate glucose transport in insulin-sensitive tissues is poorly defined. Phorbol esters, such as PMA, are potent activators of conventional and novel PKCs. Addition of PMA increases the rate of glucose uptake in many different cell systems. We aimed to investigate the mechanism via which PMA stimulates glucose transport in 3T3-L1 adipocytes in more detail. We observed a good correlation between the rate of disappearance of PKC{beta}II during prolonged PMA treatment and the increase in glucose uptake. Moreover, inhibition of PKC{beta}II with a specific myristoylated PKC{beta}C2-4 peptide inhibitor significantly increased the rate of glucose transport. Western blot analysis demonstrated that both PMA treatment and incubation with the myristoylated PKC{beta}C2-4 pseudosubstrate resulted in more GLUT-1 but not GLUT-4 at the plasma membrane. To our knowledge, we are the first to demonstrate that inactivation of PKC, mostly likely PKC{beta}II, elevates glucose uptake in 3T3-L1 adipocytes. The observation that PKC{beta}II influences the rate of glucose uptake through manipulation of GLUT-1 expression levels at the plasma membrane might reveal a yet unidentified regulatory mechanism involved in glucose homeostasis.
Key words: 3T3-L1 adipocytes • protein kinase C • glucose uptake • down-regulation • myristoylated PKC{beta}C2-4 peptide inhibitor




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