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J Biol Chem, Vol. 274, Issue 15, 10071-10078, April 9, 1999
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From the The precise mechanisms underlying
insulin-stimulated glucose transport still require investigation. Here
we assessed the effect of SB203580, an inhibitor of the p38 MAP kinase
family, on insulin-stimulated glucose transport in 3T3-L1 adipocytes
and L6 myotubes. We found that SB203580, but not its inactive analogue
(SB202474), prevented insulin-stimulated glucose transport in both cell
types with an IC50 similar to that for inhibition of
p38 MAP kinase (0.6 µM). Basal glucose uptake was not
affected. Moreover, SB203580 added only during the transport assay did
not inhibit basal or insulin-stimulated transport. SB203580 did not
inhibit insulin-stimulated translocation of the glucose transporters
GLUT1 or GLUT4 in 3T3-L1 adipocytes as assessed by immunoblotting of
subcellular fractions or by immunofluorescence of membrane lawns. L6
muscle cells expressing GLUT4 tagged on an extracellular domain with a
Myc epitope (GLUT4myc) were used to assess the functional insertion of
GLUT4 into the plasma membrane. SB203580 did not affect the
insulin-induced gain in GLUT4myc exposure at the cell surface but
largely reduced the stimulation of glucose uptake. SB203580 had no
effect on insulin-dependent insulin receptor substrate-1
phosphorylation, association of the p85 subunit of phosphatidylinositol
3-kinase with insulin receptor substrate-1, nor on phosphatidylinositol
3-kinase, Akt1, Akt2, or Akt3 activities in 3T3-L1 adipocytes. In
conclusion, in the presence of SB203580, insulin caused normal
translocation and cell surface membrane insertion of glucose
transporters without stimulating glucose transport. We propose that
insulin stimulates two independent signals contributing to stimulation
of glucose transport: phosphatidylinositol 3-kinase leads to glucose
transporter translocation and a pathway involving p38 MAP kinase leads
to activation of the recruited glucose transporter at the membrane.
Programme in Cell Biology,
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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