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J. Biol. Chem., Vol. 276, Issue 30, 27816-27824, July 27, 2001
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From the Institute for Molecular Bioscience and the
¶ Department of Physiology and Pharmacology, University of
Queensland, St. Lucia, Queensland 4072, Australia
We have examined the requirement for
Ca2+ in the signaling and trafficking pathways involved in
insulin-stimulated glucose uptake in 3T3-L1 adipocytes. Chelation of
intracellular Ca2+, using 1,2-bis
(o-aminophenoxy)ethane-N,N,N',N'-tetraacetic
acid tetra (acetoxy- methyl) ester (BAPTA-AM), resulted in >95%
inhibition of insulin-stimulated glucose uptake. The calmodulin
antagonist, W13, inhibited insulin-stimulated glucose uptake by 60%.
Both BAPTA-AM and W13 inhibited Akt phosphorylation by 70-75%.
However, analysis of insulin-dose response curves indicated that this
inhibition was not sufficient to explain the effects of BAPTA-AM and
W13 on glucose uptake. BAPTA-AM inhibited insulin-stimulated
translocation of GLUT4 by 50%, as determined by plasma membrane lawn
assay and subcellular fractionation. In contrast, the
insulin-stimulated appearance of HA-tagged GLUT4 at the cell
surface, as measured by surface binding, was blocked by BAPTA-AM. While
the ionophores A23187 or ionomycin prevented the inhibition of Akt
phosphorylation and GLUT4 translocation by BAPTA-AM, they did not
overcome the inhibition of glucose transport. Moreover, glucose uptake
of cells pretreated with insulin followed by rapid cooling to 4 °C,
to promote cell surface expression of GLUT4 and prevent subsequent endocytosis, was inhibited specifically by BAPTA-AM. This indicates that inhibition of glucose uptake by BAPTA-AM is independent of both
trafficking and signal transduction. These data indicate that
Ca2+ is involved in at least two different steps of the
insulin-dependent recruitment of GLUT4 to the plasma
membrane. One involves the translocation step. The second involves the
fusion of GLUT4 vesicles with the plasma membrane. These data are
consistent with the hypothesis that Ca2+/calmodulin plays a
fundamental role in eukaryotic vesicle docking and fusion. Finally,
BAPTA-AM may inhibit the activity of the facilitative transporters by
binding directly to the transporter itself.
The Role of Ca2+ in Insulin-stimulated Glucose
Transport in 3T3-L1 Cells*
,
*
This work was supported by the National Health and Medical
Research Council of Australia and the Juvenile Diabetes Foundation International. The Institute for Molecular Bioscience is a Special Research Center of the Australian Research Council.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Wellcome Prize Traveling Fellow. To whom all correspondence should
be addressed: Inst. for Molecular Bioscience, University of Queensland,
Ritchie Research Bldg., Research Rd., St. Lucia, QLD 4072, Australia.
Tel.: 617-3365-4991; Fax: 617-3365-4388; E-mail:
J.Whitehead@imb.uq.edu.au.
§
Recipient of a fellowship from Subprograma General de
Perfeccionamiento de Doctores en el Extranjero, S.E.U.I.D, Ministerio de Educacion y Cultura, Spain.
Principal Research Fellow of the National Health and Medical
Research Council of Australia.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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