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1 Copenhagen Muscle Research Center, Department of Human Physiology, University of Copenhagen, DK-2100 Copenhagen, Denmark; 2 Centre de Recherche en Rhumatologie et Immunologie, Centre de Recherche du Pavillon CHUL, Sainte-Foy, Quebec G1V 4G2, 3 Division of Cell Biology, The Hospital for Sick Children, Toronto, Ontario M5G 1X8, Canada; and 4 Centre National de la Recherche Scientifique, Institute de Pharmacologie Moleculaire et Cellulaire, Sophia Antipolis, 06560 Valbonne, France
GLUT-4-containing membranes
immunoprecipitated from insulin-stimulated rat skeletal muscle produce
the phospholipase D (PLD) product phosphatidic acid. In vitro
stimulation of PLD in crude membrane with ammonium sulfate (5 mM)
resulted in transfer of GLUT-4 (3.0-fold vs. control) as well as
transferrin receptor proteins from large to small membrane structures.
The in vitro GLUT-4 transfer could be blocked by neomycin (a PLD
inhibitor), and neomycin also reduced insulin-stimulated glucose
transport in intact incubated soleus muscles. Furthermore, protein
kinase B
(PKB) was found to associate
with the GLUT-4 protein and was transferred to small vesicles in
response to ammonium sulfate in vitro. Finally, addition of cytosolic
proteins, prepared from basal skeletal muscle, and GTP nucleotides to
an enriched GLUT-4 membrane fraction resulted in in vitro transfer of
GLUT-4 to small membranes (6.8-fold vs. unstimulated control). The
cytosol and nucleotide-induced GLUT-4 transfer could be blocked by
neomycin and N-ethylmaleimide. In conclusion, we have
developed a cell-free assay that demonstrates in vitro GLUT-4 transfer.
This transfer may suggest release of GLUT-4-containing vesicles from
donor GLUT-4 membranes involving PLD activity and binding of
PKB to GLUT-4.
glucose transport; adenosine diphosphate ribosylation factors; protein kinase B; neomycin
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