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J. Biol. Chem., Vol. 268, Issue 16, 11691-11696, Jun, 1993
G Thoidis, N Kotliar and PF Pilch
In adipocytes and muscle, insulin stimulates the translocation of glucose
transporter proteins from an intracellular vesicle pool to the plasma
membrane. To study the molecular basis of this process, we used the
anti-GLUT4 antibody 1F8 to isolate intracellular vesicles from rat
adipocytes that are enriched in the muscle/fat glucose transporter isoform.
These vesicles were then used as immunogens to generate monoclonal
antibodies against their protein components. We isolated an antibody, 3F8,
that recognizes three polypeptides, designated GTV3, migrating in the
36-40-kDa range as analyzed by SDS-polyacrylamide gel electrophoresis and
Western blotting. These proteins are enriched in GLUT4-containing vesicles,
and the two smallest of the polypeptides recognized by 3F8 translocate to
the cell surface in response to insulin. GTV3 proteins are also present in
plasma membranes of fat cells and liver as well as in a wide number of
tissues, red blood cells being the only exception. In adipocytes from
streptozotocin-induced diabetic rats, GTV3 protein levels decrease
dramatically and return to normal levels when animals are treated with
insulin. The localization of GTV3 in glucose transporter-containing
vesicles as well as their wide tissue distribution suggests that these
proteins may be involved in vesicle mediated transport and regulated
trafficking between membrane compartments.
Immunological analysis of GLUT4-enriched vesicles. Identification of novel proteins regulated by insulin and diabetes
Department of Biochemistry, Boston University School of Medicine, Massachusetts 02118.
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