DOI: 10.1042/bj3010177. Insulin-induced translocation of the glucose transporter GLUT4 in cardiac muscle: studies on the role of small-molecular-mass GTP-binding proteins

Insulin-induced translocation of the glucose transporter GLUT4 in cardiac muscle: studies on the role of small-molecular-mass GTP-binding proteins

10.1042/bj3010177

Crossref journal-article

Portland Press Ltd.

Biochemical Journal (288)

Abstract

Subcellular fractions obtained from rat cardiac ventricular tissue were used to elucidate a possible functional relationship between small-molecular-mass G-proteins and the insulin-responsive glucose transporter GLUT4. Proteins were separated by SDS/PAGE and transferred to nitrocellulose membranes. Incubation with [alpha-32P]GTP revealed the presence of two major distinct GTP-binding protein bands of 24 and 26 kDa in both plasma and microsomal membranes. Immunoadsorption of microsomal membranes to anti-GLUT4 antibodies was used to isolate GLUT4-enriched membrane vesicles. This material was found to contain a much decreased amount of small G-proteins, with the exclusive presence of the 24 kDa species. Insulin treatment in vivo had no effect on the microsomal membrane content of small GTP-binding proteins, but significantly decreased the 24 kDa species in GLUT4-enriched vesicles by 36 +/- 5% (n = 3). This correlated with a decreased (30-40%) recovery of GLUT4-enriched vesicles from insulin-treated animals. Western-blot analysis of microsomal membranes with a panel of antisera against rab GTP-binding proteins indicated the presence of rab4A, with a molecular mass of 24 kDa, whereas rab1A, rab2 and rab6 were not observed. rab4A was barely detectable in GLUT4-enriched vesicles; however, insulin produced an extensive shift of rab4A from the cytosol and the microsomal fraction to the plasma membrane with a parallel increase in GLUT4. These data show that a small GTP-binding protein is co-localized with GLUT4 in an insulin-responsive intracellular compartment, and strongly suggest that this protein is involved in the exocytosis of GLUT4 in cardiac muscle. Furthermore, the observed translocation of rab4A is compatible with insulin-induced endosome recycling processes, possibly including the glucose transporters.

Bibliography

Uphues, I., Kolter, T., Goud, B., & Eckel, J. (1994). Insulin-induced translocation of the glucose transporter GLUT4 in cardiac muscle: studies on the role of small-molecular-mass GTP-binding proteins. Biochemical Journal, 301(1), 177â182.

Authors 4

I Uphues (first)
T Kolter (additional)
B Goud (additional)
J Eckel (additional)

References 0 Referenced 36

None

Dates

Type	When
Created	10 years ago (Aug. 10, 2015, 5:38 p.m.)
Deposited	3 years, 9 months ago (Nov. 23, 2021, 6:03 p.m.)
Indexed	1 year, 2 months ago (June 17, 2024, 4 p.m.)
Issued	31 years, 1 month ago (July 1, 1994)
Published	31 years, 1 month ago (July 1, 1994)
Published Print	31 years, 1 month ago (July 1, 1994)

Funders 0

None

BibTeX

@article{Uphues_1994, title={Insulin-induced translocation of the glucose transporter GLUT4 in cardiac muscle: studies on the role of small-molecular-mass GTP-binding proteins}, volume={301}, ISSN={1470-8728}, url={http://dx.doi.org/10.1042/bj3010177}, DOI={10.1042/bj3010177}, number={1}, journal={Biochemical Journal}, publisher={Portland Press Ltd.}, author={Uphues, I and Kolter, T and Goud, B and Eckel, J}, year={1994}, month=jul, pages={177–182} }

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