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Volume 272, Number 11, Issue of March 14, 1997 pp. 7085-7092
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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Insulin-induced Recruitment of Glucose Transporter 4 (GLUT4) and GLUT1 in Isolated Rat Cardiac Myocytes
EVIDENCE OF THE EXISTENCE OF DIFFERENT INTRACELLULAR GLUT4 VESICLE POPULATIONS

(Received for publication, September 27, 1996, and in revised form, December 13, 1996)

Yvan Fischer , Julia Thomas , Lidia Sevilla ^¶ , Purificación Muñoz ^¶ , Christoph Becker , Geoffrey Holman , Izabela J. Kozka , Manuel Palacín ^¶ , Xavier Testar ^¶ , Helmut Kammermeier and Antonio Zorzano ^¶

From the  Institute of Physiology, Medical Faculty, RWTH Aachen, Pauwelsstrasse 30, Aachen  D-52057, Federal Republic of Germany, ^¶ Departament de Bioquímica i Biologia Molecular, Facultat de Biologia, Universitat de Barcelona, Avda. Diagonal 645, 08028 Barcelona, Spain, and  Department of Biochemistry, University of Bath, Claverton Down, Bath BA2 7AY, United Kingdom

Using isolated rat cardiomyocytes we have examined: 1) the effect of insulin on the cellular distribution of glucose transporter 4 (GLUT4) and GLUT1, 2) the total amount of these transporters, and 3) the co-localization of GLUT4, GLUT1, and secretory carrier membrane proteins (SCAMPs) in intracellular membranes. Insulin induced 5.7- and 2.7-fold increases in GLUT4 and GLUT1 at the cell surface, respectively, as determined by the nonpermeant photoaffinity label [³H]2-N-[4(1-azi-2,2,2-trifluoroethyl)benzoyl]-1,3-bis-(D-mannos-4-yloxy)propyl-2-amine. The total amount of GLUT1, as determined by quantitative Western blot analysis of cell homogenates, was found to represent a substantial fraction (~30%) of the total glucose transporter content. Intracellular GLUT4-containing vesicles were immunoisolated from low density microsomes by using monoclonal anti-GLUT4 (1F8) or anti-SCAMP antibodies (3F8) coupled to either agarose or acrylamide. With these different immunoisolation conditions two GLUT4 membrane pools were found in nonstimulated cells: one pool with a high proportion of GLUT4 and a low content in GLUT1 and SCAMP 39 (pool 1) and a second GLUT4 pool with a high content of GLUT1 and SCAMP 39 (pool 2). The existence of pool 1 was confirmed by immunotitration of intracellular GLUT4 membranes with 1F8-acrylamide. Acute insulin treatment caused the depletion of GLUT4 in both pools and of GLUT1 and SCAMP 39 in pool 2. In conclusion: 1) GLUT4 is the major glucose transporter to be recruited to the surface of cardiomyocytes in response to insulin; 2) these cells express a high level of GLUT1; and 3) intracellular GLUT4-containing vesicles consist of at least two populations, which is compatible with recently proposed models of GLUT4 trafficking in adipocytes.

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