Identification of a novel glucose transporter-like protein—GLUT-12

Identification of a novel glucose transporter-like protein—GLUT-12 Abstract Facilitative glucose transporters exhibit variable hexose affinity and tissue-specific expression. These characteristics contribute to specialized metabolic properties of cells. Here we describe the characterization of a novel glucose transporter-like molecule, GLUT-12. GLUT-12 was identified in MCF-7 breast cancer cells by homology to the insulin-regulatable glucose transporter GLUT-4. The GLUT-12 cDNA encodes 617 amino acids, which possess features essential for sugar transport. Di-leucine motifs are present in NH 2 and COOH termini at positions similar to the GLUT-4 FQQI and LL targeting motifs. GLUT-12 exhibits 29% amino acid identity with GLUT-4 and 40% to the recently described GLUT-10. Like GLUT-10, a large extracellular domain is predicted between transmembrane domains 9 and 10. Genomic organization of GLUT-12 is highly conserved with GLUT-10 but distinct from GLUTs 1–5. Immunofluorescence showed that, in the absence of insulin, GLUT-12 is localized to the perinuclear region in MCF-7 cells. Immunoblotting demonstrated GLUT-12 expression in skeletal muscle, adipose tissue, and small intestine. Thus GLUT-12 is potentially part of a second insulin-responsive glucose transport system. facilitative glucose transporter insulin-responsive tissues breast cancer Footnotes This work was supported by the National Health and Medical Research Council (NHMRC) of Australia, the Diabetes Australia Research Trust, the Eli Lilly Australia Research Grant Programme, and St. Vincent's Hospital Melbourne Research and Grants Committee. D. E. James is the recipient of a Principal NHMRC Research Fellowship. Address for reprint requests and other correspondence: S. Rogers, The Univ. of Melbourne Dept. of Medicine, St. Vincent's Hospital Melbourne, Victoria Parade, Fitzroy, Victoria 3065, Australia (E-mail: s.rogers@medicine.unimelb.edu.au ). 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. Copyright © 2002 the American Physiological Society http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png AJP - Endocrinology and Metabolism The American Physiological Society

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Publisher
The American Physiological Society
Copyright
Copyright © 2011 the American Physiological Society
ISSN
0193-1849
eISSN
1522-1555
Publisher site
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Abstract

Abstract Facilitative glucose transporters exhibit variable hexose affinity and tissue-specific expression. These characteristics contribute to specialized metabolic properties of cells. Here we describe the characterization of a novel glucose transporter-like molecule, GLUT-12. GLUT-12 was identified in MCF-7 breast cancer cells by homology to the insulin-regulatable glucose transporter GLUT-4. The GLUT-12 cDNA encodes 617 amino acids, which possess features essential for sugar transport. Di-leucine motifs are present in NH 2 and COOH termini at positions similar to the GLUT-4 FQQI and LL targeting motifs. GLUT-12 exhibits 29% amino acid identity with GLUT-4 and 40% to the recently described GLUT-10. Like GLUT-10, a large extracellular domain is predicted between transmembrane domains 9 and 10. Genomic organization of GLUT-12 is highly conserved with GLUT-10 but distinct from GLUTs 1–5. Immunofluorescence showed that, in the absence of insulin, GLUT-12 is localized to the perinuclear region in MCF-7 cells. Immunoblotting demonstrated GLUT-12 expression in skeletal muscle, adipose tissue, and small intestine. Thus GLUT-12 is potentially part of a second insulin-responsive glucose transport system. facilitative glucose transporter insulin-responsive tissues breast cancer Footnotes This work was supported by the National Health and Medical Research Council (NHMRC) of Australia, the Diabetes Australia Research Trust, the Eli Lilly Australia Research Grant Programme, and St. Vincent's Hospital Melbourne Research and Grants Committee. D. E. James is the recipient of a Principal NHMRC Research Fellowship. Address for reprint requests and other correspondence: S. Rogers, The Univ. of Melbourne Dept. of Medicine, St. Vincent's Hospital Melbourne, Victoria Parade, Fitzroy, Victoria 3065, Australia (E-mail: s.rogers@medicine.unimelb.edu.au ). 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. Copyright © 2002 the American Physiological Society

Journal

AJP - Endocrinology and MetabolismThe American Physiological Society

Published: Mar 1, 2002

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