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AJP - Endocrinology and Metabolism, Vol 269, Issue 5 E897-E902, Copyright © 1995 by American Physiological Society
ARTICLES |
H. Ishihara, T. Asano, K. Tsukuda, H. Katagiri, K. Inukai, M. Anai, Y. Yazaki, J. Miyazaki, M. Kikuchi and Y. Oka
Institute for Adult Diseases, Asahi Life Foundation, Tokyo, Japan.
Accumulated evidence suggests that GLUT-2, in addition to its role in glucose transport, may also have other functions in glucose-stimulated insulin secretion. As a first step in addressing this possibility, we have engineered MIN6 cells overexpressing human GLUT-2 by transfection with human GLUT-2 cDNA. Stable transformants harboring human GLUT-2 cDNA exhibited an approximately twofold increase in 3-O-methyl-D-glucose uptake at 0.5 and 15 mM. Glucokinase activity or glucose utilization measured by conversion of [5-3H]glucose to [3H]H2O was not, however, altered in the MIN6 cells overexpressing human GLUT-2. Furthermore, glucose-stimulated insulin secretion was not affected by over-expression of human GLUT-2. An abundance of GLUT-2, therefore, does not correlate with the glucose responsiveness of cells in which glycolysis is regulated at the glucose phosphorylating step. These data suggest that GLUT-2 by itself does not have significant functions other than its role in glucose transport in glucose sensing by MIN6 cells.
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