Replacement of intracellular C-terminal domain of GLUT1 glucose transporter with that of GLUT2 increases V(max) and K(m) of transport activity

H. Katagiri, T. Asano, H. Ishihara, K. Tsukuda, J. L. Lin, K. Inukai, M. Kikuchi, Y. Yazaki, Y. Oka

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48 Citations (Scopus)

Abstract

The intracellular C-terminal domain is diverse in size and amino acid sequence among facilitative glucose transporter isoforms. The characteristics of glucose transport are also divergent, and GLUT2 has far higher K(m) and V(max) values compared with GLUT1. To investigate the role of the intracellular C-terminal domain in glucose transport, we expressed in Chinese hamster ovary cells the mutated GLUT1 protein whose intracellular C-terminal domain was replaced with that of GLUT2 by means of engineering the chimeric cDNA. Cytochalasin B, for which GLUT2 protein has much lower affinity, bound to this chimeric protein in a fashion similar to GLUT1. In contrast, greater transport activity was observed in this chimeric glucose transporter compared with the wild-type GLUT1 at 10 mM 2-deoxy-D-glucose concentration. The kinetic studies on 2-deoxy-D-glucose uptake revealed a 3.8-fold increase in K(m) and a 4.3-fold increase in V(max) in this chimeric glucose transporter compared with the wild-type GLUT1. Thus, replacement of the intracellular C- terminal domain confers the GLUT2-like property on the glucose transporter. These results strongly suggest that the diversity of intracellular C-terminal domain contributes to the diversity of glucose transport characteristics among isoforms.

Original languageEnglish
Pages (from-to)22550-22555
Number of pages6
JournalJournal of Biological Chemistry
Volume267
Issue number31
Publication statusPublished - 1992
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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