Regulation of glucose uptake by stressed cells

✍ Scribed by C. A. Pasternak; J. E. J. Aiyathurai; V. Makinde; A. Davies; S. A. Baldwin; E. M. Konieczko; C. C. Widnell

• Publisher: John Wiley and Sons
• Year: 1991
• Tongue: English
• Weight: 976 KB
• Volume: 149
• Category: Article
• ISSN: 0021-9541
• DOI: 10.1002/jcp.1041490221

✦ Synopsis

Lactate production by BHK cells is stimulated by arsenite, azide, or by infection with Semliki Forest virus (SFV). In the case of arsenite or SFV infection, the increase correlates approximately with the increase in glucose transport a5 measured by uptake of ['HI deoxy glucose (dGlc); in the case of azide, the increase in lactate production exceeds that of glucose transport. Hence glucose utilization by BHK cells and its stimulation by anaerobic and other types of cellular stress is controlled at least in part at the level of glucose transport. The glucose uptake by BHK cells is also stimulated by serum and by glucose deprivation. In these circumstances, as with arsenite, stimulation is reversible, with t,,? of 1-2 hours; stimulation is compatible with a translocation of the glucose transporter protein between an intracellular site and the plasma membrane (shown here for serum and previously for arsenite). The suriace binding and rate of internalization of ['2'11-labelled transferrin and ['251] a2 -macroglobulin was studied to determine whether changes in glucose transport are accompanied by changes in the surface concentration or rate of internalization of membrane proteins. The findings indicate that changes in glucose transport do not reflect a consistent and general redistribution of membrane receptors. Taken together, the results are compatible with the proposal that BHK cells exposed to stimuli like insulin or serum, or to stresses like arsenite, azide, SFV infection, or deprivation of glucose, respond in the same manner: namely, by an increased capacity to transport glucose brought about by reversible and speciiic translocation of the transporter protein from an (inactive) intracellular site to the plasma membrane.