Regulation of glucose uptake by stressed cells

Abstract

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 as measured by uptake of [3H] 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 t1/2 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 surface binding and rate of internalization of [125I]-labelled transferrin and [125I] alpha 2-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 specific translocation of the transporter protein from an (inactive) intracellular site to the plasma membrane.

Streptozotocin diabetes and the expression of GLUT1 at the brush border and basolateral membranes of intestinal enterocytes

“…However, a cytoplasmic localisation for a plasma membrane protein that cycles through the endocytic compartment is to be expected. Indeed, intense intracellular vesicular staining for GLUT1 in BHK cells, particularly in the perinuclear region, has been reported and the transporters move from this compartment to the cell surface in response to a variety of stimuli including metabolic stress [18].…”

Examination of the effects of arsenic on glucose homeostasis in cell culture and animal studies: Development of a mouse model for arsenic-induced diabetes

“…These studies used high concentrations of arsenicals that are cytotoxic for most cell types. Here, PAO (50 μM) or iAs III (200-1000 μM) have been shown to stimulate basal, insulin-independent, glucose uptake in baby hamster kidney (BHK) cells (Pasternak et al, 1991;Sviderskaya et al, 1996;Warren et al, 1986;Widnell et al, 1990), bovine chromaffin cells (Fladeby and Serck-Hanssen, 1999), 3T3-L1 adipocytes (Bazuine et al, 2004;Bazuine et al, 2003;Gould et al, 1989) and in L6 myotubes (McDowell et al, 1997). A modest 1-3 fold increase in basal glucose uptake was typically found with no effect on the translocation of GLUT4, an insulin-sensitive glucose transporter, to the plasma membrane.…”

Acute regulation of glucose transport in a monocyte–macrophage cell line: Glut-3 affinity for glucose is enhanced during the respiratory burst

“…Stress induced by a variety of reagents stimulates glucose transport by translocating transporters from intracellular sites to the plasma membrane [12] or by increasing transporter expression [13]. In contrast, glucose deprivation or Cd# + treatment of 3T3L1 cells [14,15] or treatment of Chinese hamster V29 lung fibroblasts with allose [16] modulates the intrinsic activity of Glut-1.…”