Monensin stimulates sugar transport in avian erythrocytes.
The cell-medium distribution of the nonmetabolized glucose analog, 3-O-methyl-D-glucose was studied in pigeon erythrocytes. The sodium ionophore monensin increased in parallel and in a dose-dependent manner the influx of hexose and of Na+. These effects were independent of external Ca2+ and there was no alteration in 45Ca influx. If, as suggested previously, hexose transport in these cells is modulated by cytoplasmic Ca2+, the stimulatory effect of monensin on hexose transport may be due to increased mitochondrial Ca2+ efflux via Na+-Ca2+ exchange, owing to the elevation of cytoplasmic Na+. Such a mechanism is consistent with the observed failure of monensin to affect 3-O-methyl-D-glucose transport in cells partially depleted of Ca2+. Monensin also depressed cellular ATP levels but the data favour a Ca2+-dependent mechanism of hexose transport regulation rather than a direct effect of metabolic depletion. The inhibitor of specific-mediated hexose transport, cytochalasin B was found to inhibit equally basal and stimulated 3-O-methyl-D-glucose uptake but there was a cytochalasin B-insensitive uptake component in excess of L-glucose uptake. This appears to reflect a greater diffusional permeability of 3-O-methyl-D-glucose than of L-glucose.
D019325:3-O-Methylglucose; D000818:Animals; D001693:Biological Transport, Active / Q000187:drug effects; D010856:Columbidae; D003571:Cytochalasin B / Q000494:pharmacology; D004912:Erythrocytes / Q000187:drug effects / Q000378:metabolism*; D005663:Furans / Q000494:pharmacology*; D007700:Kinetics; D008757:Methylglucosides / Q000097:blood; D008985:Monensin / Q000494:pharmacology*; D009004:Monosaccharide Transport Proteins / Q000097:blood*; D011188:Potassium / Q000097:blood; D012964:Sodium / Q000097:blood
D005663:Furans; D008757:Methylglucosides; D009004:Monosaccharide Transport Proteins; D019325:3-O-Methylglucose; D003571:Cytochalasin B; D008985:Monensin; D012964:Sodium; D011188:Potassium