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AJP - Cell Physiology, Vol 259, Issue 4 C647-C653, Copyright © 1990 by American Physiological Society
ARTICLES |
D. W. Lundgren and C. V. Vacca
Department of Pediatrics, Case Western Reserve Univesity, Cleveland, Ohio 44109.
This report examines the effect of nonmetabolizable glucose analogues on ornithine decarboxylase (ODC) activity in LLC-PK1 cells. The addition of Na(+)-dependent cotransported glucose analogues, 1-O-methyl-alpha-D-glucopyranoside (alpha-MDG) and 1-O-methyl-beta-D-glucopyranoside, to Earle's balanced salt solution minus glucose (EBSS-G) increased ODC activity five- to sevenfold above basal levels. The passive carrier-mediated transported glucose analogue 3-O-methyl-D-glucopyranose had very little effect on enzyme activity. alpha-MDG increased ODC activity in quiescent but not growing cells. ODC activity increased as a function of both the incubation time in EBSS-G + alpha-MDG and the concentration of alpha-MDG in EBSS-G. Phlorizin significantly reduced the level of enzyme activity induced by alpha-MDG. ODC expression by alpha-MDG was reduced in cells incubated in hypertonic EBSS-G + alpha-MDG. Enzyme activity, in the absence of extracellular organic substrates, was markedly elevated in cells incubated in hypotonic media. It is suggested that an influx of Na+ and/or an increase in cell volume elevates one or more signal transducers that regulate ODC expression.
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