author_facet Lundgren, D. W.
Vacca, C. V.
Lundgren, D. W.
Vacca, C. V.
author Lundgren, D. W.
Vacca, C. V.
spellingShingle Lundgren, D. W.
Vacca, C. V.
American Journal of Physiology-Cell Physiology
Nonmetabolizable glucose analogues and ornithine decarboxylase expression in LLC-PK1 cells
Cell Biology
Physiology
author_sort lundgren, d. w.
spelling Lundgren, D. W. Vacca, C. V. 0363-6143 1522-1563 American Physiological Society Cell Biology Physiology http://dx.doi.org/10.1152/ajpcell.1990.259.4.c647 <jats:p>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.</jats:p> Nonmetabolizable glucose analogues and ornithine decarboxylase expression in LLC-PK1 cells American Journal of Physiology-Cell Physiology
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series American Journal of Physiology-Cell Physiology
source_id 49
title Nonmetabolizable glucose analogues and ornithine decarboxylase expression in LLC-PK1 cells
title_unstemmed Nonmetabolizable glucose analogues and ornithine decarboxylase expression in LLC-PK1 cells
title_full Nonmetabolizable glucose analogues and ornithine decarboxylase expression in LLC-PK1 cells
title_fullStr Nonmetabolizable glucose analogues and ornithine decarboxylase expression in LLC-PK1 cells
title_full_unstemmed Nonmetabolizable glucose analogues and ornithine decarboxylase expression in LLC-PK1 cells
title_short Nonmetabolizable glucose analogues and ornithine decarboxylase expression in LLC-PK1 cells
title_sort nonmetabolizable glucose analogues and ornithine decarboxylase expression in llc-pk1 cells
topic Cell Biology
Physiology
url http://dx.doi.org/10.1152/ajpcell.1990.259.4.c647
publishDate 1990
physical C647-C653
description <jats:p>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.</jats:p>
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author Lundgren, D. W., Vacca, C. V.
author_facet Lundgren, D. W., Vacca, C. V., Lundgren, D. W., Vacca, C. V.
author_sort lundgren, d. w.
container_issue 4
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container_title American Journal of Physiology-Cell Physiology
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description <jats:p>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.</jats:p>
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spelling Lundgren, D. W. Vacca, C. V. 0363-6143 1522-1563 American Physiological Society Cell Biology Physiology http://dx.doi.org/10.1152/ajpcell.1990.259.4.c647 <jats:p>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.</jats:p> Nonmetabolizable glucose analogues and ornithine decarboxylase expression in LLC-PK1 cells American Journal of Physiology-Cell Physiology
spellingShingle Lundgren, D. W., Vacca, C. V., American Journal of Physiology-Cell Physiology, Nonmetabolizable glucose analogues and ornithine decarboxylase expression in LLC-PK1 cells, Cell Biology, Physiology
title Nonmetabolizable glucose analogues and ornithine decarboxylase expression in LLC-PK1 cells
title_full Nonmetabolizable glucose analogues and ornithine decarboxylase expression in LLC-PK1 cells
title_fullStr Nonmetabolizable glucose analogues and ornithine decarboxylase expression in LLC-PK1 cells
title_full_unstemmed Nonmetabolizable glucose analogues and ornithine decarboxylase expression in LLC-PK1 cells
title_short Nonmetabolizable glucose analogues and ornithine decarboxylase expression in LLC-PK1 cells
title_sort nonmetabolizable glucose analogues and ornithine decarboxylase expression in llc-pk1 cells
title_unstemmed Nonmetabolizable glucose analogues and ornithine decarboxylase expression in LLC-PK1 cells
topic Cell Biology, Physiology
url http://dx.doi.org/10.1152/ajpcell.1990.259.4.c647