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(Received for publication, April 7, 1997, and in revised form, May 5, 1997)
From the Dehydroascorbic acid (DHA) is rapidly taken up by
cells and reduced to ascorbic acid (AA). Using the Xenopus
laevis oocyte expression system we examined transport of DHA and
AA via glucose transporter isoforms GLUT1-5 and SGLT1. The apparent
Km of DHA transport via GLUT1 and GLUT3 was
1.1 ± 0.2 and 1.7 ± 0.3 mM, respectively. High
performance liquid chromatography analysis confirmed 100% reduction of
DHA to AA within oocytes. GLUT4 transport of DHA was only 2-4-fold
above control and transport kinetics could not be calculated. GLUT2,
GLUT5, and SGLT1 did not transport DHA and none of the isoforms
transported AA. Radiolabeled sugar transport confirmed transporter
function and identity of all cDNA clones was confirmed by
restriction fragment mapping. GLUT1 and GLUT3 cDNA were further
verified by polymerase chain reaction. DHA transport activity in both
GLUT1 and GLUT3 was inhibited by 2-deoxyglucose, D-glucose,
and 3-O-methylglucose among other hexoses while fructose
and L-glucose showed no inhibition. Inhibition by the
endofacial inhibitor, cytochalasin B, was non-competitive and
inhibition by the exofacial inhibitor,
4,6-O-ethylidene-
Volume 272, Number 30,
Issue of July 25, 1997
pp. 18982-18989
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
,
and
NIDDK, National Institutes of Health,
Bethesda, Maryland 20892 and the ¶ Department of Medicine,
University of Chicago, Chicago, Illinois 60637
-glucose, was competitive. Expressed
mutant constructs of GLUT1 and GLUT3 did not transport DHA. DHA and
2-deoxyglucose uptake by Chinese hamster ovary cells overexpressing
either GLUT1 or GLUT3 was increased 2-8-fold over control cells. These
studies suggest GLUT1 and GLUT3 isoforms are the specific glucose
transporter isoforms which mediate DHA transport and subsequent
accumulation of AA.
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