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J Biol Chem, Vol. 275, Issue 16, 11981-11986, April 21, 2000
From the Department of Pathology, Duke University Medical Center,
Durham, North Carolina 27710 and Laboratory of Molecular
Carcinogenesis, NIEHS, National Institutes of Health,
Research Triangle Park, North Carolina 27709
Ischemia is reported to stimulate glucose uptake,
but the signaling pathways involved are poorly understood. Modulation
of glucose transport could be important for the cardioprotective effects of brief intermittent periods of ischemia and reperfusion, termed ischemic preconditioning. Previous work indicates that preconditioning reduces production of acid and lactate during subsequent sustained ischemia, consistent with decreased glucose utilization. However, there are also data that preconditioning enhances
glucose uptake. The present study examines whether preconditioning alters glucose transport and whether this is mediated by either phosphatidylinositol 3-kinase (PI3K) or p38 MAP kinase.
Langendorff-perfused rat hearts were preconditioned with 4 cycles of 5 min of ischemia and 5 min of reperfusion, with glucose as substrate.
During the last reflow, glucose was replaced with 5 mM acetate and 5 mM 2-deoxyglucose (2DG),
and hexose transport was measured from the rate of production of
2-deoxyglucose 6-phosphate (2DG6P), using 31P nuclear
magnetic resonance. Preconditioning stimulated 2DG uptake; after 15 min
of perfusion with 2DG, 2DG6P levels were 165% of initial ATP in
preconditioned hearts compared with 96% in control hearts
(p < 0.05). Wortmannin, an inhibitor of PI3K, did not
block the preconditioning induced stimulation of 2DG6P production, but perfusion with SB202190, an inhibitor of p38 MAP kinase, did attenuate 2DG6P accumulation (111% of initial ATP, p < 0.05 compared with preconditioned hearts). SB202190 had no effect on 2DG6P
accumulation in nonpreconditioned hearts. Preconditioning stimulation
of translocation of GLUT4 to the plasma membrane was not inhibited by
wortmannin. The data demonstrate that ischemic preconditioning
increases hexose transport and that this is mediated by p38 MAP kinase
and is PI3K-independent.
Preconditioning Enhanced Glucose Uptake Is Mediated by p38 MAP
Kinase Not by Phosphatidylinositol 3-Kinase*
,,
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Contributed equally to this work.
§
To whom correspondence should be addressed: Box 3712, Duke
University Medical Center, Durham, NC 27710. Fax: 919-681-7634; E-mail:
steen001@mc.duke.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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