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J Biol Chem, Vol. 273, Issue 26, 15920-15926, June 26, 1998
From the The newly cloned proton-linked monocarboxylate
transporter MCT3 was shown by Western blotting and immunofluorescence
confocal microscopy to be expressed in all muscle fibers. In contrast, MCT1 is expressed most abundantly in oxidative fibers but is almost totally absent in fast-twitch glycolytic fibers. Thus MCT3 appears to
be the major MCT isoform responsible for efflux of glycolytically derived lactic acid from white skeletal muscle. MCT3 is also expressed in several other tissues requiring rapid lactic acid efflux. The expression of both MCT3 and MCT1 was decreased by 40-60% 3 weeks after denervation of rat hind limb muscles, whereas chronic stimulation of the muscles for 7 days increased expression of MCT1 2-3-fold but
had no effect on MCT3 expression. The kinetics and substrate and
inhibitor specificities of monocarboxylate transport into cell lines
expressing only MCT3 or MCT1 have been determined. Differences in the
properties of MCT1 and MCT3 are relatively modest, suggesting that the
significance of the two isoforms may be related to their regulation
rather than their intrinsic properties.
Lactic Acid Efflux from White Skeletal Muscle Is Catalyzed by the
Monocarboxylate Transporter Isoform MCT3
,,,,
,,,, and
Department of Biochemistry, School of
Medical Sciences, University of Bristol, Bristol BS8 1TD, United
Kingdom, the Copenhagen Muscle Research Centre, August Krogh
Institute, University of Copenhagen DK2100, Copenhagen, Denmark, the
** Department of Kinesiology, University of Waterloo, Waterloo, Ontario
N2L 3G1, Canada, and the Department of
Physiology, University of Glasgow, Glasgow G12 8QQ, Scotland
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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