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Physiol. Genomics 17: 31-37, 2004. First published December 23, 2003; doi:10.1152/physiolgenomics.00190.2003
1094-8341/04 $5.00
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Received 12 November 2003; accepted in final form 19 December 2003.
Physiological Genomics 17:31-37 (2004)
1094-8341/04 $5.00 © 2004 American Physiological Society

Overexpression of membrane-associated fatty acid binding protein (FABPpm) in vivo increases fatty acid sarcolemmal transport and metabolism

David C. Clarke1, Dragana Miskovic2, Xiao-Xia Han1, Jorge Calles-Escandon3, Jan F. C. Glatz4, Joost J. F. P. Luiken4, John J. Heikkila2 and Arend Bonen5

1 Departments of Kinesiology
2 Biology, University of Waterloo, Waterloo, Ontario N2L 3G1, Canada
3 Section of Endocrinology and Metabolism, Wake Forest University School of Medicine and Baptist Medical Center, Winston-Salem, North Carolina 27157
4 Department of Molecular Genetics, Maastricht University, 6200-MD Maastricht, The Netherlands
5 Department of Human Biology and Nutritional Sciences, University of Guelph, Guelph, Ontario N1G 2W1, Canada

Fatty acid translocase (FAT/CD36) is a key fatty acid transporter in skeletal muscle. However, the effects on fatty acid transport by another putative fatty acid transporter, plasma membrane-associated fatty acid binding protein (FABPpm), have not been determined in mammalian tissue. We examined the functional effects of overexpressing FABPpm on the rates of 1) palmitate transport across the sarcolemma and 2) palmitate metabolism in skeletal muscle. One muscle (soleus) was transfected with pTracer containing FABPpm cDNA. The contralateral muscle served as control. After injecting the FABPpm cDNA, muscles were electroporated. FABPpm overexpression was directly related to the quantity of DNA administered. Electrotransfection (200 µg/muscle) rapidly induced FABPpm protein overexpression (day 1, +92%, P < 0.05), which was further increased during the next few days (days 3–7; range +142% to +160%, P < 0.05). Sarcolemmal FABPpm was comparably increased (day 7, +173%, P < 0.05). Neither FAT/CD36 expression nor sarcolemmal FAT/CD36 content was altered. FABPpm overexpression increased the rates of palmitate transport (+79%, P < 0.05). Rates of palmitate incorporation into phospholipids were also increased +36%, as were the rates of palmitate oxidation (+20%). Rates of palmitate incorporation into triacylglycerol depots were not altered. These studies demonstrate that in mammalian tissue FABPpm overexpression increased the rates of palmitate transport across the sarcolemma, an effect that is independent of any changes in FAT/CD36. However, since the overexpression of plasmalemmal FABPpm (+173%) exceeded the effects on the rates of palmitate transport and metabolism, it appears that the overexpression of FABPpm alone is not sufficient to induce completely parallel increments in palmitate transport and metabolism. This suggests that other mechanisms are required to realize the full potential offered by FABPpm overexpression.

muscle; giant vesicles; FAT/CD36; palmitate esterification; palmitate oxidation




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