Lipids

, Volume 34, Supplement 1, pp S169–S175

Cellular fatty acid transport in heart and skeletal muscle as facilitated by proteins

Authors

  • J. J. F. P. Luiken
    • Department of KinesiologyUniversity of Waterloo
    • Department of Physiology, Cardiovascular Research Institute Maastricht (CARIM)Maastricht University
  • F. G. Schaap
    • Department of Physiology, Cardiovascular Research Institute Maastricht (CARIM)Maastricht University
  • F. A. van Nieuwenhoven
    • Department of Physiology, Cardiovascular Research Institute Maastricht (CARIM)Maastricht University
  • G. J. van der Vusse
    • Department of Physiology, Cardiovascular Research Institute Maastricht (CARIM)Maastricht University
  • A. Bonen
    • Department of KinesiologyUniversity of Waterloo
    • Department of Physiology, Cardiovascular Research Institute Maastricht (CARIM)Maastricht University
Lipid Traffideing

DOI: 10.1007/BF02562278

Cite this article as:
Luiken, J.J.F.P., Schaap, F.G., van Nieuwenhoven, F.A. et al. Lipids (1999) 34: S169. doi:10.1007/BF02562278

Abstract

Despite the importance of long-chain fatty acids (FA) as fuels for heart and skeletal muscles, the mechanism of their cellular uptake has not yet been clarified. There is dispute as to whether FA are taken up by the muscle cellsvia passive diffusion and/or carrier-mediated transport. Kinetic studies of FA uptake by cardiac myocytes and the use of membrane protein-modifying agents have suggested the bulk of FA uptake is due to a protein component. Three membrane-associated FA-binding proteins were proposed to play a role in FA uptake, a 40-kDa plasma membrane FA-binding protein (FABPpm), an 88-kDa FA translocase (FAT/CD36), and a 60-kDa FA transport protein (FATP). In cardiac and skeletal myocytes the intracellular carrier for FA is cytoplasmic heart-type FA-binding protein (H-FABP), which likely transports FA from the sarcolemma to their intracellular sites of metabolism. A scenario is discussed in which FABPpm, FAT/CD36, and H-FABP, probably assisted by an albumin-binding protein, cooperate in the translocation of FA across the sarcolemma.

Abbreviations

E-FABP

epidermal-type fatty acid-binding protein

FA

long-chain fatty acids

FABP

fatty acid-binding protein

FABPpm

plasmalemmal fatty acid-binding protein

FAT

fatty acid translocase (CD36)

FATP

fatty acid-transport protein

H-FABP

heart-type fatty acid-binding protein

mAAT

mitochondrial aspartate aminotransferase

SSO

sulfo-N-succinimidyloleate

Copyright information

© AOCS Press 1999