Abstract
The cellular transport of long-chain fatty acid moieties is thought to be mediated by a plasmalemmal and a cytoplasmic fatty acid binding protein (FABP PM and FABP C, respectively) and a cytoplasmic acyl-coenzyme A binding protein (ACBP). Their putative main physiological significance is the assurance that long-chain fatty acids and derivatives, either in transit through membranes or present in intracellular compartments, are largely complexed to proteins. FABP C distinguishes from the other proteins in that distinct types of FABP C exist and that these are found in a variety of tissues in remarkable abundance, with some cells containing more than one type In addition, liver type FABP C binds not only fatty acids, but also several other hydrophobic ligands, including heme, bilirubin, prostaglandin E 1 and lipoxygenase metabolites of arachidonic acid. Calculations made for rat cardiomyocytes reveal that the presence of FABP C substantially enhances the cytoplasmic solubility as well as the maximal diffusional flux of fatty acids in these cells. Apart from this putative function in the bulk transport of ligands, FABP C may also function in the fine-tuning of cellular events by modulating the metabolism of hydrophobic compounds implicated in the regulation of cell growth and differentiation.
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