The intracellular fatty acid-binding proteins (FABPs) comprise a family of
14-15 kDa proteins which bind long-chain fatty acids. A role for FABPs in f
atty acid transport has been hypothesized for several decades, and the accu
mulated indirect and correlative evidence is largely supportive of this pro
posed function. In recent years, a number of experimental approaches which
more directly examine the transport function of FABPs have been taken. Thes
e include molecular level in vitro modeling of fatty acid transfer mechanis
ms, whole cell studies of fatty acid uptake and intracellular transfer foll
owing genetic manipulation of FABP type and amount, and an examination of c
ells and tissues from animals engineered to lack expression of specific FAB
Ps. Collectively, data from these studies have provided strong support for
defining the FABPs as fatty acid transport proteins. Further studies are ne
cessary to elucidate the fundamental mechanisms by which cellular fatty aci
d trafficking is modulated by the FABPs. (C) 2000 Elsevier Science B.V. All
rights reserved.