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(Received for publication, February 6, 1996, and in revised form, March 15, 1996)
From the Department of Nutritional Sciences, Cook College, Rutgers
University, New Brunswick, New Jersey 08903
Intestinal absorptive cells contain high levels
of expression of two homologous fatty acid-binding proteins (FABP),
liver FABP (L-FABP), and intestinal FABP (I-FABP). Both bind long chain
fatty acids with relatively high affinity. The functional distinction,
if any, between these two proteins remains unknown. It is often
hypothesized that FABP are important in intracellular transport of
fatty acids. To assess whether fatty acid transport properties might
differ between the two enterocyte FABPs, we examined the rate and
mechanism of transfer of fluorescent anthroyloxy fatty acids (AOFA)
from these proteins to model membranes using a resonance energy
transfer assay. The results show that the absolute rate of AOFA
transfer from I-FABP is faster than from L-FABP. Moreover, the apparent
mechanism of fatty acid transfer is different between the two proteins.
The rate of AOFA transfer from I-FABP is independent of ionic strength,
directly dependent on the concentration of acceptor membrane vesicles,
and dramatically regulated by the lipid composition of the membranes.
These data strongly suggest that fatty acid transfer from I-FABP to
membranes occurs by direct collisional interaction of the protein with
the phospholipid bilayer. In contrast, the characteristics of fatty
acid transfer from L-FABP are consistent with an aqueous
diffusion-mediated process. Thus the two enterocyte FABPs may perform
different functions within the intestinal absorptive cell in the
regulation of fatty acid transport and utilization. It is hypothesized
that L-FABP may act as a cytosolic buffer for fatty acids, maintaining
the unbound fatty acid concentration, whereas I-FABP may be involved in
the uptake and/or specific targeting of fatty acid to subcellular
membrane sites.
Volume 271, Number 23,
Issue of June 7, 1996
pp. 13317-13323
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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