Intestinal fatty acid-binding protein expression stimulates
fibroblasts fatty acid esterification.
Prows, Daniel R., Eric J. Murphy, Dino Moncecchi, and Friedhelm
Schroeder.
Division of Pharmacology and Medicinal Chemistry, University of
Cincinnati, College of Pharmacy, Cincinnati, OH 45267-0004 and
Department of Physiology and Pharmacology, Texas A & M University,
TVMC, College Station, TX 77843-4466
APStracts 3:0015G, 1996.
Mouse L-cell fibroblasts were transfected with the cDNA encoding for
rat intestinal fatty acid-binding protein (I-FABP). I-FABP levels in
stable transfectants were 0.35% of the total cytosolic proteins. Mock
transfected L-cell clones were also isolated and did not differ from
control L-cells in any properties tested. I-FABP expressing cells
preferentially esterified exogenous [3H]-oleic acid into the neutral
lipid fraction with a 2.0-fold increase in the esterification rate
compared to control cells after 30 min of incubation. The [3H]-oleic
acid was primarily esterified into the triacylglycerol and
cholesteryl ester fractions. Both triacylglycerol and cholesteryl
ester levels were significantly increased by 60% and 20%,
respectively, in I-FABP expressing cells. [3H]-oleic acid
esterification into total phospholipids was decreased by 28% in I
-FABP expressing cells. Phospholipid levels were not significantly
different between L-cells and I-FABP expressing cells, indicating I
-FABP did not alter phospholipid homeostasis. These observed
differences suggest a distinct role for I-FABP in intracellular lipid
trafficking and metabolism.
Received 11 September 1995; accepted in final form 27 December
1995.
APS Manuscript Number G401-5.
Article publication pending Am. J. Physiol. (Gastrointest. Liver
Physiology).
ISSN 1080-4757 Copyright 1996 The American Physiological Society.
Published in APStracts on 22 January 96