Dr. Prows et al., INTESTINAL FATTY-ACID-BINDING PROTEIN EXPRESSION STIMULATES FIBROBLAST FATTY-ACID ESTERIFICATION, Chemistry and physics of lipids, 84(1), 1996, pp. 47-56
The effect of intestinal fatty acid binding protein (I-FABP) expressio
n on cell growth and cell lipid content is not known. Therefore, mouse
L-cell fibroblasts were transfected with the cDNA encoding for I-FABP
. The high expression clones expressed 0.35% of the total cytosolic pr
oteins as I-FABP. Mock transfected L-cells did not differ from control
L-cells in any properties tested. Neither the growth rate, maximal ce
ll density, nor [H-3]oleic acid uptake differed in I-FABP expressing a
s compared to control cells. In contrast, I-FABP expression increased
triacylglycerol and cholesteryl ester mass (nmol/mg protein) by 63% an
d 25%, respectively. Phospholipid mass was unchanged in I-FABP express
ing cells. The initial [3H]oleic acid esterification into triacylglyce
rols and cholesteryl esters was increased 3.9- and 2.5-fold in I-FABP
expressing cells. Although, the initial [H-3]oleic acid esterification
into total phospholipids was unchanged, within the phospholipid fract
ion the initial [H-3]oleic acid esterification into phosphatidylethano
lamine was increased 70% and decreased 50% in phosphatidylcholine in I
-FABP expressing cells. These observed differences suggest a distinct
role for I-FABP in stimulating net formation, and not just turnover, o
f triacylglycerides and cholesteryl esters in transfected L-cell fibro
blasts.