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Intestinal and liver fatty acid binding proteins differentially affect fatty acid uptake and esterification in L‐cells
Author(s) -
Prows Daniel R.,
Murphy Eric J.,
Schroeder Friedhelm
Publication year - 1995
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02537481
Subject(s) - glycerophospholipids , fatty acid binding protein , oleic acid , biochemistry , fatty acid , intracellular , clinical chemistry , chemistry , free fatty acid receptor , acyl coa , biology , polyunsaturated fatty acid , enzyme , phospholipid , gene , membrane
Differential effects of intestinal (I‐FABP) or liver (L‐FABP) fatty acid binding proteins on fatty acid uptake and esterification were examined using transfected mouse L‐cell fibroblasts. L‐FABP, but not I‐FABP, expression increased the initial rate and extent of cis ‐parinaric acid uptake by 50 and 29%, respectively, compared to control cells. I‐FABP and L‐FABP expression preferentially increased [ 3 H]‐oleic acid incorporation into triacylglycerols by 5.5‐fold and 3.8‐fold, respectively. While both L‐FABP and I‐FABP increasedesterification of [ 3 H]‐oleic acid into ethanolamine glycerophospholipids, these proteins had opposite effect on esterification into choline glycerophospholipids. These data show for the first time that distinct FABP differentially affect both fatty acid uptake and intracellular esterification.