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Papers In Press, published online ahead of print September 16, 2002
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Submitted on June 12, 2002
Biochemistry, Mol. Biol. and Biophysics, University of Minnesota, Minneapolis, MN 55455
Corresponding Author: bernl001{at}umn.edu
Fatty acid-binding proteins (FABP) are low molecular mass, soluble, intracellular lipid chaperones. Previous studies on adipocytes from adipocyte-fatty acid binding protein deficient mice have revealed that basal and isoproterenol-stimulated lipolysis were markedly reduced. [Ribarik-Coe, N.et al., (1999) J. Lipid Res. 40; 967-972]. Herein we report the construction of transgenic mice overexpressing the FABP5 gene encoding the epithelial FABP (E-FABP) in adipocytes thereby allowing evaluation of increased FABP levels and isoform specificity on changes in lipolysis. In adipocytes from transgenic mice, the total FABP protein level in the adipocyte was increased to 150% as compared to the wild type due to a 10-fold increase in the level of E-FABP and an unanticipated 2-fold down regulation of the adipocyte FABP (A-FABP). There were no significant differences in body weight, serum FFA or fat pad mass between wild type and transgenic mice. Importantly, both basal and hormone-stimulated lipolysis increased in adipocytes from the FABP5 transgenic animals. The molecular composition of the fatty acid pool from either the intracellular compartment or that effluxed from the adipocyte was unaltered. These results demonstrate that lipolysis is directly proportional to the total level of FABP and not to a specific FABP isoform.
Revised on September 9, 2002
Accepted on September 10, 2002
Increased lipolysis in transgenic animals overexpressing the Epithelial fatty acid binding protein in adipose cells
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