HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in ISI Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via ISI Web of Science (11) Citing Articles via Google Scholar Google Scholar Articles by García-Martínez, C. Articles by Gómez-Foix, A. M. Search for Related Content PubMed PubMed Citation Articles by García-Martínez, C. Articles by Gómez-Foix, A. M.

CELLULAR METABOLISM

Impact on fatty acid metabolism and differential localization of FATP1 and FAT/CD36 proteins delivered in cultured human muscle cells

Departament Bioquímica i Biologia Molecular, Universitat de Barcelona, Barcelona, Spain

Submitted 7 June 2004 ; accepted in final form 6 January 2005

We compared the intracellular distribution and regulatory role of fatty acid transporter protein (FATP1) and fatty acid translocase (FAT/CD36) on muscle cell fatty acid metabolism. With the use of adenoviruses, FATP1 and FAT genes were delivered to primary cultured human muscle cells. FATP1 and FAT moderately enhanced palmitate and oleate transport evenly at concentrations of 0.05, 0.5, and 1 mM. Long-term (16 h) consumption of palmitate and oleate from the media, and particularly incorporation into triacylglyceride (TAG), was stimulated equivalently by FATP1 and FAT at all fatty acid concentrations tested. In contrast, long-term CO₂ production was reduced by FATP1 and FAT at all doses of palmitate and at the lower concentrations of oleate. Neither FATP1 nor FAT markedly altered the production of acid-soluble metabolic intermediates from palmitate or oleate. The intracellular localization of fusion constructs of FATP1 and FAT with enhanced green fluorescent protein (EGFP) was examined. Independently of fatty acid treatment, FATPGFP was observed throughout the cytosol in a reticular pattern and concentrated in the perinuclear region, partly overlapping with the Golgi marker GM-130. FATGFP was found in the extracellular membrane and in cytosolic vesicles not coincident with GM-130. Neither FATP1 nor FAT proteins colocalized with lipid droplets in oleate-treated cells. We conclude that whereas FAT is localized on the extracellular membrane, FATP1 is active in the cytosol and imports fatty acids into myotubes. Overall, both FATP1 and FAT stimulated transport and consumption of palmitate and oleate, which they channeled away from complete oxidation and toward TAG synthesis.

palmitate; oleate; fatty acid binding proteins; skeletal muscle

This article has been cited by other articles:

				N. S. Eyre, L. G. Cleland, N. N. Tandon, and G. Mayrhofer Importance of the carboxyl terminus of FAT/CD36 for plasma membrane localization and function in long-chain fatty acid uptake J. Lipid Res., March 1, 2007; 48(3): 528 - 542. [Abstract] [Full Text] [PDF]

				K. Milger, T. Herrmann, C. Becker, D. Gotthardt, J. Zickwolf, R. Ehehalt, P. A. Watkins, W. Stremmel, and J. Fullekrug Cellular uptake of fatty acids driven by the ER-localized acyl-CoA synthetase FATP4 J. Cell Sci., November 15, 2006; 119(22): 4678 - 4688. [Abstract] [Full Text] [PDF]

				G. K. Bandyopadhyay, J. G. Yu, J. Ofrecio, and J. M. Olefsky Increased Malonyl-CoA Levels in Muscle From Obese and Type 2 Diabetic Subjects Lead to Decreased Fatty Acid Oxidation and Increased Lipogenesis; Thiazolidinedione Treatment Reverses These Defects. Diabetes, August 1, 2006; 55(8): 2277 - 2285. [Abstract] [Full Text] [PDF]

				S. Schenk and J. F. Horowitz Coimmunoprecipitation of FAT/CD36 and CPT I in skeletal muscle increases proportionally with fat oxidation after endurance exercise training Am J Physiol Endocrinol Metab, August 1, 2006; 291(2): E254 - E260. [Abstract] [Full Text] [PDF]