Tags

Type your tag names separated by a space and hit enter

A novel function for fatty acid translocase (FAT)/CD36: involvement in long chain fatty acid transfer into the mitochondria.
J Biol Chem. 2004 Aug 27; 279(35):36235-41.JB

Abstract

Fatty acid translocase (FAT)/CD36 is a long chain fatty acid transporter present at the plasma membrane, as well as in intracellular pools of skeletal muscle. In this study, we assessed the unexpected presence of FAT/CD36 in both subsarcolemmal and intermyofibril fractions of highly purified mitochondria. Functional assessments demonstrated that the mitochondria could bind (14)C-labeled palmitate, but could only oxidize it in the presence of carnitine. However, the addition of sulfo-N-succinimidyl oleate, a known inhibitor of FAT/CD36, resulted in an 87 and 85% reduction of palmitate oxidation in subsarcolemmal and intermyofibril fractions, respectively. Further studies revealed that maximal carnitine palmitoyltransferase I (CPTI) activity in vitro was inhibited by succinimidyl oleate (42 and 48% reduction). Interestingly, CPTI immunoprecipitated with FAT/CD36, indicating a physical pairing. Tissue differences in mitochondrial FAT/CD36 protein follow the same pattern as the capacity for fatty acid oxidation (heart >> red muscle > white muscle). Additionally, chronic stimulation of hindlimb muscles (7 days) increased FAT/CD36 expression and also resulted in a concomitant increase in mitochondrial FAT/CD36 content (46 and 47% increase). Interestingly, with acute electrical stimulation of hindlimb muscles (30 min), FAT/CD36 expression was not altered, but there was an increase in the mitochondrial content of FAT/CD36 compared with the non-stimulated control limb (35 and 37% increase). Together, these data suggest a role for FAT/CD36 in mitochondrial long chain fatty acid uptake and demonstrate system flexibility to match FAT/CD36 mitochondrial content with an increased capacity for fatty acid oxidation, possibly involving translocation of FAT/CD36 to the mitochondria.

Authors+Show Affiliations

Department of Human Biology and Nutritional Sciences, University of Guelph, Guelph, Ontario N1G 2W1, Canada.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15161924

Citation

Campbell, Shannon E., et al. "A Novel Function for Fatty Acid Translocase (FAT)/CD36: Involvement in Long Chain Fatty Acid Transfer Into the Mitochondria." The Journal of Biological Chemistry, vol. 279, no. 35, 2004, pp. 36235-41.
Campbell SE, Tandon NN, Woldegiorgis G, et al. A novel function for fatty acid translocase (FAT)/CD36: involvement in long chain fatty acid transfer into the mitochondria. J Biol Chem. 2004;279(35):36235-41.
Campbell, S. E., Tandon, N. N., Woldegiorgis, G., Luiken, J. J., Glatz, J. F., & Bonen, A. (2004). A novel function for fatty acid translocase (FAT)/CD36: involvement in long chain fatty acid transfer into the mitochondria. The Journal of Biological Chemistry, 279(35), 36235-41.
Campbell SE, et al. A Novel Function for Fatty Acid Translocase (FAT)/CD36: Involvement in Long Chain Fatty Acid Transfer Into the Mitochondria. J Biol Chem. 2004 Aug 27;279(35):36235-41. PubMed PMID: 15161924.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A novel function for fatty acid translocase (FAT)/CD36: involvement in long chain fatty acid transfer into the mitochondria. AU - Campbell,Shannon E, AU - Tandon,Narendra N, AU - Woldegiorgis,Gebretateos, AU - Luiken,Joost J F P, AU - Glatz,Jan F C, AU - Bonen,Arend, Y1 - 2004/05/25/ PY - 2004/5/27/pubmed PY - 2004/10/7/medline PY - 2004/5/27/entrez SP - 36235 EP - 41 JF - The Journal of biological chemistry JO - J. Biol. Chem. VL - 279 IS - 35 N2 - Fatty acid translocase (FAT)/CD36 is a long chain fatty acid transporter present at the plasma membrane, as well as in intracellular pools of skeletal muscle. In this study, we assessed the unexpected presence of FAT/CD36 in both subsarcolemmal and intermyofibril fractions of highly purified mitochondria. Functional assessments demonstrated that the mitochondria could bind (14)C-labeled palmitate, but could only oxidize it in the presence of carnitine. However, the addition of sulfo-N-succinimidyl oleate, a known inhibitor of FAT/CD36, resulted in an 87 and 85% reduction of palmitate oxidation in subsarcolemmal and intermyofibril fractions, respectively. Further studies revealed that maximal carnitine palmitoyltransferase I (CPTI) activity in vitro was inhibited by succinimidyl oleate (42 and 48% reduction). Interestingly, CPTI immunoprecipitated with FAT/CD36, indicating a physical pairing. Tissue differences in mitochondrial FAT/CD36 protein follow the same pattern as the capacity for fatty acid oxidation (heart >> red muscle > white muscle). Additionally, chronic stimulation of hindlimb muscles (7 days) increased FAT/CD36 expression and also resulted in a concomitant increase in mitochondrial FAT/CD36 content (46 and 47% increase). Interestingly, with acute electrical stimulation of hindlimb muscles (30 min), FAT/CD36 expression was not altered, but there was an increase in the mitochondrial content of FAT/CD36 compared with the non-stimulated control limb (35 and 37% increase). Together, these data suggest a role for FAT/CD36 in mitochondrial long chain fatty acid uptake and demonstrate system flexibility to match FAT/CD36 mitochondrial content with an increased capacity for fatty acid oxidation, possibly involving translocation of FAT/CD36 to the mitochondria. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/15161924/A_novel_function_for_fatty_acid_translocase__FAT_/CD36:_involvement_in_long_chain_fatty_acid_transfer_into_the_mitochondria_ L2 - http://www.jbc.org/cgi/pmidlookup?view=long&pmid=15161924 DB - PRIME DP - Unbound Medicine ER -