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Identification of fatty acid translocase on human skeletal muscle mitochondrial membranes: essential role in fatty acid oxidation.
Am J Physiol Endocrinol Metab. 2006 Mar; 290(3):E509-15.AJ

Abstract

Fatty acid translocase (FAT/CD36) is a transport protein with a high affinity for long-chain fatty acids (LCFA). It was recently identified on rat skeletal muscle mitochondrial membranes and found to be required for palmitate uptake and oxidation. Our aim was to identify the presence and elucidate the role of FAT/CD36 on human skeletal muscle mitochondrial membranes. We demonstrate that FAT/CD36 is present in highly purified human skeletal mitochondria. Blocking of human muscle mitochondrial FAT/CD36 with the specific inhibitor sulfo-N-succimidyl-oleate (SSO) decreased palmitate oxidation in a dose-dependent manner. At maximal SSO concentrations (200 muM) palmitate oxidation was decreased by 95% (P<0.01), suggesting an important role for FAT/CD36 in LCFA transport across the mitochondrial membranes. SSO treatment of mitochondria did not affect mitochondrial octanoate oxidation and had no effect on maximal and submaximal carnitine palmitoyltransferase I (CPT I) activity. However, SSO treatment did inhibit palmitoylcarnitine oxidation by 92% (P<0.001), suggesting that FAT/CD36 may be playing a role downstream of CPT I activity, possibly in the transfer of palmitoylcarnitine from CPT I to carnitine-acylcarnitine translocase. These data provide new insight regarding human skeletal muscle mitochondrial fatty acid (FA) transport, and suggest that FAT/CD36 could be involved in the cellular and mitochondrial adaptations resulting in improved and/or impaired states of FA oxidation.

Authors+Show Affiliations

Department of Human Biology and Nutritional Sciences, University of Guelph, Guelph, ON, Canada. vbezaire@uoguelph.caNo affiliation info availableNo affiliation info availableNo 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

16219667

Citation

Bezaire, Veronic, et al. "Identification of Fatty Acid Translocase On Human Skeletal Muscle Mitochondrial Membranes: Essential Role in Fatty Acid Oxidation." American Journal of Physiology. Endocrinology and Metabolism, vol. 290, no. 3, 2006, pp. E509-15.
Bezaire V, Bruce CR, Heigenhauser GJ, et al. Identification of fatty acid translocase on human skeletal muscle mitochondrial membranes: essential role in fatty acid oxidation. Am J Physiol Endocrinol Metab. 2006;290(3):E509-15.
Bezaire, V., Bruce, C. R., Heigenhauser, G. J., Tandon, N. N., Glatz, J. F., Luiken, J. J., Bonen, A., & Spriet, L. L. (2006). Identification of fatty acid translocase on human skeletal muscle mitochondrial membranes: essential role in fatty acid oxidation. American Journal of Physiology. Endocrinology and Metabolism, 290(3), E509-15.
Bezaire V, et al. Identification of Fatty Acid Translocase On Human Skeletal Muscle Mitochondrial Membranes: Essential Role in Fatty Acid Oxidation. Am J Physiol Endocrinol Metab. 2006;290(3):E509-15. PubMed PMID: 16219667.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Identification of fatty acid translocase on human skeletal muscle mitochondrial membranes: essential role in fatty acid oxidation. AU - Bezaire,Veronic, AU - Bruce,Clinton R, AU - Heigenhauser,George J F, AU - Tandon,Narendra N, AU - Glatz,Jan F C, AU - Luiken,Joost J J F, AU - Bonen,Arend, AU - Spriet,Lawrence L, Y1 - 2005/10/11/ PY - 2005/10/13/pubmed PY - 2006/3/24/medline PY - 2005/10/13/entrez SP - E509 EP - 15 JF - American journal of physiology. Endocrinology and metabolism JO - Am. J. Physiol. Endocrinol. Metab. VL - 290 IS - 3 N2 - Fatty acid translocase (FAT/CD36) is a transport protein with a high affinity for long-chain fatty acids (LCFA). It was recently identified on rat skeletal muscle mitochondrial membranes and found to be required for palmitate uptake and oxidation. Our aim was to identify the presence and elucidate the role of FAT/CD36 on human skeletal muscle mitochondrial membranes. We demonstrate that FAT/CD36 is present in highly purified human skeletal mitochondria. Blocking of human muscle mitochondrial FAT/CD36 with the specific inhibitor sulfo-N-succimidyl-oleate (SSO) decreased palmitate oxidation in a dose-dependent manner. At maximal SSO concentrations (200 muM) palmitate oxidation was decreased by 95% (P<0.01), suggesting an important role for FAT/CD36 in LCFA transport across the mitochondrial membranes. SSO treatment of mitochondria did not affect mitochondrial octanoate oxidation and had no effect on maximal and submaximal carnitine palmitoyltransferase I (CPT I) activity. However, SSO treatment did inhibit palmitoylcarnitine oxidation by 92% (P<0.001), suggesting that FAT/CD36 may be playing a role downstream of CPT I activity, possibly in the transfer of palmitoylcarnitine from CPT I to carnitine-acylcarnitine translocase. These data provide new insight regarding human skeletal muscle mitochondrial fatty acid (FA) transport, and suggest that FAT/CD36 could be involved in the cellular and mitochondrial adaptations resulting in improved and/or impaired states of FA oxidation. SN - 0193-1849 UR - https://www.unboundmedicine.com/medline/citation/16219667/Identification_of_fatty_acid_translocase_on_human_skeletal_muscle_mitochondrial_membranes:_essential_role_in_fatty_acid_oxidation_ L2 - http://journals.physiology.org/doi/full/10.1152/ajpendo.00312.2005?url_ver=Z39.88-2003&amp;rfr_id=ori:rid:crossref.org&amp;rfr_dat=cr_pub=pubmed DB - PRIME DP - Unbound Medicine ER -