Novel role of FATP1 in mitochondrial fatty acid oxidation in skeletal muscle cells
| Autor: | Cèlia García-Martínez, Anna M. Gómez-Foix, Fausto G. Hegardt, Maria Guitart, Josep M. Orellana-Gavaldà, Guillermina Asins, Caroline Mauvezin, Dolors Serra, David Sebastián |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
CD36 Antigens
Male Muscle Fibers Skeletal Muscle cells Àcids grassos Antígens Biochemistry Mitocondris Mice chemistry.chemical_compound Endocrinology malonyl-CoA Cèl·lules musculars Beta oxidation chemistry.chemical_classification biology Fatty Acids FAT/CD36 food and beverages Fatty Acid Transport Proteins Metabolisme Mitochondria mitochondria Protein Transport Fatty acid synthase Free fatty acid receptor Oxidation-Reduction Research Article Oxidation-reduction reaction Ratolins (Animals de laboratori) carnitine palmitoyltransferase 1 Citologia QD415-436 Cell Line Reacció d'oxidació-reducció Coenzyme A Ligases Animals Humans Immunoprecipitation Antigens Fatty acids adipocyte protein 2 Muscle Skeletal Carnitine O-Palmitoyltransferase Fatty acid Cell Biology Lipid Metabolism Metabolisme dels lípids Rats Metabolism Lipid metabolism Mice (Laboratory animals) Malonyl-CoA Gene Expression Regulation chemistry biology.protein Cytology Etomoxir |
| Zdroj: | Dipòsit Digital de la UB Universidad de Barcelona Journal of Lipid Research, Vol 50, Iss 9, Pp 1789-1799 (2009) Journal of Lipid Research |
| ISSN: | 0022-2275 |
| DOI: | 10.1194/jlr.m800535-jlr200 |
| Popis: | Carnitine palmitoyltransferase 1 (CPT1) catalyzes the first step in long-chain fatty acid import into mitochondria, and it is believed to be rate limiting for beta-oxidation of fatty acids. However, in muscle, other proteins may collaborate with CPT1. Fatty acid translocase/CD36 (FAT/CD36) may interact with CPT1 and contribute to fatty acid import into mitochondria in muscle. Here, we demonstrate that another membrane-bound fatty acid binding protein, fatty acid transport protein 1 (FATP1), collaborates with CPT1 for fatty acid import into mitochondria. Overexpression of FATP1 using adenovirus in L6E9 myotubes increased both fatty acid oxidation and palmitate esterification into triacylglycerides. Moreover, immunocytochemistry assays in transfected L6E9 myotubes showed that FATP1 was present in mitochondria and coimmunoprecipitated with CPT1 in L6E9 myotubes and rat skeletal muscle in vivo. The cooverexpression of FATP1 and CPT1 also enhanced mitochondrial fatty acid oxidation, similar to the cooverexpression of FAT/CD36 and CPT1. However, etomoxir, an irreversible inhibitor of CPT1, blocked all these effects. These data reveal that FATP1, like FAT/CD36, is associated with mitochondria and has a role in mitochondrial oxidation of fatty acids. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|