Fiber type- and fatty acid composition-dependent effects of high-fat diets on rat muscle triacylglyceride and fatty acid transporter protein-1 content

Marotta, Mario; Ferrer-Martı́nez, Andreu; Parnau, Josep; Turini, Marco; Macé, Katherine; Foix, Anna

doi:10.1016/j.metabol.2004.03.011

Cited by 27 publications

(21 citation statements)

References 28 publications

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“…We also found that FAT/CD36 demonstrated differences between breeds and anatomical locations. Its mRNA expression level was higher in the m. biceps femoris than in the m. ipsilateral pectoralis, which was in accordance with recent reports (Marotta et al, 2004;Feng et al, 2007). Interestingly, FAT/CD36 was found to positively correlate with the LA content but negatively correlate with PA content, which is significant for its effect on meat quality.…”

Section: Discussionsupporting

confidence: 92%

Selective transport of long-chain fatty acids by FAT/CD36 in skeletal muscle of broilers

Guo

Shu

Zhou

et al. 2013

Animal

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Fatty acid translocase (FAT/CD36) is a membrane receptor that facilitates long-chain fatty acid uptake. To investigate its role in the regulation of long-chain fatty acid composition in muscle tissue, we studied and compared FAT/CD36 gene expression in muscle tissues of commercial broiler chickens and Chinese local Silky fowls. The results from gas chromatography-mass spectrometry analysis of muscle samples demonstrated that Chinese local Silky fowls had significantly higher (P , 0.05) proportions of linoleic acid (LA) and palmitic acid, lower proportions (P , 0.05) of arachidonic acid (AA) and oleic acid than the commercial broiler chickens. The mRNA expression levels of fatty acid (FA) transporters (FA transport protein-1, membrane FA-binding protein, FAT/CD36 and caveolin-1) in the m. ipsilateral pectoralis and biceps femoris were analyzed by Q-PCR, and FAT/CD36 expression levels showed significant differences between these types of chickens (P , 0.01). Interestingly, the levels of FAT/CD36 expression are positively correlated with LA content (r 5 0.567, P , 0.01) but negatively correlated with palmitic acid content (r 5 20.568, P , 0.01). Further experiments in the stably transfected Chinese hamster oocytes cells with chicken FAT/CD36 cDNA demonstrated that overexpression of FAT/CD36 improves total FA uptake with a significant increase in the proportion of LA and AA, and a decreased proportion of palmitic acid. These results suggest that chicken FAT/CD36 may selectively transport LA and AA, which may lead to the higher LA deposition in muscle tissue.

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Section: Discussionsupporting

confidence: 92%

Selective transport of long-chain fatty acids by FAT/CD36 in skeletal muscle of broilers

Guo

Shu

Zhou

et al. 2013

Animal

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“…The enhanced systemic fatty acid disposal in FATP1-mice is concordant with the proven capacity of overexpressed FATP1 to mediate fatty acid uptake, as shown in cultured skm cells [11] and tissue [16]. Here, intramuscular triglyceride levels were reduced by FATP1 overexpression irrespective of diet, and there were no diet-associated changes, as already observed in rat muscle [44]. Our data diverge from that in muscle-specific FATP1-overexpressing transgenic mice [16], which show unaltered non-fasting serum triglyceride and NEFA levels compared to wild-type mice, before or after a high-fat diet, and unaltered intramuscular triglyceride content on a high-fat diet.…”

Section: Discussionsupporting

confidence: 85%

Fatty Acid Transport Protein 1 (FATP1) Localizes in Mitochondria in Mouse Skeletal Muscle and Regulates Lipid and Ketone Body Disposal

et al. 2014

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FATP1 mediates skeletal muscle cell fatty acid import, yet its intracellular localization and metabolic control role are not completely defined. Here, we examine FATP1 localization and metabolic effects of its overexpression in mouse skeletal muscle. The FATP1 protein was detected in mitochondrial and plasma membrane fractions, obtained by differential centrifugation, of mouse gastrocnemius muscle. FATP1 was most abundant in purified mitochondria, and in the outer membrane and soluble intermembrane, but not in the inner membrane plus matrix, enriched subfractions of purified mitochondria. Immunogold electron microscopy localized FATP1-GFP in mitochondria of transfected C2C12 myotubes. FATP1 was overexpressed in gastrocnemius mouse muscle, by adenovirus-mediated delivery of the gene into hindlimb muscles of newborn mice, fed after weaning a chow or high-fat diet. Compared to GFP delivery, FATP1 did not alter body weight, serum fed glucose, insulin and triglyceride levels, and whole-body glucose tolerance, in either diet. However, fatty acid levels were lower and β-hydroxybutyrate levels were higher in FATP1- than GFP-mice, irrespective of diet. Moreover, intramuscular triglyceride content was lower in FATP1- versus GFP-mice regardless of diet, and β-hydroxybutyrate content was unchanged in high-fat-fed mice. Electroporation-mediated FATP1 overexpression enhanced palmitate oxidation to CO2, but not to acid-soluble intermediate metabolites, while CO2 production from β-hydroxybutyrate was inhibited and that from glucose unchanged, in isolated mouse gastrocnemius strips. In summary, FATP1 was localized in mitochondria, in the outer membrane and intermembrane parts, of mouse skeletal muscle, what may be crucial for its metabolic effects. Overexpressed FATP1 enhanced disposal of both systemic fatty acids and intramuscular triglycerides. Consistently, it did not contribute to the high-fat diet-induced metabolic dysregulation. However, FATP1 lead to hyperketonemia, likely secondary to the sparing of ketone body oxidation by the enhanced oxidation of fatty acids.

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“…This indicates that in oxidative muscle, which uses primary fatty acids as an energy source, the interaction between FATP1 and CPT1 could be higher than in glycolytic muscles. Furthermore, FATP1 expression in rat oxidative muscle (soleus) is approximately twice that in glycolytic (gastrocnemius) muscle (37). Our immunoprecipitation assays in L6E9 myotubes and rat skeletal muscle show that FATP1 and CPT1 interact in basal conditions, suggesting that FATP1 could be constitutively present in mitochondria.…”

Section: Discussionmentioning

confidence: 99%

Novel role of FATP1 in mitochondrial fatty acid oxidation in skeletal muscle cells

Sebastián

Guitart

Garcı́a-Martı́nez

et al. 2009

Journal of Lipid Research

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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 β-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.

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Fiber type- and fatty acid composition-dependent effects of high-fat diets on rat muscle triacylglyceride and fatty acid transporter protein-1 content

Cited by 27 publications

References 28 publications

Selective transport of long-chain fatty acids by FAT/CD36 in skeletal muscle of broilers

Selective transport of long-chain fatty acids by FAT/CD36 in skeletal muscle of broilers

Fatty Acid Transport Protein 1 (FATP1) Localizes in Mitochondria in Mouse Skeletal Muscle and Regulates Lipid and Ketone Body Disposal

Novel role of FATP1 in mitochondrial fatty acid oxidation in skeletal muscle cells

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