A Novel Function for Fatty Acid Translocase (FAT)/CD36

Campbell, Sue Ann; Tandon, Narendra N.; Woldegiorgis, Gebre; Luiken, Joost J. F. P.; Glatz, Jan F. C.; Bonen, Arend

doi:10.1074/jbc.m400566200

Cited by 226 publications

(68 citation statements)

References 38 publications

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“…First, many publications had reported the translocation of FAT/CD36 both to the plasma membrane for transport of FAs and to the mitochondria for increasing FA oxidation (Koonen et al, 2005;Bezaire et al, 2006). For example, exercise induces the translocation of FAT/CD36 to mitochondria, thus increasing muscle FA oxidation (Campbell et al, 2004). Furthermore, FAT/CD36 co-immunoprecipitated with carnitine palmitoyltransferase 1 (CPT1) in cells, and its overexpression increased mitochondrial FA oxidation efficiency, showing an additive effect when co-overexpressed with CPT1 (Campbell et al, 2004).…”

Section: Discussionmentioning

confidence: 99%

“…For example, exercise induces the translocation of FAT/CD36 to mitochondria, thus increasing muscle FA oxidation (Campbell et al, 2004). Furthermore, FAT/CD36 co-immunoprecipitated with carnitine palmitoyltransferase 1 (CPT1) in cells, and its overexpression increased mitochondrial FA oxidation efficiency, showing an additive effect when co-overexpressed with CPT1 (Campbell et al, 2004). Second, mitochondria show the highest oxidation rates with C12:0-C16:0 and with C18:2 (Alexson and Cannon, 1984).…”

Section: Discussionmentioning

confidence: 99%

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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: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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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“…Protein Isolation and Western Blotting-Muscles were homogenized and proteins separated using SDS-PAGE as we have described previously (24,25). Proteins from isolated mitochondria were similarly separated using SDS-PAGE.…”

Section: Comparison Of Pgc-1␣ With Oxidative Capacity and Selected Prmentioning

confidence: 99%

“…Proteins from isolated mitochondria were similarly separated using SDS-PAGE. Western blotting was performed as we have reported elsewhere (24,25). Signals were detected using enhanced chemiluminescence (PerkinElmer Life Sciences) and were subsequently quantified by densitometry by Gene Tool as per the manufacturer's instructions (SynGene, ChemiGenius2, PerkinElmer Life Sciences).…”

Section: Comparison Of Pgc-1␣ With Oxidative Capacity and Selected Prmentioning

confidence: 99%

“…For mitochondrial isolations, fresh RTA and WTA muscles were excised and placed in ice-cold Buffer 1 (100 mM KCl, 50 mM Tris-HCl, 5 mM MgSO 4 , 5 mM EDTA, pH 7.4). Thereafter, SS and IMF mitochondria were obtained as we have described previously (24,39). To analyze protein content in the mitochondria with Western blotting, the samples were purified further to remove possible sarcolemmal membrane debris, as we have done previously (24).…”

Section: Muscle Triacylglycerol Content Mitochondrial Isolation Andmentioning

confidence: 99%

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Modest PGC-1α Overexpression in Muscle in Vivo Is Sufficient to Increase Insulin Sensitivity and Palmitate Oxidation in Subsarcolemmal, Not Intermyofibrillar, Mitochondria

Benton

Nickerson

Lally

et al. 2008

Journal of Biological Chemistry

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198

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PGC-1␣ overexpression in skeletal muscle, in vivo, has yielded disappointing and unexpected effects, including disrupted cellular integrity and insulin resistance. These unanticipated results may stem from an excessive PGC-1␣ overexpression in transgenic animals. Therefore, we examined the effects of a modest PGC-1␣ overexpression in a single rat muscle, in vivo, on fuel-handling proteins and insulin sensitivity. We also examined whether modest PGC-1␣ overexpression selectively targeted subsarcolemmal (SS) mitochondrial proteins and fatty acid oxidation, because SS mitochondria are metabolically more plastic than intermyofibrillar (IMF) mitochondria. Among metabolically heterogeneous rat hindlimb muscles, PGC-1␣ was highly correlated with their oxidative fiber content and with substrate transport proteins (GLUT4, FABPpm, and FAT/ CD36) and mitochondrial proteins (COXIV and mTFA) but not with insulin-signaling proteins (phosphatidylinositol 3-kinase, IRS-1, and Akt2), nor with 5-AMP-activated protein kinase, ␣2 subunit, and HSL. Transfection of PGC-1␣ into the red (RTA) and white tibialis anterior (WTA) compartments of the tibialis anterior muscle increased PGC-1␣ protein by 23-25%. This also induced the up-regulation of transport proteins (FAT/CD36, 35-195%; GLUT4, 20 -32%) and 5-AMP-activated protein kinase, ␣2 subunit (37-48%), but not other proteins (FABPpm, IRS-1, phosphatidylinositol 3-kinase, Akt2, and HSL). SS and IMF mitochondrial proteins were also up-regulated, including COXIV (15-75%), FAT/CD36 (17-30%), and mTFA (15-85%). PGC-1␣ overexpression also increased palmitate oxidation in SS (RTA, ؉116%; WTA, ؉40%) but not in IMF mitochondria, and increased insulin-stimulated phosphorylation of AKT2 (28 -43%) and rates of glucose transport (RTA, ؉20%; WTA, ؉38%). Thus, in skeletal muscle in vivo, a modest PGC-1␣ overexpression up-regulated selected plasmalemmal and mitochondrial fuel-handling proteins, increased SS (not IMF) mitochondrial fatty acid oxidation, and improved insulin sensitivity.

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Molecular mechanisms of hypolipidemic effects of curcumin

2013

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Recent evidence suggests potential benefits from phytochemicals and micronutrients in reducing the elevated oxidative and lipid-mediated stress associated with inflammation, obesity, and atherosclerosis. These compounds may either directly scavenge reactive oxygen or nitrogen species or they may modulate the activity of signal transduction enzymes leading to changes in the expression of antioxidant genes. Alternatively, they may reduce plasma lipid levels by modulating lipid metabolic genes in tissues and thus reduce indirectly lipid-mediated oxidative and endoplasmic reticulum stress through their hypolipidemic effect. Here we review the proposed molecular mechanisms by which curcumin, a polyphenol present in the rhizomes of turmeric (Curcuma longa) spice, influences oxidative and lipid-mediated stress in the vascular system. At the molecular level, mounting experimental evidence suggests that curcumin may act chemically as scavenger of free radicals and/or influences signal transduction (e.g., Akt, AMPK) and modulates the activity of specific transcription factors (e.g., FOXO1/3a, NRF2, SREBP1/2, CREB, CREBH, PPARγ, and LXRα) that regulate the expression of genes involved in free radicals scavenging (e.g., catalase, MnSOD, and heme oxygenase-1) and lipid homeostasis (e.g., aP2/FABP4, CD36, HMG-CoA reductase, and carnitine palmitoyltransferase-I (CPT-1)). At the cellular level, curcumin may induce a mild oxidative and lipid-metabolic stress leading to an adaptive cellular stress response by hormetic stimulation of these cellular antioxidant defense systems and lipid metabolic enzymes. The resulting lower oxidative and lipid-mediated stress may not only explain the beneficial effects of curcumin on inflammation, cardiovascular, and neurodegenerative disease, but may also contribute to the increase in maximum life-span observed in animal models.

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A Novel Function for Fatty Acid Translocase (FAT)/CD36

Cited by 226 publications

References 38 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

Modest PGC-1α Overexpression in Muscle in Vivo Is Sufficient to Increase Insulin Sensitivity and Palmitate Oxidation in Subsarcolemmal, Not Intermyofibrillar, Mitochondria

Molecular mechanisms of hypolipidemic effects of curcumin

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