Cellular fatty acid transport in heart and skeletal muscle as facilitated by proteins

Luiken, Joost J. F. P.; Schaap, Frank G.; Nieuwenhoven, Frans A. van; Vusse, Ger J.; Bonen, Arend; Glatz, Jan F. C.

doi:10.1007/bf02562278

Cited by 110 publications

(79 citation statements)

References 47 publications

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“…Approximately a third of the improved delivery of fatty acids to bird muscles could be related to their small fiber size and high capillary surface density; however, most of the improved delivery of fatty acids is likely to be due to changes in protein-mediated transport (Guglielmo et al, 2002a). The bulk of fatty acid transport across the sarcolemma is mediated by proteins, including fatty acid translocase (FAT/CD36) and plasma membrane fatty acid binding protein (FABPpm), and high intracellular concentrations of the heart-type fatty acid binding protein (H-FABP) promote rapid uptake, movement and disposal of fatty acids (Luiken et al, 1999;Sweazea and Braun, 2006). Pectoralis muscles of migrating western sandpipers have an approximately 10-fold greater concentration of H-FABP (up to 11% of cytosolic protein) than that of mouse soleus muscle, and H-FABP has been shown to increase by 70% during migratory seasons compared with winter (Guglielmo et al, 2002a).…”

Section: Meeting the Challenge Of Fat-fueled Flightmentioning

confidence: 99%

Obese super athletes: fat-fueled migration in birds and bats

Guglielmo

2018

Journal of Experimental Biology

128

112

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Migratory birds are physiologically specialized to accumulate massive fat stores (up to 50-60% of body mass), and to transport and oxidize fatty acids at very high rates to sustain flight for many hours or days. Target gene, protein and enzyme analyses and recent -omic studies of bird flight muscles confirm that high capacities for fatty acid uptake, cytosolic transport, and oxidation are consistent features that make fat-fueled migration possible. Augmented circulatory transport by lipoproteins is suggested by field data but has not been experimentally verified. Migratory bats have high aerobic capacity and fatty acid oxidation potential; however, endurance flight fueled by adipose-stored fat has not been demonstrated. Patterns of fattening and expression of muscle fatty acid transporters are inconsistent, and bats may partially fuel migratory flight with ingested nutrients. Changes in energy intake, digestive capacity, liver lipid metabolism and body temperature regulation may contribute to migratory fattening. Although control of appetite is similar in birds and mammals, neuroendocrine mechanisms regulating seasonal changes in fuel store set-points in migrants remain poorly understood. Triacylglycerol of birds and bats contains mostly 16 and 18 carbon fatty acids with variable amounts of 18:2n-6 and 18:3n-3 depending on diet. Unsaturation of fat converges near 70% during migration, and unsaturated fatty acids are preferentially mobilized and oxidized, making them good fuel. Twenty and 22 carbon n-3 and n-6 polyunsaturated fatty acids (PUFA) may affect membrane function and peroxisome proliferator-activated receptor signaling. However, evidence for dietary PUFA as doping agents in migratory birds is equivocal and requires further study.

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Section: Meeting the Challenge Of Fat-fueled Flightmentioning

confidence: 99%

Obese super athletes: fat-fueled migration in birds and bats

Guglielmo

2018

Journal of Experimental Biology

128

112

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“…9 Because of the hydrophobic nature of NEFA, it has generally been assumed that they can rapidly traverse the lipid bilayer of the cell membrane by their mass action. However NEFA may also enter the cell via a carrier-mediated process in many cells, including cardiac myocytes 10 and adipocytes. 11 FAT=CD36 is a transmembrane transporter of long-chain fatty acids, 12 which in turn have been shown to upregulate the fatty acid translocase itself.…”

Section: Introductionmentioning

confidence: 99%

Changes in FAT/CD36, UCP2, UCP3 and GLUT4 gene expression during lipid infusion in rat skeletal and heart muscle

et al. 2002

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OBJECTIVE: It has been reported that an increased availability of free fatty acids (NEFA) not only interferes with glucose utilization in insulin-dependent tissues, but may also result in an uncoupling effect of heart metabolism. We aimed therefore to investigate the effect of an increased availability of NEFA on gene expression of proteins involved in transmembrane fatty acid (FAT=CD36) and glucose (GLUT4) transport and of the uncoupling proteins UCP2 and 3 at the heart and skeletal muscle level. STUDY DESIGN: Euglycemic hyperinsulinemic clamp was performed after 24 h Intralipid 1 plus heparin or saline infusion in lean Zucker rats. Skeletal and heart muscle glucose utilization was calculated by 2-deoxy-[1-3 H]-D-glucose technique. Quantification of FAT=CD36, GLUT4, UCP2 and UCP3 mRNAs was obtained by Northern blot analysis or RT-PCR. RESULTS: In Intralipid 1 plus heparin infused animals a significant decrease in insulin-mediated glucose uptake was observed both in the heart (22.62 AE 2.04 vs 10.37 AE 2.33 ng=mg=min; P < 0.01) and in soleus muscle (13.46 AE 1.53 vs 6.84 AE 2.58 ng=mg=min; P < 0.05). FAT=CD36 mRNA was significantly increased in skeletal muscle tissue ( þ 117.4 AE 16.3%, P < 0.05), while no differences were found at the heart level in respect to saline infused rats. A clear decrease of GLUT4 mRNA was observed in both tissues. The 24 h infusion of fat emulsion resulted in a clear enhancement of UCP2 and UCP3 mRNA levels in the heart (99.5 AE 15.3 and 80 AE 4%) and in the skeletal muscle (291.5 AE 24.7 and 146.9 AE 12.7%). CONCLUSIONS: As a result of the increased availability of NEFA, FAT=CD36 gene expression increases in skeletal muscle, but not at the heart level. The augmented lipid fuel supply is responsible for the depression of insulin-mediated glucose transport and for the increase of UCP2 and 3 gene expression in both skeletal and heart muscle.

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“…Evidence is accumulating that cellular LCFA uptake is a rate-governing step in LCFA utilization (10). Using heart giant membrane vesicles, a model used to investigate cardiac LCFA uptake dissected from LCFA metabolism (11) and cardiac myocytes, in which LCFA uptake is closely linked to metabolism (12), we previously showed that ϳ50% of cardiac LCFA uptake is mediated by the 88-kDa putative LCFA transport protein, fatty acid translocase (FAT)/CD36.…”

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confidence: 99%

Enhanced Sarcolemmal FAT/CD36 Content and Triacylglycerol Storage in Cardiac Myocytes From Obese Zucker Rats

et al. 2004

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In obesity, the development of cardiomyopathy is associated with the accumulation of myocardial triacylglycerols (TAGs), possibly stemming from elevation of myocardial long-chain fatty acid (LCFA) uptake. Because LCFA uptake is regulated by insulin and contractions, we examined in cardiac myocytes from lean and obese Zucker rats the effects of insulin and the contraction-mimetic agent oligomycin on the initial rate of LCFA uptake, subcellular distribution of FAT/CD36, and LCFA metabolism. In cardiac myocytes from obese Zucker rats, under basal conditions, FAT/CD36 was relocated to the sarcolemma at the expense of intracellular stores. In addition, the LCFA uptake rate, LCFA esterification rate into TAGs, and the intracellular unesterified LCFA concentration each were significantly increased. All these metabolic processes were normalized by the FAT/CD36 inhibitor sulfo-N-succinimidyloleate, indicating its antidiabetic potential. In cardiac myocytes isolated from lean rats, in vitro administration of insulin induced the translocation of FAT/ CD36 to the sarcolemma and stimulated initial rates of LCFA uptake and TAG esterification. In contrast, in myocytes from obese rats, insulin failed to alter the subcellular localization of FAT/CD36 and the rates of LCFA uptake and TAG esterification. In cardiac myocytes from lean and obese animals, oligomycin stimulated the initial rates of LCFA uptake and oxidation, although oligomycin only induced the translocation of FAT/CD36 to the sarcolemma in lean rats. The present results indicate that in cardiac myocytes from obese Zucker rats, a permanent relocation of FAT/CD36 to the sarcolemma is responsible for myocardial TAG accumulation. Furthermore, in vitro these cardiac myocytes, although sensitive to contraction-like stimulation, were completely insensitive to insulin, as the basal conditions in hyperinsulinemic, obese animals resemble the insulin-stimulated condition in lean littermates.

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Cellular fatty acid transport in heart and skeletal muscle as facilitated by proteins

Cited by 110 publications

References 47 publications

Obese super athletes: fat-fueled migration in birds and bats

Obese super athletes: fat-fueled migration in birds and bats

Changes in FAT/CD36, UCP2, UCP3 and GLUT4 gene expression during lipid infusion in rat skeletal and heart muscle

Enhanced Sarcolemmal FAT/CD36 Content and Triacylglycerol Storage in Cardiac Myocytes From Obese Zucker Rats

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