Inhibition of platelet adhesion to collagen by monoclonal anti‐CD36 antibodies

Matsuno, Kōichirō; Díaz‐Ricart, Maribel; Montgomery, Robert R.; Aster, Richard H.; Jamieson, G.A.; Tandon, Narendra N.

doi:10.1046/j.1365-2141.1996.422962.x

Cited by 66 publications

(47 citation statements)

References 22 publications

(35 reference statements)

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“…Primary antibodies used in this study were as follows. FAT/CD36 and FABPpm were detected using the MO25 antibody (22) and FABPpm antisera (7) Animals and isolation of cardiac myocytes. Male Wistar Rats (250 -300 g) were bred on site and maintained at 20°C on a reverse light-dark cycle in approved animal holding facilities.…”

Section: Methodsmentioning

confidence: 99%

Insulin stimulates fatty acid transport by regulating expression of FAT/CD36 but not FABPpm

Chabowski

Coort²,

Callés-Escandon³

et al. 2004

American Journal of Physiology-Endocrinology and Metabolism

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Because insulin has been shown to stimulate long-chain fatty acid (LCFA) esterification in skeletal muscle and cardiac myocytes, we investigated whether insulin increased the rate of LCFA transport by altering the expression and the subcellular distribution of the fatty acid transporters FAT/CD36 and FABPpm. In cardiac myocytes, insulin very rapidly increased the expression of FAT/CD36 protein in a time-and dose-dependent manner. During a 2-h period, insulin (10 nM) increased cardiac myocyte FAT/CD36 protein by 25% after 60 min and attained a maximum after 90 -120 min (ϩ40 -50%). There was a dose-dependent relationship between insulin (10 Ϫ12 to 10 Ϫ7 M) and FAT/CD36 expression. The half-maximal increase in FAT/CD36 protein occurred at 0.5 ϫ 10 Ϫ9 M insulin, and the maximal increase occurred at 10 Ϫ9 to 10 Ϫ8 M insulin (ϩ40 -50%). There were similar insulin-induced increments in FAT/CD36 protein in cardiac myocytes (ϩ43%) and in Langendorff-perfused hearts (ϩ32%). In contrast to FAT/CD36, insulin did not alter the expression of FABPpm protein in either cardiac myocytes or the perfused heart. By use of specific inhibitors of insulin-signaling pathways, it was shown that insulin-induced expression of FAT/CD36 occurred via the PI 3-kinase/Akt insulin-signaling pathway. Subcellular fractionation of cardiac myocytes revealed that insulin not only increased the expression of FAT/CD36, but this hormone also targeted some of the FAT/CD36 to the plasma membrane while concomitantly lowering the intracellular depot of FAT/ CD36. At the functional level, the insulin-induced increase in FAT/ CD36 protein resulted in an increased rate of palmitate transport into giant vesicles (ϩ34%), which paralleled the increase in plasmalemmal FAT/CD36 (ϩ29%). The present studies have shown that insulin regulates protein expression of FAT/CD36, but not FABPpm, via the PI 3-kinase/Akt insulin-signaling pathway. fatty acid translocase; plasma membrane-associated fatty acid-binding protein; cardiac myocytes; transport; plasma membrane; low-density microsomes; perfusion; heart LONG-CHAIN FATTY ACIDS (LCFAs) are taken up into cells by passive diffusion and by protein-mediated mechanisms involving a number of fatty acid-binding proteins (12,25). Overexpression of fatty acid transporters, including fatty acid translocase (FAT/CD36) and plasma membrane-associated fatty acid-binding protein (FABPpm), increase LCFA uptake (13,14). In recent years, it has been shown that rates of LCFA transport can be regulated acutely and chronically. In heart and skeletal muscle exposed briefly to insulin (15 min) and in contracting muscle (Ͻ30 min), rates of LCFA transport are increased due to the translocation of FAT/CD36 from an intracellular depot to the plasma membrane (4, 18, 19). Expression of FAT/CD36 mRNA is upregulated by LCFAs in neonatal cardiac myocytes (30), although the functional metabolic consequences of these changes on LCFA transport and metabolism have not been determined. In more detailed studies, FAT/CD36 mRNA and protein expression and plasma...

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Section: Methodsmentioning

confidence: 99%

Insulin stimulates fatty acid transport by regulating expression of FAT/CD36 but not FABPpm

Chabowski

Coort²,

Callés-Escandon³

et al. 2004

American Journal of Physiology-Endocrinology and Metabolism

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“…In the resulting Percoll-free fraction samples, the protein content was determined by the bicinchoninic acid method, and 5 mg of each fraction were subjected to SDS-polyacrylamide gel electrophoresis and Western blotting. For detection of FAT/CD36, the antibody MO25 was used (21). The GLUT-4 was detected with a commercially available antibody (East Acres Biologicals).…”

Section: Methodsmentioning

confidence: 99%

Insulin induces the translocation of the fatty acid transporter FAT/CD36 to the plasma membrane

Luiken

Dyck

Han³

et al. 2002

American Journal of Physiology-Endocrinology and Metabolism

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-It is well known that muscle contraction and insulin can independently translocate GLUT-4 from an intracellular depot to the plasma membrane. Recently, we have shown that the fatty acid transporter FAT/CD36 is translocated from an intracellular depot to the plasma membrane by muscle contraction (Ͻ30 min) (Bonen et al. J Biol Chem 275: 14501-14508, 2000). In the present study, we examined whether insulin also induced the translocation of FAT/CD36 in rat skeletal muscle. In studies in perfused rat hindlimb muscles, we observed that insulin increased fatty acid uptake by ϩ51%. Insulin increased the rate of palmitate incorporation into triacylglycerols, diacylglycerols, and phospholipids (P Ͻ 0.05) while reducing muscle palmitate oxidation (P Ͻ 0.05). Perfusing rat hindlimb muscles with insulin increased plasma membrane FAT/CD36 by ϩ48% (P Ͻ 0.05), whereas concomitantly the intracellular FAT/CD36 depot was reduced by 68% (P Ͻ 0.05). These insulin-induced effects on FAT/CD36 translocation were inhibited by the phosphatidylinositol 3-kinase inhibitor LY-294002. Thus these studies have shown for the first time that insulin can induce the translocation of FAT/CD36 from an intracellular depot to the plasma membrane.This reveals a previously unknown level of regulation of fatty acid transport by insulin and may well have important consequences in furthering our understanding of the relation between fatty acid metabolism and insulin resistance.

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“…For detection of FAT/CD36, we used the antibody MO-25, 23 as we have reported previously. 8,9 Circulating glucose was determined as described by Bergmeyer.…”

Section: 10mentioning

confidence: 99%

The fatty acid transporter FAT/CD36 is upregulated in subcutaneous and visceral adipose tissues in human obesity and type 2 diabetes

et al. 2006

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Background: Long-chain fatty acids (LCFAs) cross the plasma membrane via a protein-mediated mechanism involving one or more LCFA-binding proteins. Among these, FAT/CD36 has been identified as key LCFA transporter in the heart and skeletal muscle, where it is regulated acutely and chronically by insulin. In skeletal muscle, FAT/CD36 expression and/or subcellular distribution is altered in obesity and type 2 diabetes. There is limited information as to whether the expression of this protein is also altered in subcutaneous and/or visceral adipose tissue depots in human obesity or type 2 diabetes. Objectives: To compare (a) the expression of FAT/CD36 in subcutaneous and visceral adipose tissue depots in lean, overweight, and obese individuals and in type 2 diabetics, (b) to determine whether the protein expression of FAT/CD36 in these depots is associated with the severity of insulin resistance (type 2 diabetes4obese4overweight/lean) and (c) whether FAT/CD36 protein expression in these adipose tissue depots is associated with alterations in circulating substrates and hormones. Subjects: Subjects who were undergoing abdominal surgery and who were lean (n ¼ 10; three men, seven women), overweight (n ¼ 10; three men, seven women) or obese (n ¼ 7; one man, six women), or who had been diagnosed with type 2 diabetes (n ¼ 5; one man, four women) participated in this study. Measurements: Subcutaneous and visceral adipose tissue samples, as well as blood samples, were obtained from the subjects while under general anesthesia. Adipose tissue samples were analyzed for FAT/CD36 using Western blotting. Serum samples were analyzed for glucose, insulin, FFA and leptin. BMI was also calculated. Results: Subcutaneous adipose tissue FAT/CD36 expression was upregulated by þ 58, þ 76 and þ 150% in overweight, obese and type 2 diabetics, respectively. Relative to subcutaneous adipose tissue, visceral adipose tissue FAT/CD36 expression was upregulated in lean ( þ 52%) and overweight subjects ( þ 30%). In contrast, in obese subjects and type 2 diabetics, no difference in FAT/CD36 protein expression was observed between their subcutaneous and visceral adipose tissue depots (P40.05). The subcutaneous adipose tissue FAT/CD36 expression (R ¼ 0.85) and the visceral adipose tissue FAT/CD36 expression (R ¼ 0.77) were associated with alteration in BMI and circulating glucose and insulin. Conclusions: Subcutaneous adipose tissue FAT/CD36 expression is upregulated in obesity and type 2 diabetes. As FAT/CD36 expression is not different in lean, overweight and obese subjects, and was only increased in type 2 diabetics, it appears that visceral adipose tissue FAT/CD36 may respond in a less dynamic manner to metabolic disturbances than subcutaneous adipose tissue FAT/CD36.

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Inhibition of platelet adhesion to collagen by monoclonal anti‐CD36 antibodies

Cited by 66 publications

References 22 publications

Insulin stimulates fatty acid transport by regulating expression of FAT/CD36 but not FABPpm

Insulin stimulates fatty acid transport by regulating expression of FAT/CD36 but not FABPpm

Insulin induces the translocation of the fatty acid transporter FAT/CD36 to the plasma membrane

The fatty acid transporter FAT/CD36 is upregulated in subcutaneous and visceral adipose tissues in human obesity and type 2 diabetes

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