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The adipocyte in insulin resistance: Key molecules and the impact of the thiazolidinediones
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Adipose tissue lipolysis as a metabolic pathway to define pharmacological strategies against obesity and the metabolic syndrome
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An unsuspected metabolic role for atrial natriuretic peptides: The control of lipolysis, lipid mobilization, and systemic nonesterified fatty acids levels in humans
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Millennium fat-cell lipolysis reveals unsuspected novel tracks
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Langin D, Lucas S, Lafontan M. Millennium fat-cell lipolysis reveals unsuspected novel tracks. Horm Metab Res 2000; 32:443-452.
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Perilipin targets a novel pool of lipid droplets for lipolytic attack by hormone-sensitive lipase
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Moore HP, Silver RB, Mottillo EP, et al. Perilipin targets a novel pool of lipid droplets for lipolytic attack by hormone-sensitive lipase. J Biol Chem 2005; 280:43109-43120.
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Moore, H.P.1
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33744944318
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Perilipin promotes hormone-sensitive lipase-mediated adipocyte lipolysis via phosphorylation- dependent and -independent mechanisms
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This article sheds new light on the role of perilipin as a regulator of HSL and disputes the original idea that perilipin merely functions as a barrier protein for HSL
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Miyoshi H, Souza SC, Zhang HH, et al. Perilipin promotes hormone-sensitive lipase-mediated adipocyte lipolysis via phosphorylation- dependent and -independent mechanisms. J Biol Chem 2006; 281:15837-15844. This article sheds new light on the role of perilipin as a regulator of HSL and disputes the original idea that perilipin merely functions as a barrier protein for HSL.
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Miyoshi, H.1
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Marcinkiewicz, A.1
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Control of adipose triglyceride lipase action by serine 517 of perilipin A globally regulates protein kinase A-stimulated lipolysis in adipocytes
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Miyoshi H, Perfield JW 2nd, Souza SC, et al. Control of adipose triglyceride lipase action by serine 517 of perilipin A globally regulates protein kinase A-stimulated lipolysis in adipocytes. J Biol Chem 2007; 282:996-1002.
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Miyoshi, H.1
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Physical association between the adipocyte fatty acid-binding protein and hormone-sensitive lipase: A fluorescence resonance energy transfer analysis
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Smith AJ, Sanders MA, Thompson BR, et al. Physical association between the adipocyte fatty acid-binding protein and hormone-sensitive lipase: a fluorescence resonance energy transfer analysis. J Biol Chem 2004; 279:52399-52405.
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Smith, A.J.1
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Importance of TNFalpha and neutral lipases in human adipose tissue lipolysis
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This is a comprehensive review on the recent developments in the study of human fat cell lipolysis
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Langin D, Arner P. Importance of TNFalpha and neutral lipases in human adipose tissue lipolysis. Trends Endocrinol Metab 2006; 17:314-320. This is a comprehensive review on the recent developments in the study of human fat cell lipolysis.
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Langin, D.1
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Fat mobilization in adipose tissue is promoted by adipose triglyceride lipase
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Zimmermann R, Strauss JG, Haemmerle G, et al. Fat mobilization in adipose tissue is promoted by adipose triglyceride lipase. Science 2004; 306:1383-1386.
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Zimmermann, R.1
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Identification, cloning, expression, and purification of three novel human calcium-independent phospholipase A2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities
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Jenkins CM, Mancuso DJ, Yan W, et al. Identification, cloning, expression, and purification of three novel human calcium-independent phospholipase A2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities. J Biol Chem 2004; 279:48968-48975.
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Jenkins, C.M.1
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Desnutrin, an adipocyte gene encoding a novel patatin domain-containing protein, is induced by fasting and glucocorticoids: Ectopic expression of desnutrin increases triglyceride hydrolysis
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Villena JA, Roy S, Sarkadi-Nagy E, et al. Desnutrin, an adipocyte gene encoding a novel patatin domain-containing protein, is induced by fasting and glucocorticoids: ectopic expression of desnutrin increases triglyceride hydrolysis. J Biol Chem 2004; 279:47066-47075.
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Villena, J.A.1
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Expression, regulation, and triglyceride hydrolase activity of adiponutrin family members
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Lake AC, Sun Y, Li JL, et al. Expression, regulation, and triglyceride hydrolase activity of adiponutrin family members. J Lipid Res 2005; 46:2477-2487.
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Lake, A.C.1
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Kershaw EE, Hamm JK, Verhagen LA, et al. Adipose triglyceride lipase: function, regulation by insulin, and comparison with adiponutrin. Diabetes 2006; 55:148-157.
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Haemmerle G, Lass A, Zimmermann R, et al. Defective lipolysis and altered energy metabolism in mice lacking adipose triglyceride lipase. Science 2006; 312:734-737. This study describes the phenotype of ATGL-deficient mice, including the impact on lipolysis.
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Haemmerle G, Lass A, Zimmermann R, et al. Defective lipolysis and altered energy metabolism in mice lacking adipose triglyceride lipase. Science 2006; 312:734-737. This study describes the phenotype of ATGL-deficient mice, including the impact on lipolysis.
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19
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Adipose triglyceride lipase and hormone-sensitive lipase are the major enzymes in adipose tissue triacylglycerol catabolism
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Schweiger M, Schreiber R, Haemmerle G, et al. Adipose triglyceride lipase and hormone-sensitive lipase are the major enzymes in adipose tissue triacylglycerol catabolism. J Biol Chem 2006; 281:40236-40241.
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Adipose triglyceride lipase-mediated lipolysis of cellular fat stores is activated by CGI-58 and defective in Chanarin-Dorfman syndrome
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Lass A, Zimmermann R, Haemmerle G, et al. Adipose triglyceride lipase-mediated lipolysis of cellular fat stores is activated by CGI-58 and defective in Chanarin-Dorfman syndrome. Cell Metab 2006; 3:309-319.
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Perilipin A mediates the reversible binding of CGI-58 to lipid droplets in 3T3-L1 adipocytes
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Subramanian V, Rothenberg A, Gomez C, et al. Perilipin A mediates the reversible binding of CGI-58 to lipid droplets in 3T3-L1 adipocytes. J Biol Chem 2004; 279:42062-42071.
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Yamaguchi T, Omatsu N, Matsushita S, Osumi T. CGI-58 interacts with perilipin and is localized to lipid droplets: possible involvement of CGI-58 mislocalization in Chanarin-Dorfman syndrome. J Biol Chem 2004; 279:30490-30497.
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Yamaguchi, T.1
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24
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33744937550
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Human adipose triglyceride lipase (PNPLA2) is not regulated by obesity and exhibits low in vitro triglyceride hydrolase activity
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This report shows that ATGL and HSL expression are differently regulated in human adipose tissue
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Mairal A, Langin D, Arner P, Hoffstedt J. Human adipose triglyceride lipase (PNPLA2) is not regulated by obesity and exhibits low in vitro triglyceride hydrolase activity. Diabetologia 2006; 49:1629-1636. This report shows that ATGL and HSL expression are differently regulated in human adipose tissue.
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Diabetologia
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Mairal, A.1
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Soni KG, Lehner R, Metalnikov P, et al. Carboxylesterase 3 (EC 3.1.1.1) is a major adipocyte lipase. J Biol Chem 2004; 279:40683-40689.
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Soni KG, Lehner R, Metalnikov P, et al. Carboxylesterase 3 (EC 3.1.1.1) is a major adipocyte lipase. J Biol Chem 2004; 279:40683-40689.
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Identification of a novel member of the carboxylesterase family that hydrolyzes triacylglycerol: A potential role in adipocyte lipolysis
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Okazaki H, Igarashi M, Nishi M, et al. Identification of a novel member of the carboxylesterase family that hydrolyzes triacylglycerol: a potential role in adipocyte lipolysis. Diabetes 2006; 55:2091-2097.
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33745294013
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The ATGL gene is associated with free fatty acids, triglycerides, and type 2 diabetes
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This study suggests a role of ATGL genetic variation in lipid metabolism
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Schoenborn V, Heid IM, Vollmert C, et al. The ATGL gene is associated with free fatty acids, triglycerides, and type 2 diabetes. Diabetes 2006; 55:1270-1275. This study suggests a role of ATGL genetic variation in lipid metabolism.
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Human fat cell lipolysis: Biochemistry, regulation and clinical role
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The gene encoding adipose triglyceride lipase (PNPLA2) is mutated in neutral lipid storage disease with myopathy
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The data in this study suggest that deficiency in ATGL activity in humans, unlike in rodents, is not associated with obesity
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Fischer J, Lefevre C, Morava E, et al. The gene encoding adipose triglyceride lipase (PNPLA2) is mutated in neutral lipid storage disease with myopathy. Nat Genet 2007; 39:28-30. The data in this study suggest that deficiency in ATGL activity in humans, unlike in rodents, is not associated with obesity.
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