Triglyceride Lipase

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Daniel J Rader - One of the best experts on this subject based on the ideXlab platform.

  • endothelial cells secrete Triglyceride Lipase and phosphoLipase activities in response to cytokines as a result of endothelial Lipase
    Circulation Research, 2003
    Co-Authors: Dawn Marchadier, Edelyn Octtaviani, Jane M Glick, Daniel J Rader
    Abstract:

    The endothelium interacts extensively with lipids and lipoproteins, but there are very few data regarding the ability of endothelial cells to secrete Lipases. In this study, we investigated the ability of endothelial cells to secrete the Triglyceride Lipase and phosphoLipase activities characteristic of endothelial Lipase (EL), a recently described member of the Triglyceride Lipase gene family. No Lipase activities were detected under basal conditions, but treatment with cytokines significantly stimulated the expression of both activities. Using antibodies to EL, we determined that both activities were primarily a result of this enzyme. In addition to the increase in lipolytic activity, cytokine treatment was demonstrated to substantially upregulate EL protein and EL mRNA in a dose-dependent manner. Cytokines did not change EL mRNA stability. Both new protein synthesis and activation of NF-κB influenced the induction of EL by cytokines, suggesting that multiple pathways contribute to this process. The upregulation of EL by cytokines is in sharp contrast to the downregulation by cytokines of the other two major members of this gene family, lipoprotein Lipase and hepatic Lipase, and has implications for the physiological role of EL in inflammatory conditions and its potential role in the modulation of lipoprotein metabolism during inflammatory conditions, including atherosclerosis.

  • endothelial Lipase colon a new member of the Triglyceride Lipase gene family
    Current Opinion in Lipidology, 2000
    Co-Authors: Daniel J Rader, Michael Jaye
    Abstract:

    The Triglyceride Lipase gene family plays a central role in intestinal lipid absorption, energy homeostasis, lipoprotein metabolism, and atherosclerosis. A new member of this gene family, termed endothelial Lipase, was recently reported. The presence of key functional motifs, the endothelial synthes

Johan Hoffstedt - One of the best experts on this subject based on the ideXlab platform.

Dominique Langin - One of the best experts on this subject based on the ideXlab platform.

Rudolf Zechner - One of the best experts on this subject based on the ideXlab platform.

  • Atglistatin ameliorates functional decline in heart failure via adipocyte-specific inhibition of adipose Triglyceride Lipase
    American Journal of Physiology-heart and Circulatory Physiology, 2018
    Co-Authors: Nirmal Parajuli, Rudolf Zechner, Shingo Takahara, Nobutoshi Matsumura, Mourad Ferdaoussi, Anna Katharina Migglautsch, Rolf Breinbauer, Erin E. Kershaw, Jason R.b. Dyck
    Abstract:

    This work shows, for the first time, that the adipose Triglyceride Lipase (ATGL)-specific inhibitor atglistatin can prevent worsening heart failure. Furthermore, using mice with adipocyte-specific ...

  • Nitric oxide signaling in adipose Triglyceride Lipase-deficient microvascular endothelial cells
    BMC Clinical Pharmacology, 2012
    Co-Authors: Marion Mussbacher, Rudolf Zechner, Sarah Winkler, Günter Hämmerle, Bernd Mayer, Astrid Schrammel
    Abstract:

    Background Adipose Triglyceride Lipase (ATGL) has been characterized as key enzyme of mammalian Triglyceride catabolism. Mice with global ATGL deficiency were previously described to suffer from lethal cardiac dysfunction that originates from defective peroxisome proliferator-activated receptor alpha (PPARa) signaling in the heart. Experiments from our laboratory demonstrated that endothelium-dependent microand macrovascular relaxation is severely blunted in those mice. The aim of the present study was to investigate this phenomenon on a cellular level.

  • resveratrol regulates lipolysis via adipose Triglyceride Lipase
    Journal of Nutritional Biochemistry, 2012
    Co-Authors: Arrate Lasa, Rudolf Zechner, Martina Schweiger, Petra Kotzbeck, Itziar Churruca, Edurne Simon, Maria P Portillo
    Abstract:

    Abstract Resveratrol has been reported to increase adrenaline-induced lipolysis in 3T3-L1 adipocytes. The general aim of the present work was to gain more insight concerning the effects of trans -resveratrol on lipid mobilization. The specific purpose was to assess the involvement of the two main Lipases: adipose Triglyceride Lipase (ATGL) and hormone-sensitive Lipase (HSL), in the activation of lipolysis induced by this molecule. For lipolysis experiments, 3T3-L1 and human SGBS adipocytes as well as adipose tissue from wild-type, ATGL knockout and HSL knockout mice were used. Moreover, gene and protein expressions of these Lipases were analyzed. Resveratrol-induced free fatty acids release but not glycerol release in 3T3-L1 under basal and isoproterenol-stimulating conditions and under isoproterenol-stimulating conditions in SGBS adipocytes. When HSL was blocked by compound 76-0079, free fatty acid release was still induced by resveratrol. By contrast, in the presence of the compound C, an inhibitor of adenosine monophosphate-activated protein kinase, resveratrol effect was totally blunted. Resveratrol increased ATGL gene and protein expressions, an effect that was not observed for HSL. Resveratrol increased fatty acids release in epididymal adipose tissue from wild-type and HSL knockout mice but not in that adipose tissue from ATGL knockout mice. Taking as a whole, the present results provide novel evidence that resveratrol regulates lipolytic activity in human and murine adipocytes, as well as in white adipose tissue from mice, acting mainly on ATGL at transcriptional and posttranscriptional levels. Enzyme activation seems to be induced via adenosine monophosphate-activated protein kinase.

  • fate of fat the role of adipose Triglyceride Lipase in lipolysis
    Biochimica et Biophysica Acta, 2009
    Co-Authors: Robert Zimmermann, Guenter Haemmerle, Achim Lass, Rudolf Zechner
    Abstract:

    Abstract Lipolysis, the coordinated catabolism of triacylglycerol (TG) stored in cellular lipid droplets, provides fatty acids, di-, and monoglycerides. These products are important energy substrates, precursors for other lipids, or lipid signaling molecules. Following their discovery by Hollenberg, C.H., Raben, M.S., and Astwood, E.B.(1961) and Vaughan, M., Berger, J.E., and Steinberg, D. (1964), hormone-sensitive Lipase (HSL) and monoacylglycerol Lipase stayed in the focus of research for three decades. Within the last decade, however, it became evident that the lipolytic pathway is incompletely understood. Studies on the regulation of lipolysis and the characterization of HSL-deficient mice indicated that additional previously unrecognized factors that contribute to fat catabolism must exist. This led to the discovery of the perilipin, adipophilin, Tip47 (PAT) family of lipid droplet binding proteins and the identification of a novel TG hydrolase named adipose Triglyceride Lipase (ATGL). This review focuses on the importance of ATGL as TG Lipase within the “lipolytic machinery” and the current knowledge of molecular mechanisms that regulate ATGL activity.

  • Fate of fat: The role of adipose Triglyceride Lipase in lipolysis
    Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids, 2009
    Co-Authors: Robert Zimmermann, Guenter Haemmerle, Achim Lass, Rudolf Zechner
    Abstract:

    Lipolysis, the coordinated catabolism of triacylglycerol (TG) stored in cellular lipid droplets, provides fatty acids, di-, and monoglycerides. These products are important energy substrates, precursors for other lipids, or lipid signaling molecules. Following their discovery by Hollenberg, C.H., Raben, M.S., and Astwood, E.B.(1961) and Vaughan, M., Berger, J.E., and Steinberg, D. (1964), hormone-sensitive Lipase (HSL) and monoacylglycerol Lipase stayed in the focus of research for three decades. Within the last decade, however, it became evident that the lipolytic pathway is incompletely understood. Studies on the regulation of lipolysis and the characterization of HSL-deficient mice indicated that additional previously unrecognized factors that contribute to fat catabolism must exist. This led to the discovery of the perilipin, adipophilin, Tip47 (PAT) family of lipid droplet binding proteins and the identification of a novel TG hydrolase named adipose Triglyceride Lipase (ATGL). This review focuses on the importance of ATGL as TG Lipase within the "lipolytic machinery" and the current knowledge of molecular mechanisms that regulate ATGL activity. © 2008 Elsevier B.V. All rights reserved.

Aline Mairal - One of the best experts on this subject based on the ideXlab platform.

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