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- Robert Zimmermann
- Institute of Molecular Biosciences, University of Graz, Graz, Austria.
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- Juliane G. Strauss
- Institute of Molecular Biosciences, University of Graz, Graz, Austria.
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- Guenter Haemmerle
- Institute of Molecular Biosciences, University of Graz, Graz, Austria.
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- Gabriele Schoiswohl
- Institute of Molecular Biosciences, University of Graz, Graz, Austria.
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- Ruth Birner-Gruenberger
- Institute of Molecular Biosciences, University of Graz, Graz, Austria.
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- Monika Riederer
- Institute of Molecular Biosciences, University of Graz, Graz, Austria.
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- Achim Lass
- Institute of Molecular Biosciences, University of Graz, Graz, Austria.
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- Georg Neuberger
- Institute of Molecular Biosciences, University of Graz, Graz, Austria.
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- Frank Eisenhaber
- Institute of Molecular Biosciences, University of Graz, Graz, Austria.
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- Albin Hermetter
- Institute of Molecular Biosciences, University of Graz, Graz, Austria.
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- Rudolf Zechner
- Institute of Molecular Biosciences, University of Graz, Graz, Austria.
抄録
<jats:p>Mobilization of fatty acids from triglyceride stores in adipose tissue requires lipolytic enzymes. Dysfunctional lipolysis affects energy homeostasis and may contribute to the pathogenesis of obesity and insulin resistance. Until now, hormone-sensitive lipase (HSL) was the only enzyme known to hydrolyze triglycerides in mammalian adipose tissue. Here, we report that a second enzyme, adipose triglyceride lipase (ATGL), catalyzes the initial step in triglyceride hydrolysis. It is interesting that ATGL contains a “patatin domain” common to plant acyl-hydrolases. ATGL is highly expressed in adipose tissue of mice and humans. It exhibits high substrate specificity for triacylglycerol and is associated with lipid droplets. Inhibition of ATGL markedly decreases total adipose acyl-hydrolase activity. Thus, ATGL and HSL coordinately catabolize stored triglycerides in adipose tissue of mammals.</jats:p>
収録刊行物
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- Science
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Science 306 (5700), 1383-1386, 2004-11-19
American Association for the Advancement of Science (AAAS)
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キーワード
詳細情報 詳細情報について
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- CRID
- 1362262944495561856
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- NII論文ID
- 30020395359
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- ISSN
- 10959203
- 00368075
- http://id.crossref.org/issn/00368075
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- データソース種別
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- Crossref
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