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Journal of Lipid Research, Vol. 50, 3-21, January 2009
Copyright © 2009 by American Society for Biochemistry and Molecular Biology

Thematic Review

Adipose triglyceride lipase and the lipolytic catabolism of cellular fat stores

Rudolf Zechner¹, Petra C. Kienesberger, Guenter Haemmerle, Robert Zimmermann and Achim Lass

Institute of Molecular Biosciences, University of Graz, Austria

Published, JLR Papers in Press, October 23, 2008.

This research was supported by a grant from Genomics of Lipid-Associated Disorders (GOLD), part of the Austrian Genome Project, Genome Research in Austria (GEN-AU), funded by the Austrian Ministry of Science and Research and by the Austrian Science Foundation (FWF), Grants W901-B05DK (Doktoratskolleg Molecular Enzymolgy) and F30-B05 (SFB Lipotox).

¹ To whom correspondence should be addressed. e-mail: rudolf.zechner{at}uni-graz.at

Fatty acids (FAs) are essential components of all lipid classes and pivotal substrates for energy production in all vertebrates. Additionally, they act directly or indirectly as signaling molecules and, when bonded to amino acid side chains of peptides, anchor proteins in biological membranes. In vertebrates, FAs are predominantly stored in the form of triacylglycerol (TG) within lipid droplets of white adipose tissue. Lipid droplet-associated TGs are also found in most nonadipose tissues, including liver, cardiac muscle, and skeletal muscle. The mobilization of FAs from all fat depots depends on the activity of TG hydrolases. Currently, three enzymes are known to hydrolyze TG, the well-studied hormone-sensitive lipase (HSL) and monoglyceride lipase (MGL), discovered more than 40 years ago, as well as the relatively recently identified adipose triglyceride lipase (ATGL). The phenotype of HSL- and ATGL-deficient mice, as well as the disease pattern of patients with defective ATGL activity (due to mutation in ATGL or in the enzyme's activator, CGI-58), suggest that the consecutive action of ATGL, HSL, and MGL is responsible for the complete hydrolysis of a TG molecule. The complex regulation of these enzymes by numerous, partially uncharacterized effectors creates the "lipolysome," a complex metabolic network that contributes to the control of lipid and energy homeostasis. This review focuses on the structure, function, and regulation of lipolytic enzymes with a special emphasis on ATGL.

Supplementary key words lipolysis • hydrolase • neutral lipid storage disease

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