Cited by 595Lipid metabolism and biosynthesisLipid metabolism and disordersAdipose Tissue and Metabolism

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Adipose triglyceride lipase and the lipolytic catabolism of cellular fat stores.

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Zechner, Rudolf, Kienesberger, Petra C., Haemmerle, Guenter, Zimmermann, Robert, Lass, Achim·2009·Journal of Lipid Research

DOI 10.1194/jlr.r800031-jlr200

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Abstract

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.

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Authors: Zechner, R., Kienesberger, P. C., Haemmerle, G., Zimmermann, R., & Lass, A.
Affiliations: University of Graz (AT)
ORCID: Zechner, Rudolf
Kienesberger, Petra C.
Haemmerle, Guenter
Zimmermann, Robert
Lass, Achim
Venue: Journal of Lipid Research
Publisher: Elsevier BV
Published: 2009-01
Volume: 50
Issue: 1
Pages: 3-21
ISSN: 0022-2275 (ISSN-L)
DOI: 10.1194/jlr.r800031-jlr200
OpenAlex: W2055651091
Cited by: 576
References: 218
Citations by year: 2026: 17 · 2025: 17 · 2024: 33 · 2023: 26 · 2022: 28 · 2021: 23 · 2020: 17 · 2019: 28 · 2018: 22 · 2017: 34 · 2016: 33 · 2015: 35 · 2014: 36 · 2013: 55 · 2012: 45
FWCI: 3.04
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 4297 d)
Locations: Journal of Lipid Research (publishedVersion, cc-by)
PubMed (publishedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipid metabolism and disorders
Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
Keywords: adipose triglyceride lipase, hormone-sensitive lipase, monoglyceride lipase, lipolysis, lipid droplets, triacylglycerol mobilization, CGI-58, energy homeostasis, fatty acid mobilization
MeSH terms: Adipose Tissue, Animals, Sterol Esterase, Fatty Acids, Humans, Hydrolases, Hydrolysis, Lipase, Lipids, Lipolysis, Metabolism, Monoacylglycerol Lipases, Mutation, Phenotype, Mice

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Adipose triglyceride lipase and the lipolytic catabolism of cellular fat stores.

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