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

The DOI matches its Crossref record; 217 of the 218 references it cites were found in a registry or an index.

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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Crossref · 10.1194/jlr.r800031-jlr200

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217 of 217 references verified0 citation errors · 0 not checkable

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Citations

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1 retracted

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Research works printed but not linked: 1

  1. Quagliarello, 1932, The existence of a lipase in adipose tissue., Arch. Sci. Biol., 17, 513

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Metadata

Authors
Zechner, R., Kienesberger, P. C., Haemmerle, G., Zimmermann, R., & Lass, A.
Affiliations
University of Graz (AT)
ORCID
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
Licence
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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