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Adipose triglyceride lipase and the lipolytic catabolism of cellular fat stores.
Open accessAbstract
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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“Insulin suppresses lipolysis by increasing the activity of phosphodiesterase 3B (PDE3B), leading to decreased cAMP-mediated activation of protein kinase A (PKA), and, consequently, reduced phosphorylation of hormone-sensitive lipase (HSL) and perilipin (PLIN).”
From Effect of Exercise Training on Fat Loss—Energetic Perspectives and the Role of Improved Adipose Tissue Function and Body Fat Distribution (2021) · cites this paper as Zechner et al., 2009
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Metadata
- Authors
- Zechner, R., Kienesberger, P. C., Haemmerle, G., Zimmermann, R., & Lass, A.
- Affiliations
- University of Graz (AT)
- Venue
- Journal of Lipid Research
- Publisher
- Elsevier BV
- Published
- 2009-01
- Volume
- 50
- Issue
- 1
- Pages
- 3-21
- ISSN
- 0022-2275 (ISSN-L)
- 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
- 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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