Carboxylesterase 3 (EC is a major adipocyte lipase

Soni, Krishnakant G., Lehner, Richard, Metalnikov, Pavel, O'Donnell, Paul, Semache, Meriem, Gao, Wenhui, Ashman, Keith, Pshezhetsky, Alexey V. and Mitchell, Grant A. (2004) Carboxylesterase 3 (EC is a major adipocyte lipase. Journal of Biological Chemistry, 279 39: 40683-40689. doi:10.1074/jbc.M400541200

Attached Files (Some files may be inaccessible until you login with your UQ eSpace credentials)
Name Description MIMEType Size Downloads
UQ291800_OA.pdf Full text (open access) application/pdf 456.46KB 0

Author Soni, Krishnakant G.
Lehner, Richard
Metalnikov, Pavel
O'Donnell, Paul
Semache, Meriem
Gao, Wenhui
Ashman, Keith
Pshezhetsky, Alexey V.
Mitchell, Grant A.
Title Carboxylesterase 3 (EC is a major adipocyte lipase
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
Publication date 2004-09-24
Sub-type Article (original research)
DOI 10.1074/jbc.M400541200
Open Access Status File (Publisher version)
Volume 279
Issue 39
Start page 40683
End page 40689
Total pages 7
Place of publication Bethesda, MD, United States
Publisher American Society for Biochemistry and Molecular Biology
Language eng
Formatted abstract
Hydrolysis of triglycerides is central to energy homeostasis in white adipose tissue (WAT). Hormone-sensitive lipase (HSL) was previously felt to mediate all lipolysis in WAT. Surprisingly, HSL-deficient mice show active HSL-independent lipolysis, suggesting that other lipase(s) also mediate triglyceride hydrolysis. To clarify this, we used functional proteomics to detect non-HSL lipase(s) in mouse WAT. After cell fractionation of intraabdominal WAT, most non-HSL neutral lipase activity is localized in the 100,000 × g infranatant and fat cake fractions. By oleic acid-linked agarose chromatography of infranatant followed by elution in a 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonic acid gradient, we identified two peaks of esterase activity using p-nitrophenyl butyrate as a substrate. One of the peaks contained most of the lipase activity. In the corresponding fractions, gel permeation chromatography and SBS-PAGE, followed by tandem mass spectrometric analysis of excised Coomassie Blue-stained peptides, revealed carboxylesterase 3 (triacylglycerol hydrolase (TGH); EC TGH is also the principle lipase of WAT fat cake extracts. Partially purified WAT TGH had lipase activity as well as lesser but detectable neutral cholesteryl ester hydrolase activity. Western blotting of subcellular fractions of WAT and confocal microscopy of fibroblasts following in vitro adipocytic differentiation are consistent with a distribution of TGH to endoplasmic reticulum, cytosol, and the lipid droplet. TGH is responsible for a major part of non-HSL lipase activity in WAT in vitro and may mediate some or all HSL-independent lipolysis in adipocytes.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemistry and Molecular Biosciences
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 109 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 103 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Thu, 21 Feb 2013, 22:38:16 EST by System User on behalf of Learning and Research Services (UQ Library)