Adipose triglyceride lipase and hormone-sensitive lipase are the major enzymes in adipose tissue triacylglycerol catabolism
(2006) In Journal of Biological Chemistry 281(52). p.40236-40241- Abstract
- The mobilization of free fatty acids from adipose triacylglycerol (TG) stores requires the activities of triacylglycerol lipases. In this study, we demonstrate that adipose triglyceride lipase (ATGL) and hormone-sensitive lipase (HSL) are the major enzymes contributing to TG breakdown in in vitro assays and in organ cultures of murine white adipose tissue (WAT). To differentiate between ATGL- and HSL-specific activities in cytosolic preparations of WAT and to determine the relative contribution of these TG hydrolases to the lipolytic catabolism of fat, mutant mouse models lacking ATGL or HSL and a mono-specific, small molecule inhibitor for HSL (76-0079) were used. We show that 76-0079 had no effect on TG catabolism in HSL-deficient WAT... (More)
- The mobilization of free fatty acids from adipose triacylglycerol (TG) stores requires the activities of triacylglycerol lipases. In this study, we demonstrate that adipose triglyceride lipase (ATGL) and hormone-sensitive lipase (HSL) are the major enzymes contributing to TG breakdown in in vitro assays and in organ cultures of murine white adipose tissue (WAT). To differentiate between ATGL- and HSL-specific activities in cytosolic preparations of WAT and to determine the relative contribution of these TG hydrolases to the lipolytic catabolism of fat, mutant mouse models lacking ATGL or HSL and a mono-specific, small molecule inhibitor for HSL (76-0079) were used. We show that 76-0079 had no effect on TG catabolism in HSL-deficient WAT but, in contrast, essentially abolished free fatty acid mobilization in ATGL- deficient fat. CGI-58, a recently identified coactivator of ATGL, stimulates TG hydrolase activity in wild-type and HSL-deficient WAT but not in ATGL- deficient WAT, suggesting that ATGL is the sole target for CGI-58-mediated activation of adipose lipolysis. Together, ATGL and HSL are responsible for more than 95% of the TG hydrolase activity present in murine WAT. Additional known or unknown lipases appear to play only a quantitatively minor role in fat cell lipolysis. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/681632
- author
- Schweiger, Martina ; Schreiber, Renate ; Haemmerle, Guenter ; Lass, Achim ; Fledelius, Christian ; Jacobsen, Poul ; Tornqvist, Hans LU ; Zechner, Rudolf and Zimmermann, Robert
- organization
- publishing date
- 2006
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 281
- issue
- 52
- pages
- 40236 - 40241
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- wos:000243033900054
- scopus:33846029180
- ISSN
- 1083-351X
- DOI
- 10.1074/jbc.M608048200
- language
- English
- LU publication?
- yes
- id
- a640fde8-935d-43f1-97ea-87929be839f1 (old id 681632)
- date added to LUP
- 2016-04-01 11:46:35
- date last changed
- 2024-05-07 14:03:02
@article{a640fde8-935d-43f1-97ea-87929be839f1, abstract = {{The mobilization of free fatty acids from adipose triacylglycerol (TG) stores requires the activities of triacylglycerol lipases. In this study, we demonstrate that adipose triglyceride lipase (ATGL) and hormone-sensitive lipase (HSL) are the major enzymes contributing to TG breakdown in in vitro assays and in organ cultures of murine white adipose tissue (WAT). To differentiate between ATGL- and HSL-specific activities in cytosolic preparations of WAT and to determine the relative contribution of these TG hydrolases to the lipolytic catabolism of fat, mutant mouse models lacking ATGL or HSL and a mono-specific, small molecule inhibitor for HSL (76-0079) were used. We show that 76-0079 had no effect on TG catabolism in HSL-deficient WAT but, in contrast, essentially abolished free fatty acid mobilization in ATGL- deficient fat. CGI-58, a recently identified coactivator of ATGL, stimulates TG hydrolase activity in wild-type and HSL-deficient WAT but not in ATGL- deficient WAT, suggesting that ATGL is the sole target for CGI-58-mediated activation of adipose lipolysis. Together, ATGL and HSL are responsible for more than 95% of the TG hydrolase activity present in murine WAT. Additional known or unknown lipases appear to play only a quantitatively minor role in fat cell lipolysis.}}, author = {{Schweiger, Martina and Schreiber, Renate and Haemmerle, Guenter and Lass, Achim and Fledelius, Christian and Jacobsen, Poul and Tornqvist, Hans and Zechner, Rudolf and Zimmermann, Robert}}, issn = {{1083-351X}}, language = {{eng}}, number = {{52}}, pages = {{40236--40241}}, publisher = {{American Society for Biochemistry and Molecular Biology}}, series = {{Journal of Biological Chemistry}}, title = {{Adipose triglyceride lipase and hormone-sensitive lipase are the major enzymes in adipose tissue triacylglycerol catabolism}}, url = {{http://dx.doi.org/10.1074/jbc.M608048200}}, doi = {{10.1074/jbc.M608048200}}, volume = {{281}}, year = {{2006}}, }