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Molecular & Cellular Proteomics 4:1710-1717, 2005.
© 2005 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

The Lipolytic Proteome of Mouse Adipose Tissue^*,S

Ruth Birner-Gruenberger, Heidrun Susani-Etzerodt, Markus Waldhuber, Gernot Riesenhuber, Hannes Schmidinger, Gerald Rechberger, Manfred Kollroser^¶, Juliane G. Strauss, Achim Lass, Robert Zimmermann, Guenter Haemmerle, Rudolf Zechner and Albin Hermetter^,||

From the Institute of Biochemistry, Graz University of Technology, Petersgasse 12/2, the Institute of Molecular Biosciences, University of Graz, Heinrichstrasse 31a/2, and the ^¶ Institute of Forensic Medicine, Medical University of Graz, A-8010 Graz, Austria

Hydrolysis of triacylglycerols and cholesteryl esters is a key event in energy homeostasis of animals. However, many lipolytic activities still await their molecular identification. Here we report on a novel tool for concomitant analysis of lipases in complex proteomes. Fluorescent activity tags mimicking lipid substrates were used to label the proteome of mouse adipose tissue. Analysis by two-dimensional gel electrophoresis and LC-MS/MS led to the identification of all known intracellular lipases as well as a number of novel candidates. One of them was recently shown to be involved in triacylglycerol mobilization in adipocytes and therefore named adipose triglyceride lipase. Functional characterization of expressed enzymes demonstrated that lipolytic and esterolytic activities could be well discriminated. Thus our results show the first map of the lipolytic proteome of mouse adipose tissue and demonstrate the general applicability of our method for rapid profiling and identification of lipolytic activities in complex biological samples.

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