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A more recent version of this article appeared on November 1, 2005.
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Submitted on March 4, 2005
Revised on July 5, 2005
Accepted on July 26, 2005

The lipolytic proteome of mouse adipose tissue

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

Biochemistry Dept., Graz University of Technology, Graz A-8010

Corresponding Author: albin.hermetter{at}tugraz.at

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 2D-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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