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Molecular & Cellular Proteomics 1:213-222, 2002.
© 2002 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

A Proteomic Approach for Identification of Secreted Proteins during the Differentiation of 3T3-L1 Preadipocytes to Adipocytes^*

Irina Kratchmarova, Dario E. Kalume, Blagoy Blagoev, Philipp E. Scherer, Alexandre V. Podtelejnikov^¶, Henrik Molina^¶, Perry E. Bickel^||,**, Jens S. Andersen, Minerva M. Fernandez, Jacob Bunkenborg^¶, Peter Roepstorff, Karsten Kristiansen, Harvey F. Lodish, Matthias Mann^,¶, and Akhilesh Pandey^,¶¶,||||

Center for Experimental Bioinformatics, University of Southern Denmark, Odense M, DK-5230 Denmark
Department of Cell Biology, Albert Einstein College of Medicine, Bronx, New York 10461
^|| Departments of Medicine and Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110
^¶ MDS-Proteomics, Staermosegaardsvej 6, Odense M, DK-5230 Denmark
Whitehead Institute for Biomedical Research, Cambridge, Massachusetts 02142
^¶¶ Department of Pathology, Brigham and Women’s Hospital, Boston, Massachusetts 02115

We have undertaken a systematic proteomic approach to purify and identify secreted factors that are differentially expressed in preadipocytes versus adipocytes. Using one-dimensional gel electrophoresis combined with nanoelectrospray tandem mass spectrometry, proteins that were specifically secreted by 3T3-L1 preadipocytes or adipocytes were identified. In addition to a number of previously reported molecules that are up- or down-regulated during this differentiation process (adipsin, adipocyte complement-related protein 30 kDa, complement C3, and fibronectin), we identified four secreted molecules that have not been shown previously to be expressed differentially during the process of adipogenesis. Pigment epithelium-derived factor, a soluble molecule with potent antiangiogenic properties, was found to be highly secreted by preadipocytes but not adipocytes. Conversely, we found hippocampal cholinergic neurostimulating peptide, neutrophil gelatinase-associated lipocalin, and haptoglobin to be expressed highly by mature adipocytes. We also used liquid chromatography-based separation followed by automated tandem mass spectrometry to identify proteins secreted by mature adipocytes. Several additional secreted proteins including resistin, secreted acidic cysteine-rich glycoprotein/osteonectin, stromal cell-derived factor-1, cystatin C, gelsolin, and matrix metalloprotease-2 were identified by this method. To our knowledge, this is the first study to identify several novel secreted proteins by adipocytes by a proteomic approach using mass spectrometry.

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