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Originally published In Press as doi:10.1074/mcp.M200006-MCP200 on February 14, 2002.
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Molecular & Cellular Proteomics 1:213-222, 2002.
© 2002 by The American Society for Biochemistry and Molecular Biology, Inc.

Research

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

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

{ddagger} 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
{ddagger}{ddagger} 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.

§§ To whom correspondence may be addressed. E-mail: mann{at}bmb.sdu.dk.


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