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Originally published In Press as doi:10.1074/mcp.M500330-MCP200 on February 7, 2006.
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Molecular & Cellular Proteomics 5:845-857, 2006.
© 2006 by The American Society for Biochemistry and Molecular Biology, Inc.

Research

Profiling of the Tetraspanin Web of Human Colon Cancer Cells *,S

François Le Naour{ddagger},§, Magali André{ddagger},¶, Céline Greco{ddagger}, Martine Billard{ddagger}, Bernard Sordat||, Jean-François Emile{ddagger},**, François Lanza{ddagger}{ddagger}, Claude Boucheix{ddagger} and Eric Rubinstein{ddagger}

From the {ddagger} INSERM U602, Institut André Lwoff, Université Paris XI, Hôpital Paul Brousse, 94807 Villejuif Cedex, France, || Institut Suisse de Recherches Expérimentales sur le Cancer, 1066 Epalinges, Switzerland, ** Hôpital Ambroise Paré, 92100 Boulogne-Billancourt, France, and {ddagger}{ddagger} INSERM U311, Etablissement Français du Sang-Alsace, 67065 Strasbourg, France

Tetraspanins are integral membrane proteins involved in a variety of physiological and pathological processes. In cancer, clinical and experimental studies have reported a link between tetraspanin expression levels and metastasis. Tetraspanins play a role as organizers of multimolecular complexes in the plasma membrane. Indeed each tetraspanin associates specifically with one or a few other membrane proteins forming primary complexes. Thus, tetraspanin-tetraspanin associations lead to a molecular network of interactions, the "tetraspanin web." We performed a proteomic characterization of the tetraspanin web using a model of human colon cancer consisting of three cell lines derived from the primary tumor and two metastases (hepatic and peritoneal) from the same patient. The tetraspanin complexes were isolated after immunoaffinity purification using monoclonal antibodies directed against the tetraspanin CD9, and the associated proteins were separated by SDS-PAGE and identified by mass spectrometry using LC-MS/MS. This allowed the identification of 32 proteins including adhesion molecules (integrins, proteins with Ig domains, CD44, and epithelial cell adhesion molecule) (EpCAM), membrane proteases (ADAM10, TADG-15, and CD26/dipeptidyl peptidase IV), and signaling proteins (heterotrimeric G proteins). Importantly some components were differentially detected in the tetraspanin web of the three cell lines: the laminin receptor Lutheran/B-cell adhesion molecule (Lu/B-CAM) was expressed only on the primary tumor cells, whereas CD26/dipeptidyl peptidase IV and tetraspanin Co-029 were observed only on metastatic cells. Concerning Co-029, immunohistofluorescence showed a high expression of Co-029 on epithelial cells in normal colon and a lower expression in tumors, whereas heterogeneity in terms of expression level was observed on metastasis. Finally we demonstrated that epithelial cell adhesion molecule and CD9 form a new primary complex in the tetraspanin web.

To whom correspondence should be addressed: INSERM U602, Hôpital Paul Brousse, 94807 Villejuif Cedex, France. Tel.: 33-1-45-59-53-13; Fax: 33-1-45-59-53-29; E-mail: flenaour{at}vjf.inserm.fr


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