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Originally published In Press as doi:10.1074/mcp.M100020-MCP200 on October 29, 2001.
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Molecular & Cellular Proteomics 1:30-36, 2002.
© 2002 by The American Society for Biochemistry and Molecular Biology, Inc.

Research

A Proteomic Approach for the Identification of Cell-surface Proteins Shed by Metalloproteases*

Lin Guo, June R. Eisenman, Rajeev M. Mahimkar, Jacques J. Peschon, Raymond J. Paxton, Roy A. Black and Richard S. Johnson{ddagger}

From the Immunex Corporation, Seattle, Washington 98101-2936

Proteolytic cleavage (shedding) of extracellular domains of many membrane proteins by metalloproteases is an important regulatory mechanism used by mammalian cells in response to environmental and physiological changes. Here we describe a proteomic system for analyzing cell surface shedding. The method utilized short-term culture supernatants from induced cells as starting material, followed by lectin-affinity purification, deglycosylation, and polyacrylamide gel electrophoresis separation. Relative quantitation of proteins was achieved via isotope dilution. In this study, a number of proteins already known to be shed were identified from activated monocytes and endothelial cells, thereby validating the method. In addition, a group of proteins were newly identified as being shed. The method provides an unbiased means to screen for shed proteins.

{ddagger} To whom correspondence should be addressed. Tel.: 206-381-6412; Fax: 206-621-5440; E-mail: JohnsonR{at}immunex.com.


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