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Submitted on September 26, 2001
Protein Chemistry, Immunex Corporation, Seattle, WA 98101-2936
Corresponding Author: johnsonr{at}immunex.com
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. Proteins were labeled with a new stable isotope coded thiol-alkylating agent prior to mass spectrometry analysis. 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.
Revised on October 24, 2001
Accepted on October 29, 2001
A proteomic approach for the identification of cell surface proteins shed by metalloproteases
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