Identification of redox-active cell-surface proteins by mechanism-based kinetic trapping
| Autor: | Lars Weingarten, Tobias P. Dick, Ulla Schwertassek |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
Cell
Integrin Molecular Sequence Data Cell Culture Techniques Cell Surface Proteins Biology Proteomics Polymorphism Single Nucleotide Thioredoxins Bacterial Proteins medicine Extracellular Escherichia coli Base Sequence Cell Membrane Membrane Proteins General Medicine Recombinant Proteins Cell biology Kinetics Membrane medicine.anatomical_structure Membrane protein biology.protein Thioredoxin Oxidation-Reduction |
| Zdroj: | Science's STKE : signal transduction knowledge environment. 2007(417) |
| ISSN: | 1525-8882 |
| Popis: | A number of thiol-dependent oxidoreductases are released from cells and act on the cell surface. Correspondingly, several cell-surface processes appear to depend on catalyzed thiol-disulfide exchange, including integrin activation and the fusion of viral particles with the host membrane. Tumor cells frequently increase the abundance of secreted and cell-surface forms of particular oxidoreductases, and evidence suggests that oxidoreductases released from tumor cells promote growth and contribute to the remodeling of the cellular microenvironment. Few cell-surface or membrane proteins that are targeted by extracellular redox enzymes have been identified. One major reason for this slow progress is the highly transient nature of thiol-disulfide exchange, making its detection by conventional techniques difficult or impossible. Here we describe the application of an activity-based proteomics approach, also known as "mechanism-based kinetic trapping," to identify individual cell-surface target proteins that engage in disulfide exchange with thiol-dependent oxidoreductases. Although we have applied this approach to thioredoxin-1, it should also be applicable to other members of the thioredoxin superfamily whose activity is based on the CXXC active-site motif. |
| Databáze: | OpenAIRE |
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