Document Detail


Identification of redox-active cell-surface proteins by mechanism-based kinetic trapping.
MedLine Citation:
PMID:  18089859     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Ulla Schwertassek; Lars Weingarten; Tobias P Dick
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Publication Detail:
Type:  Journal Article     Date:  2007-12-18
Journal Detail:
Title:  Science's STKE : signal transduction knowledge environment     Volume:  2007     ISSN:  1525-8882     ISO Abbreviation:  Sci. STKE     Publication Date:  2007 Dec 
Date Detail:
Created Date:  2007-12-19     Completed Date:  2008-01-16     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  100964423     Medline TA:  Sci STKE     Country:  United States    
Other Details:
Languages:  eng     Pagination:  pl8     Citation Subset:  IM    
Affiliation:
Redox Regulation Research Group (A160), German Cancer Research Center (DKFZ), Im Neuenheimer Feld 280, 69120 Heidelberg, Germany.
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MeSH Terms
Descriptor/Qualifier:
Bacterial Proteins / genetics,  physiology
Base Sequence
Cell Culture Techniques / methods
Cell Membrane / physiology*
Escherichia coli / genetics,  ultrastructure
Kinetics
Membrane Proteins / genetics,  physiology*
Molecular Sequence Data
Oxidation-Reduction
Polymorphism, Single Nucleotide
Recombinant Proteins / chemistry,  metabolism
Thioredoxins / genetics
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Membrane Proteins; 0/Recombinant Proteins; 52500-60-4/Thioredoxins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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