Document Detail


Copper-mediated cross-linking of S100A4, but not of S100A2, results in proinflammatory effects in melanoma cells.
MedLine Citation:
PMID:  21924240     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
The aim of this study was to investigate the response to and the physiological consequences of copper-mediated cross-linking of S100A2 and S100A4, two members of the S100 family of EF-hand calcium-binding proteins. As demonstrated by electrophoresis and mass spectrometry techniques S100A2 and S100A4 show formation of cross-links due to copper-mediated oxidation of cysteine residues. For S100A4, but not for S100A2, this results in both increased activation of NFκB and secretion of TNF-α in human A375 and, to a higher extent, in RAGE-transfected melanoma cells. The data suggest that a prooxidative tumor microenvironment enhances proinflammatory and prometastatic action of S100A4.
Authors:
Cathleen Haase-Kohn; Susann Wolf; Jens Lenk; Jens Pietzsch
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-9-6
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  -     ISSN:  1090-2104     ISO Abbreviation:  -     Publication Date:  2011 Sep 
Date Detail:
Created Date:  2011-9-19     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2011. Published by Elsevier Inc.
Affiliation:
Helmholtz-Zentrum Dresden-Rossendorf, Institute of Radiopharmacy, Department of Radiopharmaceutical Biology, Dresden, Germany.
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