| Copper-mediated cross-linking of S100A4, but not of S100A2, results in proinflammatory effects in melanoma cells. | |
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MedLine Citation:
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PMID: 21924240 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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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. |
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Authors:
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Cathleen Haase-Kohn; Susann Wolf; Jens Lenk; Jens Pietzsch |
Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-9-6 |
Journal Detail:
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Title: Biochemical and biophysical research communications Volume: - ISSN: 1090-2104 ISO Abbreviation: - Publication Date: 2011 Sep |
Date Detail:
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Created Date: 2011-9-19 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0372516 Medline TA: Biochem Biophys Res Commun Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Copyright Information:
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Copyright © 2011. Published by Elsevier Inc. |
Affiliation:
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Helmholtz-Zentrum Dresden-Rossendorf, Institute of Radiopharmacy, Department of Radiopharmaceutical Biology, Dresden, Germany. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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