Copper-mediated cross-linking of S100A4, but not of S100A2, results in proinflammatory effects in melanoma cells.

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Haase-Kohn C, Wolf S, Lenk J, Pietzsch J

Copper-mediated cross-linking of S100A4, but not of S100A2, results in proinflammatory effects in melanoma cells.

Biochem Biophys Res Commun. 2011 Sep 30;413(3):494-8. doi: 10.1016/j.bbrc.2011.08.132. Epub 2011 Sep 6.

PubMed ID
21924240 [ View in PubMed
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Abstract

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 NFkappaB and secretion of TNF-alpha 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.

DrugBank Data that Cites this Article

Drug Targets
DrugTargetKindOrganismPharmacological ActionActions
CopperProtein S100-A2ProteinHumans
Unknown
Not AvailableDetails
CopperProtein S100-A4ProteinHumans
Unknown
Not AvailableDetails