Copper-mediated cross-linking of S100A4, but not of S100A2, results in proinflammatory effects in melanoma cells |
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Authors: | Haase-Kohn Cathleen Wolf Susann Lenk Jens Pietzsch Jens |
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Institution: | Helmholtz-Zentrum Dresden-Rossendorf, Institute of Radiopharmacy, Department of Radiopharmaceutical Biology, Dresden, Germany |
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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 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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Keywords: | Abbreviations: CuSO4 copper(II)-sulfate DTPA ethylene-diaminepentaacetic acid DTT dithiothreitol EDTA ethylenediaminetetraacetic acid HEPES 4-(2-hydroxyethyl)-1-piperazine-ethanesulfonic acid KCl kalium chloride MgCl2 magnesium chloride MALDI-MS matrix-assisted laser desorption/ionization mass spectrometry NFκB nuclear factor &lsquo kappa-light-chain-enhancer&rsquo of activated B-cells PVDF polyvinylidene fluoride RAGE receptor for advanced glycation endproducts SDS&ndash PAGE sodium dodecylsulfate polyacrylamide gel electrophoresis TNF-α tumor necrosis factor-alpha |
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