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

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

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

doi

10.1016/j.bbrc.2011.08.132

subject

Has Abstract

pub_date

2011-09-30 00:00:00

pages

494-8

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(11)01551-8

journal_volume

413

pub_type

杂志文章

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