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• W2080357351 startingPage "1189" @default.
• W2080357351 abstract "Thioredoxin (Trx) is a protein disulfide oxidoreductase that can be secreted and act as a chemoattractant for leukocytes. Like chemokines, it causes desensitization of monocytes against its chemotactic activity and that of monocyte chemoattractant protein-1 (MCP-1). To investigate the role of the redox properties of Trx, and particularly of some of its five cysteines, in its chemotactic and desensitizing action, we tested different mutants, including Trx80, a truncated form, and various mutants lacking specific cysteines: Trx C62S/C73S and the redox-inactive mutant Trx C32S/C35S. Of the mutants, only Trx80 maintained the chemotactic activity of wild-type Trx toward both monocytes and polymorphonuclear neutrophils, all of them desensitized monocytes against wild-type Trx or MCP-1, but not chemotactic peptide formyl-methionyl-leucil peptide. These data indicate that different redox-active cysteines are important for Trx chemotactic action, whereas its desensitizing action does not have these requirements, suggesting a redox-independent mechanism.Antioxid. Redox Signal. 7, 1189–1194." @default.
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• W2080357351 date "2005-09-01" @default.
• W2080357351 modified "2023-10-11" @default.
• W2080357351 title "Requirements for the Different Cysteines in the Chemotactic and Desensitizing Activity of Human Thioredoxin" @default.
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• W2080357351 doi "https://doi.org/10.1089/ars.2005.7.1189" @default.
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