Truncated thioredoxin (Trx80) exerts unique mitogenic cytokine effects via a mechanism independent of thiol oxido-reductase activity

Recently we discovered that a naturally occurring C-terminally truncated thioredoxin (Trx80) is a potent mitogenic cytokine stimulating IL-12 production from CD40 + monocytes. To further characterise Trx80 we have engineered cysteine to serine mutants of Trx80 corresponding to the active site cystei...

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Veröffentlicht in:	FEBS letters 2003-03, Vol.539 (1), p.143-148
Hauptverfasser:	Pekkari, Klas, Avila-Cariño, Javier, Gurunath, Ramanathan, Bengtsson, Åsa, Scheynius, Annika, Holmgren, Arne
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding Sites Cell Division Cells, Cultured Cysteine - chemistry Cysteine - metabolism Cytokine DTT, dithiothreitol Humans Interferon-gamma - metabolism Interleukin-12 - metabolism Mitogens - chemistry Mitogens - genetics Mitogens - physiology Monocyte Mutagenesis, Site-Directed PBMC, peripheral blood mononuclear cell Peptide Fragments - chemistry Peptide Fragments - genetics Peptide Fragments - physiology Redox Substrate Specificity Thioredoxin Thioredoxins - chemistry Thioredoxins - genetics Trx, thioredoxin Trx80, C-terminally truncated thioredoxin containing the 80 N-terminal amino acids of Trx TrxR, thioredoxin reductase
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Zusammenfassung:	Recently we discovered that a naturally occurring C-terminally truncated thioredoxin (Trx80) is a potent mitogenic cytokine stimulating IL-12 production from CD40 + monocytes. To further characterise Trx80 we have engineered cysteine to serine mutants of Trx80 corresponding to the active site cysteines of Trx (Trx80SGPS) and to the structural cysteine at position 72 (Trx80C72S). Trx80SGPS and Trx80C72S retained the cell stimulatory activity of Trx80 and increased peripheral blood mononuclear cell (PBMC) proliferation three- to five-fold in vitro ( P
ISSN:	0014-5793 1873-3468
DOI:	10.1016/S0014-5793(03)00214-X