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Truncated thioredoxin (Trx80) exerts unique mitogenic cytokine effects via a mechanism independent of thiol oxido‐reductase activity
Author(s) -
Pekkari Klas,
Avila-Cariño Javier,
Gurunath Ramanathan,
Bengtsson Åsa,
Scheynius Annika,
Holmgren Arne
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00214-x
Subject(s) - thioredoxin , peripheral blood mononuclear cell , cysteine , chemistry , thiol , dimer , serine , biochemistry , secretion , thioredoxin reductase , cytokine , cell growth , microbiology and biotechnology , in vitro , biology , enzyme , immunology , organic chemistry
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 <0.01, n =18). Both Trx80SGPS and Trx80C72S significantly stimulated IL‐12 and IFN‐γ secretion from PBMCs in the same manner as Trx80 ( P <0.01, n =9 and 10). The previously described Trx80 dimer is caused by non‐covalent interactions, and not by any intermolecular disulphide bonds.