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Blood, 15 May 2001, Vol. 97, No. 10, pp. 3184-3190
IMMUNOBIOLOGY
Truncated thioredoxin (Trx80) induces production of
interleukin-12 and enhances CD14 expression in human monocytes
Klas Pekkari,
Javier Avila-Cariño,
Åsa Bengtsson,
Ramanathan Gurunath,
Annika Scheynius, and
Arne Holmgren
Human thioredoxin (Trx) is the major 12-kd cellular
disulfide-reductase that on secretion acts as a cocytokine with several interleukins. Truncated Trx with the 80 N-terminal residues (Trx80), also present in plasma, was by itself a mitogenic cytokine for human
peripheral blood mononuclear cells (PBMC). This study investigated which cells in PBMC are targets of recombinant Trx80. Purified human
CD14+ monocytes, but not B or T cells, in a synthetic
medium were activated to differentiation by Trx80 as measured by
flow cytometry of surface antigens because exposure to 100 nM Trx80
increased expression of CD14, CD40, CD54, and CD86. Proliferation of
the monocytes was increased in a dose-dependent manner by Trx80 in
concentrations ranging from 10 nM to 1 µM. Trx or interleukin (IL) 2 did not induce proliferation or expression of surface antigens on
monocytes. Trx80 alone induced secretion of IL-12 from
CD40+ monocytes in the PBMC cultures and this effect was
enhanced by IL-2. Trx80 and IL-2 together were strongly synergistic to
induce secretion of interferon- in PBMC cultures. The results showed that Trx80 is a potent cytokine for normal human monocytes and directs
the immune system in favor of a Th1 response via IL-12 production.
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