| Literature DB >> 15081538 |
Norihiko Kondo1, Yasuyuki Ishii, Aoi Son, Junko Sakakura-Nishiyama, Yong-Won Kwon, Masaki Tanito, Yumiko Nishinaka, Yoshiyuki Matsuo, Toshinori Nakayama, Masaru Taniguchi, Junji Yodoi.
Abstract
Thioredoxin (TRX) superfamily proteins that contain a conserved redox-active site -Cys-Xa.a.-Xa.a.-Cys- includes proinflammatory cytokine, macrophage migration inhibiting factor (MIF) and the immune regulatory cytokine, glycosylation inhibiting factor (GIF) in which Cys-60 is cysteinylated. In this report, we have analyzed the functional interaction between TRX and MIF/GIF. The stable Jurkat T cell line transfected with human TRX gene (TRX-transfectant) was highly resistant to hydrogen peroxide-induced apoptosis, but not the cell line transfected with vector (mock-transfectant). The expression level of MIF/GIF protein of TRX-transfectant was lower than that of mock-transfectant. Conversely, the expression level of intracellular TRX protein in CD4(+)-T cells derived from MIF -/- mice were significantly higher than that from background BALB/c mice. These findings collectively suggest that oxidative stress-induced apoptosis on T lymphocytes might be protected by the reciprocal regulation of TRX and MIF/GIF expression.Entities:
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Year: 2004 PMID： 15081538 DOI： 10.1016/j.imlet.2003.11.030
Source DB: PubMed Journal: Immunol Lett ISSN： 0165-2478 Impact factor: 3.685