Details

Autor(en) / Beteiligte

• Nakamura, Takayuki
• Hoshino, Yuma
• Yamada, Akira
• Teratani, Akie
• Furukawa, Suzuyo
• Okuyama, Hiroaki
• Ueda, Shugo
• Wada, Hiromi
• Yodoi, Junji
• Nakamura, Hajime

Titel

Recombinant human thioredoxin-1 becomes oxidized in circulation and suppresses bleomycin-induced neutrophil recruitment in the rat airway

Ist Teil von

• Free radical research, 2007-01, Vol.41 (10), p.1089-1098

Ort / Verlag

England: Informa UK Ltd

Erscheinungsjahr

2007

Quelle

Taylor & Francis

Beschreibungen/Notizen

• Thioredoxin-1 (TRX) is a redox-active protein with anti-inflammatory effects. This study investigated the optimal delivery method and the mechanisms of recombinant human TRX (rhTRX) to suppress neutrophil recruitment in a rat bleomycin (BLM)-induced sustained acute lung injury model. In male Wister rats intratracheally administered with 0.125 mg/kg BLM, 8 mg/kg/day rhTRX was intravenously administered on days 3-6 using one of three protocols: daily bolus injection, 3 h daily infusion or continuous infusion for 96 h. Only the continuous-infusion of rhTRX significantly reduced the neutrophil infiltration compared with the other two methods. The BLM-induced down-regulation of l-selectin expression on circulating neutrophils was inhibited by rhTRX. Oxidized rhTRX showed a comparable effect with reduced rhTRX and rhTRX incubated with plasma or circulating in plasma was more than 99% oxidized. These results suggest that rhTRX becomes oxidized in circulation and continuous infusion of rhTRX suppresses neutrophil recruitment in the airway.