pubmed-article:17886030 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17886030 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:17886030 | lifeskim:mentions | umls-concept:C0034721 | lld:lifeskim |
pubmed-article:17886030 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
pubmed-article:17886030 | lifeskim:mentions | umls-concept:C0005775 | lld:lifeskim |
pubmed-article:17886030 | lifeskim:mentions | umls-concept:C0458827 | lld:lifeskim |
pubmed-article:17886030 | lifeskim:mentions | umls-concept:C0751982 | lld:lifeskim |
pubmed-article:17886030 | lifeskim:mentions | umls-concept:C1956394 | lld:lifeskim |
pubmed-article:17886030 | pubmed:issue | 10 | lld:pubmed |
pubmed-article:17886030 | pubmed:dateCreated | 2007-9-21 | lld:pubmed |
pubmed-article:17886030 | pubmed:abstractText | 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. | lld:pubmed |
pubmed-article:17886030 | pubmed:language | eng | lld:pubmed |
pubmed-article:17886030 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17886030 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:17886030 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17886030 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17886030 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17886030 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17886030 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17886030 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17886030 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17886030 | pubmed:month | Oct | lld:pubmed |
pubmed-article:17886030 | pubmed:issn | 1071-5762 | lld:pubmed |
pubmed-article:17886030 | pubmed:author | pubmed-author:UedaShugoS | lld:pubmed |
pubmed-article:17886030 | pubmed:author | pubmed-author:YodoiJunjiJ | lld:pubmed |
pubmed-article:17886030 | pubmed:author | pubmed-author:NakamuraTakay... | lld:pubmed |
pubmed-article:17886030 | pubmed:author | pubmed-author:WadaHiromiH | lld:pubmed |
pubmed-article:17886030 | pubmed:author | pubmed-author:YamadaAkiraA | lld:pubmed |
pubmed-article:17886030 | pubmed:author | pubmed-author:NakamuraHajim... | lld:pubmed |
pubmed-article:17886030 | pubmed:author | pubmed-author:OkuyamaHiroak... | lld:pubmed |
pubmed-article:17886030 | pubmed:author | pubmed-author:HoshinoYumaY | lld:pubmed |
pubmed-article:17886030 | pubmed:author | pubmed-author:TerataniAkieA | lld:pubmed |
pubmed-article:17886030 | pubmed:author | pubmed-author:FurukawaSuzuy... | lld:pubmed |
pubmed-article:17886030 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:17886030 | pubmed:volume | 41 | lld:pubmed |
pubmed-article:17886030 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17886030 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17886030 | pubmed:pagination | 1089-98 | lld:pubmed |
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pubmed-article:17886030 | pubmed:meshHeading | pubmed-meshheading:17886030... | lld:pubmed |
pubmed-article:17886030 | pubmed:year | 2007 | lld:pubmed |
pubmed-article:17886030 | pubmed:articleTitle | Recombinant human thioredoxin-1 becomes oxidized in circulation and suppresses bleomycin-induced neutrophil recruitment in the rat airway. | lld:pubmed |
pubmed-article:17886030 | pubmed:affiliation | Thioredoxin Project, Department of Experimental Therapeutics, Translational Research Center, Kyoto University Hospital, Sakyo-ku, Kyoto, Japan. | lld:pubmed |
pubmed-article:17886030 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:17886030 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |