Albumin fusion of thioredoxin - The production and evaluation of its biological activity for potential therapeutic applications
Albumin fusion of thioredoxin - The production and evaluation of its biological activity for potential therapeutic applications
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DOI：
10.1016/j.jconrel.2010.05.020
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发表时间：
2010-10-01
影响因子：
10.8
通讯作者：
Otagiri, Masaki
中科院分区：
文献类型：
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作者：
Ikuta, Shotaro;Chuang, Victor Tuan Giam;Otagiri, Masaki
硫氧还蛋白-1（Trx）是一种具有抗炎作用的氧化还原活性蛋白。本研究评价了白蛋白融合对Trx药代动力学和药效学特性的影响。结果表明，人血清白蛋白和融合蛋白的性质相当。融合蛋白显示出与人血清白蛋白相似的血浆浓度和器官分布特征。融合蛋白在肺中积累，达到高于Trx的水平。在胰岛素降低试验中，融合蛋白的活性是Trx活性的60%。然而，内毒素休克小鼠诱导的融合蛋白的脂多糖和D-氨基半乳糖的管理的存活率是两倍的Trx。本文报道的研究结果表明，融合蛋白可能在诸如再灌注损伤的治疗等领域具有巨大的临床应用。皇冠版权所有（C）2010由爱思唯尔B. V.出版保留所有权利。
Thioredoxin-1 (Trx) is a redox-active protein with anti-inflammatory effects. The effect of albumin fusion on the pharmacokinetic and pharmacodynamic properties of Trx was evaluated in this study. The findings indicate that the properties of human serum albumin and the fusion protein are comparable. The fusion protein showed similar plasma concentration and organ distribution profiles as human serum albumin. The fusion protein accumulated in lungs, reaching levels higher than Trx. In an insulin reducing assay, the activity of the fusion protein was 60% of the activity of Trx. However, survival rate of endotoxic shock mice induced by the administration of a lipopolysaccharide and D-galactosamine for fusion protein was double that of Trx. The findings reported herein indicate that the fusion protein is likely to have great clinical applications in areas such as the treatment of reperfusion injuries. Crown Copyright (C) 2010 Published by Elsevier B.V. All rights reserved.