Cold-inducible RNA-binding protein (CIRP) triggers inflammatory responses in hemorrhagic shock and sepsis.
Cold-inducible RNA-binding protein (CIRP) triggers inflammatory responses in hemorrhagic shock and sepsis.
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作者：
在出血性和脓毒性休克的患者中观察到过量的促炎介质的产生。在这里，我们报告了在外科ICU个体血液中检测冷诱导rna结合蛋白（CIRP）。在出血和脓毒症的动物模型中，CIRP在几个器官中上调并释放到循环中。在缺氧胁迫下，巨噬细胞中的CIRP从细胞核转移到胞浆中并主动释放。重组CIRP刺激动物巨噬细胞释放TNF-α和HMGB1，诱导炎症反应，引起组织损伤。CIRP的抗血清可减轻休克引起的炎症、组织损伤和致死率。细胞外CIRP的活性是通过TLR4/MD2复合物介导的。表面等离子体共振分析表明，CIRP结合TLR4/MD2复合物以及单个TLR4和MD2。人CIRP氨基酸段106-125以高亲和力与MD2结合。综上所述，CIRP是一种新的促炎休克介质。
Excessive production of proinflammatory mediators is observed in patients undergoing hemorrhagic and septic shock. Here, we report the detection of cold-inducible RNA-binding protein (CIRP) in the blood of surgical ICU individuals. In animal models of hemorrhage and sepsis, CIRP is up-regulated in several organs and released into the circulation. Under hypoxic stresses, CIRP in macrophages is translocated from the nucleus to the cytosol and actively released. Recombinant CIRP stimulates TNF-α and HMGB1 release in macrophages as well as induces inflammatory responses and causes tissue injury in animals. Antisera to CIRP attenuate shock-induced inflammation, tissue injury, and lethality. Extracellular CIRP's activity is mediated through the TLR4/MD2 complex. Surface plasmon resonance analysis indicates that CIRP binds to the TLR4/MD2 complex as well as to individual TLR4 and MD2. The human CIRP amino-acid segment 106-125 binds to MD2 with high affinity. Collectively, CIRP is a new proinflammatory mediator of shock.
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富含甘氨酸的RNA结合蛋白，介导了对哺乳动物细胞生长的冷诱导抑制。
影响因子：
7.8
作者：
Nishiyama, H;Itoh, K;Kaneko, Y;Kishishita, M;Yoshida, O;Fujita, J
通讯作者：
Fujita, J
影响因子：
8.8
作者：
Benhamou, Ygal;Favre, Julie;Tamion, Fabienne
通讯作者：
Tamion, Fabienne
DOI：
10.1006/bbrc.1998.8482
发表时间：
1998-04-17
影响因子：
3.1
作者：
Nishiyama, H;Xue, JH;Fujita, J
通讯作者：
Fujita, J
影响因子：
3.7
作者：
De Leeuw, Frederic;Zhang, Tong;Gueydan, Cyril
通讯作者：
Gueydan, Cyril
影响因子：
4.4
作者：
Ohashi, K;Burkart, V;Kolb, H
通讯作者：
Kolb, H