TAK1 regulates multiple protein kinase cascades activated by bacterial lipopolysaccharide
TAK1 regulates multiple protein kinase cascades activated by bacterial lipopolysaccharide
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DOI：
10.1189/jlb.68.6.909
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发表时间：
2000-12
影响因子：
5.5
通讯作者：
Jongdae Lee;Laurence Mira‐Arbibe;R. Ulevitch
中科院分区：
文献类型：
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作者：
Jongdae Lee;Laurence Mira‐Arbibe;R. Ulevitch
在炎症期间，细胞活化和细胞死亡之间的平衡是由多种细胞内酶级联反应的严格调控决定的。关键的调控步骤通常涉及蛋白激酶。我们发现，典型的促炎分子细菌脂多糖通过转化生长因子β激活激酶1 （TAK1）激活多种蛋白激酶，如p38、JNK、IKK‐β和PKB/Akt。我们还发现TAK1在由白细胞介素- 1触发的类似激活途径中发挥重要作用。因此，TAK1必须被认为是细胞内信号通路的一个重要组成部分，参与宿主在炎症期间对生理和/或环境应激信号的反应。
During inflammation the balance between cell activation and cell death is determined by the tight regulation of multiple intracellular enzyme cascades. Key regulatory steps often involve protein kinases. We show that the prototypical pro‐inflammatory molecule, bacterial lipopolysaccharide, activates multiple protein kinases such as p38, JNK, IKK‐β, and PKB/Akt via transforming growth factor β‐activated kinase‐1 (TAK1). We also show that TAK1 plays an important role in similar activation pathways triggered by interleukin‐1. Thus TAK1 must be considered as an important component of intracellular signaling pathways in cells involved in host responses to physiological and/or environmental stress signals during inflammation.