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TAK1 regulates multiple protein kinase cascades activated by bacterial lipopolysaccharide
Author(s) -
Lee Jongdae,
MiraArbibe Laurence,
Ulevitch Richard J.
Publication year - 2000
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1189/jlb.68.6.909
Subject(s) - microbiology and biotechnology , kinase , p38 mitogen activated protein kinases , biology , intracellular , protein kinase b , inflammation , signal transduction , map kinase kinase kinase , ask1 , iκb kinase , lipopolysaccharide , protein kinase a , nf κb , mitogen activated protein kinase kinase , immunology
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.