Premium
Toll‐like receptor 2 (TLR2) mediates activation of stress‐activated MAP kinase p38
Author(s) -
Vasselon Thierry,
Hanlon William A,
Wright Samuel D,
Detmers Patricia A.
Publication year - 2002
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.71.3.503
Subject(s) - tlr2 , p38 mitogen activated protein kinases , biology , microbiology and biotechnology , mitogen activated protein kinase , kinase , toll like receptor , tlr4 , signal transduction , protein kinase a , receptor , innate immune system , biochemistry
Early events in the response of cells to lipopolysaccharide (LPS) include activation of NF‐κB and stress‐activated MAP kinase p38. Recent studies have shown that the human Toll‐like receptor 2 (TLR2) mediates activation of NF‐κB in response to commercial preparations of LPS (comLPS), membrane lipoproteins, and Gram‐positive bacterial products. Here, we show that expression of TLR2 in human embryonic kidney 293 cells enabled p38 phosphorylation in response to comLPS, a synthetic bacterial lipoprotein, and B. subtilis . Activation of p38 was confirmed by an in vitro kinase assay using ATF2 as substrate and by an assay measuring activation of the downstream effector of p38, MAP kinase‐activated protein kinase in cells. Thus, TLR2 initiated the signaling pathway for p38 in response to bacterial products.