
Protein phosphorylation pathways involved during lipopolysaccharide‐induced expression of CD14 in mouse bone marrow granulocytes
Author(s) -
Pedron Thierry,
Girard Robert,
Chaby Richard
Publication year - 2000
Publication title -
fems immunology & medical microbiology
Language(s) - English
Resource type - Journals
eISSN - 1574-695X
pISSN - 0928-8244
DOI - 10.1111/j.1574-695x.2000.tb01484.x
Subject(s) - biology , kinase , protein kinase a , cd14 , c raf , map2k7 , map kinase kinase kinase , microbiology and biotechnology , p38 mitogen activated protein kinases , mitogen activated protein kinase , ask1 , mitogen activated protein kinase kinase , cyclin dependent kinase 2 , biochemistry , receptor
Lipopolysaccharide (LPS) of Gram‐negative bacteria interacts with a CD14‐independent receptor of mouse bone marrow granulocytes (BMC), and triggers in these cells the expression of CD14, an inducible type of LPS receptor (iLpsR). This particular response of BMC to LPS required the activation of protein tyrosine kinase and p38 MAP kinase. The inhibition of the LPS effect by the MEK inhibitor PD‐98059 suggested that the ERK pathway was also involved. Unexpectedly, protein kinase C, myosin light chain kinase, cAMP‐, cGMP‐, and Ca 2+ /calmodulin‐dependent kinases, as well as ecto‐protein kinases, were not required for iLpsR expression. However, other yet unidentified serine/threonine protein kinase(s) were implied since the BMC response to LPS was markedly reduced after exposure to three inhibitors of such kinases (K‐252a, H‐7, and KT‐5823). The atypical kinase requirements observed in this study may be due either to a novel signaling LPS receptor complex present in BMC, or to the particular events involved in CD14 biosynthesis.