Open AccessPorphyromonas gingivalis surface components induce interleukin‐1 release and tyrosine phosphorylation in macrophages
Author(s) -
Saito Atsushi,
Sojar Hakimuddin T.,
Genco Robert J.
Publication year - 1996
Publication title -
fems immunology & medical microbiology
Language(s) - English
Resource type - Journals
eISSN - 1574-695X
pISSN - 0928-8244
DOI - 10.1111/j.1574-695x.1996.tb00358.x
Subject(s) - porphyromonas gingivalis , tyrosine phosphorylation , biology , phosphorylation , tyrosine , secretion , macrophage , antigen , tyrosine kinase , sh2 domain , microbiology and biotechnology , signal transduction , immunology , biochemistry , in vitro , genetics , bacteria
The aim of the present study was to characterize the responses of macrophages to surface antigens of Porphyromonas gingivalis . Native fimbriae, full‐length recombinant fimbrillin, and a lectin‐like 12‐kDa antigen all stimulated BALB/c peritoneal macrophages to secrete interleukin (IL)‐1β. The antigens induced similar patterns of tyrosine phosphorylation; proteins in approximately 35–46 kDa range of undetermined identities were phosphorylated in the macrophages. The abilities of the surface antigens to induce IL‐1β were markedly attenuated by tyrosine kinase inhibitors. This inhibition correlated with inhibition of the induced phosphorylation of specific macrophage proteins at tyrosine. The data suggest that tyrosine kinase(s) plays an important role in the regulatory intracellular signaling mechanisms by which P. gingivalis surface antigens can mediate certain responses in macrophages.