Open AccessTyrosine protein phosphorylation in murine B lymphocytes by stimulation with lipopolysaccharide from Porphyromonas gingivalis
Author(s) -
Kimura Shigenobu,
Koga Toshiya,
Fujiwara Taku,
Kontani Masanori,
Shintoku Keiichiro,
Kaya Hidehiro,
Hamada Shigeyuki
Publication year - 1995
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1995.tb07689.x
Subject(s) - porphyromonas gingivalis , phosphorylation , tyrosine phosphorylation , lipopolysaccharide , tyrosine , protein tyrosine phosphatase , escherichia coli , microbiology and biotechnology , biology , bacterial outer membrane , chemistry , biochemistry , immunology , bacteria , gene , genetics
The molecular effect of lipopolysaccharides (LPS) from Porphyromonas gingivalis as well as Escherichia coli on the tyrosine protein phosphorylation in the splenic B lymphocytes from LPS‐responsive C3H/HeN and LPS‐hyporesponsive C3H/HeJ mice was examined. P. gingivalis LPS induced tyrosine phosphorylation of selected membrane proteins that included the phosphoproteins with apparent molecular masses of 24.8 kDa and 26.0 kDa (p24.8 and p26.0) in the B lymphocytes from both strains of mice, while E. coli LPS induced p24.8 and p26.0 in C3H/HeN B lymphocytes only. These findings suggest that through the same tyrosine phosphorylation pathway as observed in C3H/HeN B lymphocytes, P. gingivalis LPS induced the activation of C3H/HeJ B lymphocytes in which a trigger signal by E. coli LPS could not be transduced to initiate tyrosine protein phosphorylation.