Porphyromonas gingivalis LPSによるマウスB細胞の増殖反応にかかわる25kDaチロシンリン酸化タンパク質の解析

概要

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To elucidate B cell activation induced by Porphyromonas gingivalis, the lipopolysaccharide (LPS)-induced B cell proliferation and tyrosine phosphorylation in B cells from C 3 H/HeN and LPS-hyporesponsive C 3 H/HeJ mice were examined. P. gingivalis LPS induced cell proliferation of both C 3 H/HeN and C 3 H/HeJ B cells, accompanied by the induction of tyrosine phosphorylation of selected proteins that included 25 kDa protein (p25). In contrast, Escherichia coli LPS activated only C 3 H/HeN B cells to proliferate and to induce tyrosine phosphorylation of p25. In order to characterize p25, P. gingivalis LPS-activated B cell lysates were separated by two-dimensional gel electrophoresis (2D-PAGE). Two out of 8 spots of the candidates of p25 separated by 2D-PAGE were identified as Ran (Ras-like nuclear protein) by peptide mass fingerprinting with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). Western blotting analysis revealed that Ran existed as at least 4 spots in B cells with and without LPS stimulation. However, total amounts and the amount of the most acidic spot of Ran apparently increased by P. gingivalis LPS stimulation. These results suggested that quantitative alteration and tyrosine phosphorylation of Ran are involved in P. gingivalis LPS-induced B cell proliferation.
岩手医科大学歯学会の論文
2007-04-25