کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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2831816 | 1163819 | 2010 | 7 صفحه PDF | دانلود رایگان |
In addition to their essential role in antigen presentation, MHC class II molecules have been widely described as receptors associated with signal transduction involved in regulating B cell function. However, their precise function and mechanism in signal transduction are not yet fully elucidated. Our previous studies demonstrated that cross-linking of MHC class II molecules led to the inhibition of resting B cell activation in which various signal molecules were involved. Especially, Rac-associated ROS-dependent MAP kinases, including ERK1/2 and p38, are involved in MHC class II-associated negative signal transduction in the phorbol 12, 13-dibutyrate (PDBU)-treated, but not LPS-treated, resting B cell line, 38B9. In this study, we further illustrated that PKC regulates downstream signal molecules, including MAP kinases and NF-κB in PDBU-stimulated resting B cells, together with Rac and ROS. In addition, we found that phosphatidylinositol 3-kinase (PI3K)-dependent activation of ERK/p38 MAP kinases was associated with the signaling procedure in PDBU-induced B cell activation. Collectively, Rac/ROS-related PKC and PI3K signaling are involved in a negative regulation cascade through the cross-linking of MHC class II molecules by anti-MHC class II antibodies in resting B cells.
Journal: Molecular Immunology - Volume 47, Issue 4, January 2010, Pages 706–712