| First Author | Kin NW | Year | 2007 |
| Journal | J Immunol | Volume | 179 |
| Issue | 3 | Pages | 1516-23 |
| PubMed ID | 17641017 | Mgi Jnum | J:149951 |
| Mgi Id | MGI:3849403 | Doi | 10.4049/jimmunol.179.3.1516 |
| Citation | Kin NW, et al. (2007) CD86 regulates IgG1 production via a CD19-dependent mechanism. J Immunol 179(3):1516-23 |
| abstractText | CD86 signals directly in a B cell to activate PI3K and increase the rate of IgG(1) production, without affecting germline transcription. However, the mechanism by which CD86 activates PI3K in a B cell and the relevance of CD86 stimulation in vivo remains unknown. We show that the addition of CD28/Ig to CD40 ligand/IL-4-activated wild-type, but not CD86- or CD19-deficient, B cells increased the level of phosphorylation for Lyn and CD19, as well as the amount of Lyn, Vav, and PI3K that immunoprecipitated with CD19. Adoptive transfer of CD86-deficient B cells and wild-type CD4(+) T cells into RAG2-deficient mice and immunization with trinitrophenylated keyhole limpet hemocyanin resulted in an IL-4 and germline IgG(1) response equivalent to control mice, but a decrease in serum IgG(1). Thus, our findings suggest that CD86 plays a key role in regulating the level of IgG(1) produced in vitro and in vivo, and that Lyn and CD19 may be the signaling intermediates activated by CD86 proximal to PI3K. |
