| First Author | Bai L | Year | 2007 |
| Journal | Mol Cell Biol | Volume | 27 |
| Issue | 17 | Pages | 5957-67 |
| PubMed ID | 17591700 | Mgi Jnum | J:125007 |
| Mgi Id | MGI:3723357 | Doi | 10.1128/MCB.02273-06 |
| Citation | Bai L, et al. (2007) Phospholipase Cgamma2 contributes to light-chain gene activation and receptor editing. Mol Cell Biol 27(17):5957-67 |
| abstractText | Phospholipase Cgamma2 (PLCgamma2) is critical for pre-B-cell receptor (pre-BCR) and BCR signaling. Current studies discovered that PLCgamma2-deficient mice had reduced immunoglobulin lambda (Iglambda) light-chain usage throughout B-cell maturation stages, including transitional type 1 (T1), transitional type 2 (T2), and mature follicular B cells. The reduction of Iglambda rearrangement by PLCgamma2 deficiency was not due to specifically increased apoptosis or decreased proliferation of mutant Iglambda+ B cells, as lack of PLCgamma2 exerted a similar effect on apoptosis and proliferation of both Iglambda+ and Igkappa+ B cells. Moreover, PLCgamma2-deficient IgHEL transgenic B cells exhibited an impairment of antigen-induced receptor editing among both the endogenous lambda and kappa loci in vitro and in vivo. Importantly, PLCgamma2 deficiency impaired BCR-induced expression of IRF-4 and IRF-8, the two transcription factors critical for lambda and kappa light-chain rearrangements. Taken together, these data demonstrate that the PLCgamma2 signaling pathway plays a role in activation of light-chain loci and contributes to receptor editing. |
