Phospholipase Cgamma2 contributes to light-chain gene activation and receptor editing.

Abstract:

: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.

journal_name

Mol Cell Biol

authors

Bai L,Chen Y,He Y,Dai X,Lin X,Wen R,Wang D

doi

10.1128/MCB.02273-06

subject

Has Abstract

pub_date

2007-09-01 00:00:00

pages

5957-67

issue

17

eissn

0270-7306

issn

1098-5549

pii

MCB.02273-06

journal_volume

27

pub_type

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