Uncoupling CD21 and CD19 of the B-cell coreceptor.

Complement receptors (CRs) CD21 and CD35 form a coreceptor with CD19 and CD81 on murine B cells that when coligated with the B-cell receptor lowers the threshold of activation by several orders of magnitude. This intrinsic signaling role is thought to explain the impaired humoral immunity of mice bearing deficiency in CRs. However, CRs have additional roles on B cells independent of CD19, such as transport of C3-coated immune complexes and regulation of C4 and C3 convertase.

B cell activation leads to upregulated expression of the murine Sik-similar protein gene.

B cells stimulated by the combination of CD40L plus anti-Ig were screened for upregulated gene expression in an unbiased fashion through differential display. An inducible transcript was obtained that corresponds to a sequence previously isolated from pre-B cells and termed murine Sik-similar protein (mSSP). The mSSP gene is predominantly expressed in lymphoid tissues, including spleen and thymus, as well as testis, with lesser amounts in kidney and ovary.

BCR engagement induces Fas resistance in primary B cells in the absence of functional Bruton's tyrosine kinase.

B cell susceptibility to Fas-mediated apoptosis is regulated in a receptor-specific fashion. CD40 engagement produces marked sensitivity to Fas killing, whereas surface Ig (sIg) engagement blocks Fas signaling for cell death in otherwise sensitive, CD40-stimulated B cell targets, and thus, induces a state of Fas resistance. The signaling mediator, Bruton's tyrosine kinase (Btk), is required for certain sIg-triggered responses, and Btk is reported to directly bind Fas and block Fas-mediated apoptosis.