Abstract
To study the function of Ig-α in the selection of autoreactive B cells, we have analyzed mb-1 cytoplasmic truncation mutant mice ( mb-1 Δc/Δc ), which coexpress transgenes encoding hen egg lysozyme (HEL) and HEL-specific immunoglobulin. We demonstrate that in the presence of soluble HEL (sHEL) and dependent on the mb-1 Δc mutation, most immature B cells bearing the HEL-specific Ig transgene undergo rearrangements of endogenous κ light chains, resulting in loss of HEL specificity. Moreover, immature B cells from Ig-α mutant mice respond to BCR cross-linking with an exaggerated and prolonged calcium response and induction of protein tyrosine phosphorylation. Our data imply a negative signaling role for Ig-α in immature B cells.
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