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The Ig-alpha/Ig-beta heterodimers encoded by mb-1 and B29 genes, respectively, are crucial for the constitution of the B-cell receptor (BCR). We report here novel variants of mb-1 and B29 transcripts produced by alternative mRNA splicing. The proteins encoded by these variants are predicted to conserve transmembrane and cytoplasmic portions of Ig-alpha and Ig-beta but lack a part of the extracellular portions containing cysteine residues which are required for intramolecular and intermolecular S-S bonds. Transfection studies revealed that the variant mb-1 and B29 did not contribute to the BCR expression on cell surfaces. Although peripheral B cells contain small amounts of the variant mb-1 and B29 transcripts, treatment with an anti-IgM antibody, LPS or IL-4 induces a significant increase in amounts of the variant transcripts. These observations suggest that B-cell activation induces alternative splicing of mb-1 and B29 transcripts which encode proteins unable to constitute the BCR.
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