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• W492788421 abstract "B-chronic lymphocytic leukemia (B-CLL) is an accumulative disease of resting CD5+ B lymphocytes that present a number of distinctive features including the expression of faint to virtually undetectable amounts of monoclonal surface immunoglobulins (sIg), an unusual kinetic hyporesponsiveness, an extended cell survival due to defective apoptosis and a failure to present soluble and allo antigens (1). It is conceivable that abnormalities of the B cell receptor (BCR) may play a prominent role in causing these functional anomalies. The BCR of mature B cells is a multimeric complex formed by the slg homodimer and the noncovalently bound heterodimer Igα/Igß (CD79a/CD79b) encoded by the mb-1 and the B29 genes (2,3). CD79a and CD79b have an extracellular part that forms an Ig-like domain and binds to slg, a transmembrane and a cytoplasmic domain (4). The heterodimer, which is both essential and sufficient for Ig to reach the membrane (2–5), is the signal transducing unit of the BCR (6–8). CD79a and CD79b function synergistically to induce the apoptosis mediated via the BCR (9), influence Ag internalization and increase the efficiency of Ag presentation (10). RNA truncated forms (ΔCD79a and ΔCD79b) which arise by alternative splicing have been described in a variety of human B cells and B cell lines (11,12). ΔCD79a lacks a portion of the extracellular domain encoded by exon 2(13) and ΔCD79b lacks the entire extracellular Ig-like domain encoded by exon 3(11)." @default.
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• W492788421 date "1999-01-01" @default.
• W492788421 modified "2023-10-16" @default.
• W492788421 title "Alternative Splicing of CD79a (Igα) and CD79b (Igß Transcripts in Human B-CLL Cells" @default.
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• W492788421 doi "https://doi.org/10.1007/978-3-642-60162-0_30" @default.
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