DIFFERENTIAL SIGNALING THROUGH THE IG-ALPHA AND IG-BETA COMPONENTS OF THE B-CELL ANTIGEN RECEPTOR
DIFFERENTIAL SIGNALING THROUGH THE IG-ALPHA AND IG-BETA COMPONENTS OF THE B-CELL ANTIGEN RECEPTOR
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DOI:
10.1002/eji.1830230422
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发表时间:
1993-04-01
影响因子:
5.4
通讯作者:
RETH, M
中科院分区:
文献类型:
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作者:
KIM, KM;ALBER, G;RETH, M
The B cell antigen receptor is a complex containing the antigen-binding immunoglobulin molecules and the Ig-alpha/Ig-beta heterodimer which presumably connects the B cell antigen receptor to intracellular signaling components. To analyze the functional properties of the cytoplasmic parts of the B cell antigen receptor. we used the K46 B lymphoma line (IgG2a, chi) to express chimeric molecules composed of the extracellular and transmembrane part of the CD8alpha molecule and the cytoplasmic sequence of either the Ig-alpha (CD8alpha/Ig-alpha), the Ig-beta (CD8alpha/Ig-beta) protein or the membrane-bound gamma2a heavy chain (CD8alpha/gamma2a). From these three types of chimeric molecules only CD8alpha/Ig-alpha and CD8alpha/Ig-beta, but not CD8alpha/gamma2a, could transduce signals. thus providing the first evidence that the cytoplasmic tail of Ig-alpha and Ig-beta have a signaling capacity. After cross-linking with anti-CD8alpha antibodies, both molecules induced a similar increase in intracellular free calcium ion and in MAP kinase phosphorylation. Protein tyrosine kinases, however. were strongly activated via the CD8alpha/Ig-alpha and only marginally via the CD8alpha/Ig-beta molecule. This suggests that the Ig-alpha and Ig-beta proteins have distinct roles during signal transduction through the B cell antigen receptor.