B‐cell activation 2000
B‐cell activation 2000
复制标题
B细胞激活2000
DOI:
10.1034/j.1600-065x.2000.00620.x
复制
发表时间:
2000
影响因子:
8.7
通讯作者:
K. Tsukida
中科院分区:
文献类型:
--
作者:
K. Tsukida
As we stand on the edge of the genome era, research into how antibody production is regulated is both vital and diverse, as exemplified by the articles of this volume. Although we have achieved a considerable understanding of B-cell activation at the cellular and molecular level, there are many aspects of this problem that remain to be elucidated. This volume reviews much of our understanding in this area and highlights many of the current unknowns although, due to space constraints, there are many important contributors to this area whose thoughts on the topic could not be included. Moreover, related topics that have recently been covered by Immunological Reviews, such as the germinal center reaction and somatic mutation of immunoglobulin genes, have not been included. Here Ibriefly highlight just a few of the exciting findings and ideas that are presented in this volume.B-cell antigen receptor structure and function Central to the control of antibody production is the function of the B-cell antigen receptor (BCR), which is a complex between membrane immunoglobulin and one or more heterodimers of Ig-a and Ig-B. The latter components engage the signaling machinery of the cell to transmit information about antigen binding to the interior of the cell. For many years, the predominant hypothesis in the field has been that binding of oligova-lent or multivalent antigen to the BCR results in receptor clustering, which in turn activates the signaling reactions. How this would actually occur has not been demonstrated. One view is that Src-family tyrosine kinases are prebound to the BCR, such that receptor clustering brings the cytoplasmic tails of Ig-o and Ig-B, with their immunoreceptor tyrosine-based activation motifs (ITAMs), adjacent to tyrosine kinases bound to other receptors. This would promote phosphorylation of the ITAM tyrosines, which then serve as binding sites for another intra-