TYROSINE PHOSPHORYLATION OF CD22 DURING B-CELL ACTIVATION
TYROSINE PHOSPHORYLATION OF CD22 DURING B-CELL ACTIVATION
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DOI：
10.1126/science.1279802
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发表时间：
1992-11-06
期刊：
影响因子：
56.9
通讯作者：
SEFTON, BM
中科院分区：
文献类型：
--
作者：
SCHULTE, RJ;CAMPBELL, MA;SEFTON, BM
B 细胞上抗原受体的连接诱导许多细胞蛋白上酪氨酸的快速磷酸化。生成了可识别活化 B 细胞中存在的酪氨酸磷酸化细胞表面蛋白的单克隆抗体。氨基酸序列分析表明，这个 140 千道尔顿的蛋白质是 CD22，一种 B 细胞特异性细胞表面糖蛋白，也是蛋白质酪氨酸磷酸酶 CD45 的假定细胞外配体。 CD22 的酪氨酸磷酸化可能在 B 细胞信号转导中很重要，可能是通过调节活化 B 细胞的粘附性来实现的。
Ligation of the antigen receptor on B cells induces the rapid phosphorylation of tyrosine on a number of cellular proteins. A monoclonal antibody that recognized a tyrosine-phosphorylated cell surface protein that was present in activated B cells was generated. Amino acid sequence analysis showed that this 140-kilodalton protein was CD22, a B cell-specific cell surface glycoprotein and putative extracellular ligand of the protein tyrosine phosphatase CD45. Tyrosine phosphorylation of CD22 may be important in B cell signal transduction, possibly through regulation of the adhesiveness of activated B cells.