Campbell M A, Sefton B M
Molecular Biology and Virology Laboratory, Salk Institute, San Diego, California 92186-5800.
Mol Cell Biol. 1992 May;12(5):2315-21. doi: 10.1128/mcb.12.5.2315-2321.1992.
Treatment of B lymphocytes with antibodies to membrane immunoglobulin (Ig) stimulates protein tyrosine phosphorylation. We have examined the phosphorylation in vitro of proteins associated with membrane Ig. The Src family protein tyrosine kinases p53/56lyn, p59fyn, and p56lck are associated with membrane Ig in spleen B cells and B-cell lines and undergo phosphorylation in vitro. The pattern of expression of Src family protein tyrosine kinases in B cells varied. Our studies suggest that multiple kinases can potentially interact with membrane Ig and that within any one B-cell type, all of the Src family kinases expressed can be found in association with membrane Ig. We also observed that the Ig-associated Ig alpha protein, multiple forms of Ig beta, and proteins of 100 and 25 kDa were tyrosine phosphorylated in vitro. The 100- and 25-kDa proteins remain unidentified.
用抗膜免疫球蛋白（Ig）抗体处理B淋巴细胞可刺激蛋白酪氨酸磷酸化。我们已经检测了与膜Ig相关的蛋白质在体外的磷酸化情况。Src家族蛋白酪氨酸激酶p53/56lyn、p59fyn和p56lck与脾B细胞和B细胞系中的膜Ig相关，并在体外发生磷酸化。Src家族蛋白酪氨酸激酶在B细胞中的表达模式各不相同。我们的研究表明，多种激酶可能与膜Ig相互作用，并且在任何一种B细胞类型中，所有表达的Src家族激酶都可以与膜Ig结合。我们还观察到，与Ig相关的Igα蛋白、多种形式的Igβ以及100 kDa和25 kDa的蛋白质在体外发生了酪氨酸磷酸化。100 kDa和25 kDa的蛋白质身份尚未确定。
