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布鲁顿酪氨酸激酶在前B淋巴细胞和受体连接的B细胞中发生酪氨酸磷酸化并被激活。

Bruton tyrosine kinase is tyrosine phosphorylated and activated in pre-B lymphocytes and receptor-ligated B cells.

作者信息

Aoki Y, Isselbacher K J, Pillai S

机构信息

Massachusetts General Hospital Cancer Center, Boston 02129.

出版信息

Proc Natl Acad Sci U S A. 1994 Oct 25;91(22):10606-9. doi: 10.1073/pnas.91.22.10606.

Abstract

The gene encoding Bruton tyrosine kinase (Btk) is known to be mutated in human X chromosome-linked agammaglobulinemia and in the Xid mouse. This kinase was examined in B lymphocytes before and after antigen receptor ligation and also in pre-B cells. Btk was found to be catalytically activated and tyrosine phosphorylated in response to anti-IgM stimulation in B cells. This kinase is also constitutively phosphorylated on tyrosine residues in pre-B cells. These findings point to a functional role for Btk in pre-antigen and antigen receptor signaling during B-cell development and provide a biochemical explanation for the X-linked genetic syndromes already linked to this kinase.

摘要

已知编码布鲁顿酪氨酸激酶(Btk)的基因在人类X染色体连锁无丙种球蛋白血症和Xid小鼠中发生突变。在抗原受体连接前后的B淋巴细胞以及前B细胞中对该激酶进行了检测。结果发现,Btk在B细胞中响应抗IgM刺激而被催化激活并发生酪氨酸磷酸化。该激酶在前B细胞中也在酪氨酸残基上组成性磷酸化。这些发现表明Btk在B细胞发育过程中的抗原前和抗原受体信号传导中发挥功能性作用,并为已经与该激酶相关的X连锁遗传综合征提供了生化解释。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d166/45070/a1d6a1fe170f/pnas01144-0374-a.jpg

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