Coassociation of CD26 (dipeptidyl peptidase IV) with CD45 on the surface of human T lymphocytes.
Coassociation of CD26 (dipeptidyl peptidase IV) with CD45 on the surface of human T lymphocytes.
复制标题
DOI：
10.4049/jimmunol.147.8.2514
复制
发表时间：
1991-10
影响因子：
4.4
通讯作者：
Y. Torimoto;N. Dang;É. Vivier;T. Tanaka;S. Schlossman;C. Morimoto
中科院分区：
文献类型：
--
作者：
Y. Torimoto;N. Dang;É. Vivier;T. Tanaka;S. Schlossman;C. Morimoto
在本报告中，我们证明了抗CD26（1F7）诱导的T细胞表面CD26的调节导致CD3 zeta酪氨酸残基的磷酸化增强和CD4相关p56lck酪氨酸激酶活性增加。我们进一步表明，CD26与CD45（一种已知的膜连接蛋白酪氨酸磷酸酶）在T细胞表面共调节，并且抗CD26能够从T细胞裂解物中沉淀CD45。这些发现有力地表明，CD26可能与T细胞表面上的CD45蛋白酪氨酸磷酸酶密切相关，并进一步支持CD26与CD45的相互作用导致增强的酪氨酸激酶活性、zeta链磷酸化和T细胞活化的观点。
In the present report, we demonstrated that modulation of CD26 from T cell surface induced by antiCD26 (1F7) led to enhanced phosphorylation of CD3 zeta tyrosine residues and increased CD4 associated p56lck tyrosine kinase activity. We further showed that CD26 was comodulated on the T cell surface with CD45, a known membrane-linked protein tyrosine phosphatase and that anti-CD26 was capable of precipitating CD45 from T cell lysates. These findings strongly suggest that CD26 may be closely associated with the CD45 protein tyrosine phosphatase on T cell surface and further support the notion that the interaction of CD26 with CD45 results in enhanced tyrosine kinase activity, zeta chain phosphorylation, and T cell activation.