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首页> 外文期刊>The Journal of Immunology: Official Journal of the American Association of Immunologists >Uncoupling activation-dependent HS1 phosphorylation from nuclear factor of activated T cells transcriptional activation in Jurkat T cells: differential signaling through CD3 and the costimulatory receptors CD2 and CD28.
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Uncoupling activation-dependent HS1 phosphorylation from nuclear factor of activated T cells transcriptional activation in Jurkat T cells: differential signaling through CD3 and the costimulatory receptors CD2 and CD28.

机译：从Jurkat T细胞中活化的T细胞转录活化的核因子中解偶联活化依赖性HS1磷酸化：通过CD3和共刺激受体CD2和CD28的差异信号传导。

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摘要

CD3, CD2, and CD28 are functionally distinct receptors on T lymphocytes. Engagement of any of these receptors induces the rapid tyrosine phosphorylation of a shared group of intracellular signaling proteins, including Vav, Cbl, p85 phosphoinositide 3-kinase, and the Src family kinases Lck and Fyn. Ligation of CD3 also induces the tyrosine phosphorylation of HS1, a 75-kDa hematopoietic cell-specific intracellular signaling protein of unknown function. We have examined changes in HS1 phosphorylation after differential stimulation of CD3, CD2, and CD28 to elucidate its role in T cells and to further delineate the signaling pathways recruited by these receptors. Unlike ligation of CD3, stimulation with anti-CD28 mAb or CHO cells expressing the CD28 ligands CD80 or CD86 did not lead to tyrosine phosphorylation of HS1 in Jurkat T cells. Additionally, no tyrosine phosphorylation of HS1 was induced by mitogenic pairs of anti-CD2 mAbs capable of activating the transcription factor NFAT (nuclear factor of activated T cells). Costimulation through CD28 and/or CD2 did not modulate the CD3-dependent phosphorylation of HS1. In vivo studies indicated that CD3-induced HSI phosphorylation was dependent upon both the Src family tyrosine kinase Lck and the tyrosine phosphatase CD45, did not require MEK1 kinase activity, and was regulated by protein kinase C activation. Thus, although CD3, CD28, and CD2 activate many of the same signaling molecules, they differed in their capacity to induce the tyrosine phosphorylation of HSI. Furthermore, activation-dependent tyrosine phosphorylation of HS1 was not required for NFAT transcriptional activation.
机译：CD3，CD2和CD28是T淋巴细胞上功能不同的受体。这些受体中任何一个的参与都会诱导一组共享的细胞内信号蛋白（包括Vav，Cbl，p85磷酸肌醇3激酶以及Src家族激酶Lck和Fyn）的酪氨酸快速磷酸化。 CD3的连接还诱导HS1的酪氨酸磷酸化，HS1是一种功能未知的75 kDa造血细胞特异性细胞内信号转导蛋白。我们已经研究了CD3，CD2和CD28的差异刺激后HS1磷酸化的变化，以阐明其在T细胞中的作用，并进一步描绘了这些受体募集的信号通路。与CD3的连接不同，表达CD28配体CD80或CD86的抗CD28 mAb或CHO细胞刺激不会导致Jurkat T细胞中HS1的酪氨酸磷酸化。此外，能够激活转录因子NFAT（活化T细胞的核因子）的抗CD2 mAb的促有丝分裂对不会诱导HS1的酪氨酸磷酸化。通过CD28和/或CD2的共刺激作用不能调节HS1的CD3依赖性磷酸化。体内研究表明，CD3诱导的HSI磷酸化既依赖于Src家族的酪氨酸激酶Lck，也依赖于酪氨酸磷酸酶CD45，不需要MEK1激酶活性，并且受蛋白激酶C激活的调节。因此，尽管CD3，CD28和CD2激活许多相同的信号分子，但它们诱导HSI酪氨酸磷酸化的能力不同。此外，NFAT转录激活不需要HS1的激活依赖性酪氨酸磷酸化。

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