Rapamycin inhibits the phosphorylation of p70 S6 kinase in IL-2 and mitogen-activated human T cells.
Rapamycin inhibits the phosphorylation of p70 S6 kinase in IL-2 and mitogen-activated human T cells.
复制标题
Rapamycin 抑制 IL-2 和丝裂原激活的人 T 细胞中 p70 S6 激酶的磷酸化。
DOI：
10.1016/s0006-291x(05)81549-9
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发表时间：
1992
影响因子：
3.1
通讯作者：
Gelfand,EW
中科院分区：
文献类型：
--
作者：
Terada,N;Lucas,JJ;Szepesi,A;Franklin,RA;Takase,K;Gelfand,EW
40S核糖体蛋白S6的磷酸化部分受丝裂原激活的p70S6激酶(P70S6K)的调节。在依赖IL-2的人细胞系Kit225中加入IL-2，或激活静止的人T细胞后，免疫印迹法观察到p70s6k的快速磷酸化。雷帕霉素(RAP)是一种有效的T细胞增殖反应的抑制物，可显著抑制IL-2或加入静止T细胞的有丝分裂原诱导的p70s6的磷酸化。其他免疫抑制剂如环孢素A或FK506类似物无效。此外，RAP的作用仅限于p70S6K；它不抑制p90rsk的磷酸化，p90rsk是另一种利用S6蛋白作为底物的激酶。这些数据首次表明，在人类T细胞增殖过程中，RAP可能针对导致p70s6k磷酸化的途径。
Phosphorylation of 40S ribosomal protein S6 is regulated in part by the mitogen-activated p70 S6 kinase (p70s6k). Following the addition of IL-2 to the IL-2 dependent human cell line Kit225, or mitogenic activation of resting human T cells, a rapid phosphorylation of p70s6kwas observed by immunoblotting. Rapamycin (RAP), a potent suppressor of T-cell proliferative responses, markedly inhibited the phosphorylation of p70s6kinduced by IL-2 in Kit225 cells or by the mitogens added to resting T cells. Other immunosuppressants such as cyclosporin A or an FK506 analogue were without effect. Moreover, the effect of RAP was restricted to p70s6k; it did not inhibit the phosphorylation of p90rsk, another kinase which utilizes the S6 protein as a substrate. These data indicate for the first time that RAP may target the pathway leading to p70s6kphosphorylation during human T-cell proliferation.