Asao H, Takeshita T, Nakamura M, Nagata K, Sugamura K
Department of Microbiology, Tohoku University School of Medicine, Sendai, Japan.
J Exp Med. 1990 Mar 1;171(3):637-44. doi: 10.1084/jem.171.3.637.
We have recently established a mAb named TU11 mAb specific for the p75 subunit of human IL-2 receptor (IL-2R). The present study using TU11 mAb demonstrates the IL-2-induced phosphorylation of IL-2Rp75 on tyrosine residues in IL-2-dependent T cells. The tyrosine phosphorylation is mediated by the high affinity IL-2R, correlates with the IL-2-induced cell growth, and rapidly increases during the first 5 min of IL-2 stimulation. Phosphorylation of serine and threonine residues of IL-2Rp75 is also detected, but its IL-2 dependency is not significant during at least the first 5 min. These results suggest some roles of a tyrosine kinase associated with IL-2Rp75 in the IL-2-induced signal-transducing pathway.
我们最近制备了一种名为TU11单克隆抗体(mAb),它对人白细胞介素2受体(IL-2R)的p75亚基具有特异性。本研究使用TU11单克隆抗体证明了在IL-2依赖的T细胞中,IL-2可诱导IL-2Rp75的酪氨酸残基发生磷酸化。酪氨酸磷酸化由高亲和力IL-2R介导,与IL-2诱导的细胞生长相关,并在IL-2刺激的最初5分钟内迅速增加。还检测到IL-2Rp75丝氨酸和苏氨酸残基的磷酸化,但至少在最初5分钟内其对IL-2的依赖性不显著。这些结果表明与IL-2Rp75相关的酪氨酸激酶在IL-2诱导的信号转导途径中发挥了一些作用。