Martin M, Brigelius-Flohé R, Resch K
Institut für Molekularpharmakologie, Medizinische Hochschule Hannover, Germany.
Behring Inst Mitt. 1995 Jun(96):32-44.
A novel serine/threonine specific protein kinase was found to be associated with the type I IL-1 receptor in the murine T cell lines D10N and EL-4. This kinase was identified in immunoprecipitates from IL-1 stimulated T-cells by its ability to phosphorylate exogenous substrates in the presence of radiolabeled ATP. An endogenous protein, most likely a member of the IL-1 R1 complex, was also phosphorylated. The activation of the kinase is specific for IL-1, neither TNF nor phorbol esters were able to activate the IL-1 RI associated kinase activity. The IL-1 receptor antagonist had no intrinsic activity and inhibited the activation of the kinase. The activation of the kinase was rapid and detectable after 30 seconds of IL-1 stimulation. A minimal model of the IL-RI signal transduction complex is discussed, presenting this novel serine/threonine kinase as a constituent of the complex.
在小鼠T细胞系D10N和EL-4中，发现一种新型丝氨酸/苏氨酸特异性蛋白激酶与I型白细胞介素-1受体（IL-1R）相关。通过其在放射性标记的ATP存在下磷酸化外源底物的能力，在IL-1刺激的T细胞免疫沉淀中鉴定出这种激酶。一种内源性蛋白（很可能是IL-1R1复合物的成员）也被磷酸化。该激酶的激活对IL-1具有特异性，肿瘤坏死因子（TNF）和佛波酯均不能激活与IL-1RI相关的激酶活性。IL-1受体拮抗剂没有内在活性，并抑制该激酶的激活。IL-1刺激30秒后，该激酶的激活迅速且可检测到。文中讨论了IL-RI信号转导复合物的一个简化模型，将这种新型丝氨酸/苏氨酸激酶作为该复合物的一个组成部分。
