Merétey K, Falus A, Taga T, Kishimoto T
Dept. of Immunology, National Institute of Rheumatology and Physiotherapy, Budapest, Hungary.
Agents Actions. 1991 May;33(1-2):189-91. doi: 10.1007/BF01993163.
Based on our earlier data on the enhancing effect of histamine on the action of interleukin-6 (IL-6), we have studied the molecular mechanisms of these interactions. The effect of histamine was investigated on the binding of 125I-IL-6 by B lymphoma cell line CESS, monocytoid cell line U937 and hepatoma cell line HepG2. Histamine increases the IL-6 binding by CESS cells and inhibits that by U937 and HepG2 cells. Using H1 receptor (cetirizin and loderix) and H2 receptor (cimetidine and ranitidine) specific antagonists, an H1-dependent stimulation of IL-6 binding by CESS cells was found. In contrast, down-regulation of IL-6 binding by histamine was clearly mediated through H2 receptors. On U937 cells, using a monoclonal antibody reacting with the 80 kd chain of the human IL-6 receptor, and H2-receptor mediated inhibition of IL-6 receptor expression was found by FACS analysis.
基于我们早期关于组胺对白细胞介素-6(IL-6)作用的增强效应的数据,我们研究了这些相互作用的分子机制。研究了组胺对B淋巴瘤细胞系CESS、单核细胞样细胞系U937和肝癌细胞系HepG2结合125I-IL-6的影响。组胺增加了CESS细胞对IL-6的结合,并抑制了U937和HepG2细胞对IL-6的结合。使用H1受体(西替利嗪和氯雷他定)和H2受体(西咪替丁和雷尼替丁)特异性拮抗剂,发现CESS细胞对IL-6结合的刺激依赖于H1。相反,组胺对IL-6结合的下调明显是通过H2受体介导的。在U937细胞上,使用与人IL-6受体80kd链反应的单克隆抗体,通过流式细胞术分析发现H2受体介导的IL-6受体表达受到抑制。