Gabay C, Smith M F, Eidlen D, Arend W P
Division of Rheumatology, Department of Medicine, University of Colorado Health Sciences Center, Denver, Colorado 80262, USA.
J Clin Invest. 1997 Jun 15;99(12):2930-40. doi: 10.1172/JCI119488.
Interleukin 1 receptor antagonist (IL-1Ra) levels are elevated in the blood of patients with a variety of infectious, immune, or traumatic conditions. To examine whether IL1Ra is produced by liver cells with characteristics resembling an acute-phase protein, human primary hepatocytes isolated from liver biopsies and HepG2 hepatoma cells were stimulated with IL-1beta, IL-6, and TNFalpha. IL-1Ra was present in the supernatants of both cells, with production significantly enhanced by IL-1beta, and by the combination of IL-1beta and IL-6. The term IL-1Ra refers to two different proteins encoded by the same gene, but generated by alternative splicing of two different first exons. One isoform is secreted (17-kD sIL-1Ra), and the other isoform remains in the cytoplasm (18-kD icIL-1Ra). By Western blot analysis, the supernatants of human hepatoma (HepG2) cells contained only sIL-1Ra, whereas the lysates contained a novel smaller molecular mass isoform of 16 kD. RT-PCR and ribonuclease protection assay with RNA from HepG2 cells showed that only sIL-1Ra mRNA was expressed, and confirmed the inducing effect of IL-1beta and IL-6. Transfection studies were performed using constructs containing the promoters of either sIL-1Ra or icIL-1Ra coupled to the luciferase reporter gene. The sIL-1Ra promoter was active in HepG2 cells stimulated by IL-1beta and/or IL-6, whereas the icIL-1Ra promoter was inactive. Mutation of binding sites for transcription factors NF-kappaB and/or C/EBP within the proximal sIL-1Ra promoter led to significant decreases in response to IL-1beta and IL-6 in comparison to the wild-type promoter. Electromobility gel shift assays confirmed the presence of NF-kappaB and C/EBP binding sites within the sIL-1Ra promoter, and indicated a significant increase in the binding activities of nuclear proteins from HepG2 cells treated with IL-1beta and IL-6. In summary, sIL-1Ra, but not icIL-1Ra, is produced by hepatocytes, and is regulated by proinflammatory cytokines as an acute-phase protein. In addition, NF-kappaB and C/EBP family members are likely to play important roles in the full expression of IL-1Ra by hepatocytes during inflammatory conditions.
在患有各种感染、免疫或创伤性疾病的患者血液中,白细胞介素1受体拮抗剂(IL-1Ra)水平会升高。为了研究IL-1Ra是否由具有类似急性期蛋白特征的肝细胞产生,用IL-1β、IL-6和TNFα刺激从肝活检中分离出的人原代肝细胞和HepG2肝癌细胞。两种细胞的上清液中均存在IL-1Ra,IL-1β以及IL-1β与IL-6的组合可显著增强其产生。术语IL-1Ra指由同一基因编码但通过两种不同的第一个外显子的可变剪接产生的两种不同蛋白质。一种异构体是分泌型(17-kD sIL-1Ra),另一种异构体保留在细胞质中(18-kD icIL-1Ra)。通过蛋白质印迹分析,人肝癌(HepG2)细胞的上清液中仅含有sIL-1Ra,而裂解物中含有一种新的16 kD较小分子量异构体。用HepG2细胞的RNA进行逆转录聚合酶链反应(RT-PCR)和核糖核酸酶保护试验表明仅表达sIL-1Ra mRNA,并证实了IL-1β和IL-6的诱导作用。使用含有与荧光素酶报告基因偶联的sIL-1Ra或icIL-1Ra启动子的构建体进行转染研究。sIL-1Ra启动子在受到IL-1β和/或IL-6刺激的HepG2细胞中具有活性,而icIL-1Ra启动子无活性。与野生型启动子相比,近端sIL-1Ra启动子中转录因子NF-κB和/或C/EBP结合位点的突变导致对IL-1β和IL-6的反应显著降低。电泳迁移率凝胶移位分析证实了sIL-1Ra启动子内存在NF-κB和C/EBP结合位点,并表明用IL-1β和IL-6处理的HepG2细胞核蛋白的结合活性显著增加。总之,肝细胞产生sIL-1Ra而非icIL-1Ra,并且作为急性期蛋白受促炎细胞因子调节。此外,NF-κB和C/EBP家族成员可能在炎症条件下肝细胞对IL-1Ra的充分表达中起重要作用。