Jazirehi Ali R, Bonavida Benjamin
Department of Microbiology, Immunology and Molecular Genetics, Jonsson Comprehensive Cancer Center, David Geffen School of Medicine at UCLA, University of California, Los Angeles, CA 90095-1747, USA.
Oncogene. 2005 Mar 24;24(13):2121-43. doi: 10.1038/sj.onc.1208349.
The clinical application of rituximab (chimeric mouse anti-human CD20 mAb, Rituxan, IDEC-C2B8), alone and/or combined with chemotherapy, has significantly ameliorated the treatment outcome of patients with relapsed and refractory low-grade or follicular non-Hodgkin's lymphoma (NHL). The exact in vivo mechanisms of action of rituximab are not fully understood, although antibody-dependent cell-mediated cytotoxicity (ADCC), complement-dependent cytotoxicity (CDC), and apoptosis have been suggested. We have proposed that modifications of the cellular signaling pathways by rituximab may be crucial for its clinical response. The B-cell restricted cell surface phosphoprotein CD20 is involved in many cellular signaling events including proliferation, activation, differentiation, and apoptosis upon crosslinking. Monomeric rituximab chemosensitizes drug-resistant NHL cells via selective downregulation of antiapoptotic factors through the type II mitochondrial apoptotic pathway. Several signaling pathways are affected by rituximab which are implicated in the underlying molecular mechanisms of chemosensitization. ARL (acquired immunodeficiency syndrome (AIDS)-related lymphoma) and non-ARL cell lines have been examined as in vitro model systems. In ARL, rituximab diminishes the activity of the p38MAPK signaling pathway resulting in inhibition of the interleukin (IL)-10/IL-10R autocrine/paracrine cytokine autoregulatory loop leading to the inhibition of constitutive STAT-3 activity and subsequent downregulation of Bcl-2 expression leading to chemosensitization. Rituximab upregulates Raf-1 kinase inhibitor protein (RKIP) expression in non-ARL cells. Through physical association with Raf-1 and nuclear factor kappaB (NF-kappa B)-inducing kinase (NIK), RKIP negatively regulates two major survival pathways, namely, the extracellular signal-regulated kinase1/2 (ERK1/2) and the NF-kappa B pathways, respectively. Downmodulation of the ERK1/2 and NF-kappa B pathways inhibits the transcriptional activity of AP-1 and NF-kappa B transcription factors, respectively, both of which lead to the downregulation of Bcl-(xL) (Bcl-2 related gene (long alternatively spliced variant of Bcl-x gene)) transcription and expression and sensitization to drug-induced apoptosis. Bcl-(xL)-overexpressing cells corroborated the pivotal role of Bcl-(xL) in chemosensitization. The specificity of rituximab-mediated signaling and functional effects were corroborated by the use of specific pharmacological inhibitors. Many patients do not respond and/or relapse and the mechanisms of unresponsiveness are unknown. Rituximab-resistant B-NHL clones were generated to investigate the acquired resistance to rituximab-mediated signaling, and chemosensitization. Resistant clones display different phenotypic, genetic and functional properties compared to wild-type cells. This review summarizes the data highlighting a novel role of rituximab as a signal-inducing antibody and as a chemosensitizing agent through negative regulation of major survival pathways. Studies presented herein also reveal several intracellular targets modified by rituximab, which can be exploited for therapeutic and prognostic purposes in the treatment of patients with rituximab- and drug-refractory NHL.
利妥昔单抗(嵌合鼠抗人CD20单克隆抗体,美罗华,IDEC-C2B8)单独和/或联合化疗的临床应用,显著改善了复发难治性低度或滤泡性非霍奇金淋巴瘤(NHL)患者的治疗效果。尽管有人提出抗体依赖性细胞介导的细胞毒性(ADCC)、补体依赖性细胞毒性(CDC)和凋亡是利妥昔单抗确切的体内作用机制,但其确切机制尚未完全明确。我们提出,利妥昔单抗对细胞信号通路的修饰可能对其临床反应至关重要。B细胞限制性细胞表面磷蛋白CD20参与许多细胞信号事件,包括交联后的增殖、激活、分化和凋亡。单体利妥昔单抗通过II型线粒体凋亡途径选择性下调抗凋亡因子,使耐药NHL细胞对化疗药物敏感。利妥昔单抗影响了几条信号通路,这些通路与化疗增敏的潜在分子机制有关。已将获得性免疫缺陷综合征(AIDS)相关淋巴瘤(ARL)和非ARL细胞系作为体外模型系统进行研究。在ARL中,利妥昔单抗降低p38丝裂原活化蛋白激酶(p38MAPK)信号通路的活性,导致白细胞介素(IL)-10/IL-10R自分泌/旁分泌细胞因子自调节环受到抑制,从而抑制组成型信号转导和转录激活因子3(STAT-3)的活性,随后下调Bcl-2表达,导致化疗增敏。利妥昔单抗上调非ARL细胞中Raf-1激酶抑制蛋白(RKIP)的表达。通过与Raf-1和核因子κB(NF-κB)诱导激酶(NIK)的物理结合,RKIP分别对两条主要的生存通路,即细胞外信号调节激酶1/2(ERK1/2)和NF-κB通路进行负调控。ERK1/2和NF-κB通路的下调分别抑制了活化蛋白-1(AP-1)和NF-κB转录因子的转录活性,二者均导致Bcl-(xL)(Bcl-2相关基因(Bcl-x基因的长可变剪接变体))转录和表达下调,并使细胞对药物诱导的凋亡敏感。过表达Bcl-(xL)的细胞证实了Bcl-(xL)在化疗增敏中的关键作用。使用特异性药理抑制剂证实了利妥昔单抗介导的信号传导和功能效应的特异性。许多患者无反应和/或复发,且无反应机制尚不清楚。为了研究对利妥昔单抗介导的信号传导和化疗增敏的获得性耐药,构建了利妥昔单抗耐药的B-NHL克隆。与野生型细胞相比,耐药克隆表现出不同的表型、遗传和功能特性。本综述总结了相关数据,突出了利妥昔单抗作为信号诱导抗体以及通过对主要生存通路的负调控作为化疗增敏剂的新作用。本文介绍的研究还揭示了利妥昔单抗修饰的几个细胞内靶点,这些靶点可用于利妥昔单抗和药物难治性NHL患者治疗的治疗和预后目的。