Department of Oncology- Pathology, Cancer Centre Karolinska (CCK), Karolinska University Hospital Solna, SE-171 76 Stockholm, Sweden.
Curr Med Chem. 2014;21(26):3042-7. doi: 10.2174/0929867321666140414100831.
Modern anti-cancer treatment involves targeted therapy that aims at inactivating particular oncoproteins or signaling pathways in a cancer-type-specific manner. A number of potent targeted therapies affecting oncogenic kinases or receptor tyrosine kinases have revolutionized anti-cancer treatment. These drugs inactivate signaling pathways that cancer cells depend on and therefore inhibit their proliferation and survival. Molecular chaperones of the Hsp90 family (heat shock protein 90) support the integrity, folding and function of many proteins involved in proliferation, survival, DNA damage and repair. Hsp90 proteins are thus required to maintain activity of a large variety of oncogenic proteins, including members of the JAK/STAT and the PI3K pathways. Accordingly cancer cells rely on Hsp90 proteins and their expression is often elevated in malignant cells. In line with this, inhibitors of Hsp90 (Hsp90-Is) have demonstrated potent antitumor activity in preclinical studies. While Hsp90-Is can be considered as targeted therapy, their broad effects on multiple signaling pathways make it difficult to predict the therapeutic outcome. Multiple myeloma (MM) is one of the tumor types with elevated Hsp90 levels. Hsp90-Is demonstrated promising activity in preclinical studies of MM and in several clinical trials. However, large variability in response questioned the use of Hsp90-Is as single drugs in the treatment of myeloma. A critical factor in targeted therapies, including Hsp90-Is, is identification of susceptible subgroups of patients. Predictive biomarkers in each particular tumor type are important in order to use anti-cancer drugs in a rational way. Interestingly, levels of Hsp90 expression has not proven to be decisive for treatment response and hence stratification of myeloma patients. Others and we have recently found that MM cells with an IL-6-activated JAK/STAT3 pathway are particularly sensitive to Hsp90-Is. In this review we will discuss these findings, both in terms of molecular mechanisms and applications for selection of MM patients amenable to Hsp90-I treatment in an individually targeted treatment strategy.
现代癌症治疗包括靶向治疗,旨在以癌症类型特异性的方式使特定的癌蛋白或信号通路失活。许多影响致癌激酶或受体酪氨酸激酶的有效的靶向治疗药物已经彻底改变了癌症治疗。这些药物使癌细胞依赖的信号通路失活,从而抑制其增殖和存活。Hsp90 家族(热休克蛋白 90)的分子伴侣支持许多参与增殖、存活、DNA 损伤和修复的蛋白质的完整性、折叠和功能。因此,Hsp90 蛋白对于维持多种致癌蛋白的活性是必需的,包括 JAK/STAT 和 PI3K 途径的成员。相应地,癌细胞依赖于 Hsp90 蛋白,并且其表达在恶性细胞中常常升高。与此一致,Hsp90 抑制剂(Hsp90-Is)在临床前研究中显示出强大的抗肿瘤活性。虽然 Hsp90-Is 可以被认为是一种靶向治疗方法,但它们对多种信号通路的广泛影响使得难以预测治疗效果。多发性骨髓瘤(MM)是 Hsp90 水平升高的肿瘤类型之一。Hsp90-Is 在 MM 的临床前研究和几项临床试验中显示出有前途的活性。然而,反应的巨大差异使人们对 Hsp90-Is 作为单一药物治疗骨髓瘤的使用产生了质疑。包括 Hsp90-Is 在内的靶向治疗的一个关键因素是鉴定易感性患者亚组。在每种特定肿瘤类型中,预测性生物标志物对于合理使用抗癌药物非常重要。有趣的是,Hsp90 表达水平对于治疗反应并没有证明是决定性的,因此不能对骨髓瘤患者进行分层。最近我们和其他人发现,具有 IL-6 激活的 JAK/STAT3 途径的 MM 细胞对 Hsp90-Is 特别敏感。在这篇综述中,我们将讨论这些发现,包括分子机制和应用,以选择适合 Hsp90-I 治疗的 MM 患者,以实现个体化靶向治疗策略。