Department of Gastroenterological Surgery, Transplant and Surgical Oncology, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, Okayama, Japan.
Oncol Rep. 2010 Jun;23(6):1483-92. doi: 10.3892/or_00000787.
The HSP90 molecular chaperone family is highly conserved and expressed in various organisms ranging from prokaryotes to eukaryotes. HSP90 proteins play essential housekeeping functions, such as controlling the activity, turnover and trafficking of various proteins, promoting cell survival through maintaining the structural and functional integrity of some client proteins which control cell survival, proliferation and apoptosis, and play an important role in the progression of malignant disease. HSP90 proteins are ATP-dependent chaperones and the binding and hydrolysis of ATP are coupled to conformation changes of HSP90, which facilitate client protein folding and maturation. Many natural and synthetic molecular compounds have been proposed as promising cancer therapy via disrupting the formation of complex ATP-HSP90-client proteins.
HSP90 分子伴侣家族高度保守，存在于从原核生物到真核生物等各种生物体中。HSP90 蛋白具有重要的管家功能，如控制各种蛋白质的活性、周转率和运输，通过维持控制细胞存活、增殖和凋亡的某些客户蛋白的结构和功能完整性来促进细胞存活，并且在恶性疾病的进展中起着重要作用。HSP90 蛋白是 ATP 依赖性伴侣，ATP 的结合和水解与 HSP90 的构象变化偶联，这有利于客户蛋白的折叠和成熟。许多天然和合成的分子化合物已被提出作为有希望的癌症治疗方法，通过破坏复杂的 ATP-HSP90-客户蛋白的形成。
