Cabaud-Gibouin Vincent, Durand Manon, Quéré Ronan, Girodon François, Garrido Carmen, Jego Gaëtan
INSERM, UMR1231, Université de Bourgogne, 21078 Dijon, France.
Service d'Hématologie Biologique, Hôpital Universitaire François Mitterrand, 21000 Dijon, France.
Cancers (Basel). 2023 Feb 3;15(3):984. doi: 10.3390/cancers15030984.
Heat-shock proteins (HSPs) are powerful chaperones that provide support for cellular functions under stress conditions but also for the homeostasis of basic cellular machinery. All cancer cells strongly rely on HSPs, as they must continuously adapt to internal but also microenvironmental stresses to survive. In solid tumors, HSPs have been described as helping to correct the folding of misfolded proteins, sustain oncogenic pathways, and prevent apoptosis. Leukemias and lymphomas also overexpress HSPs, which are frequently associated with resistance to therapy. HSPs have therefore been proposed as new therapeutic targets. Given the specific biology of hematological malignancies, it is essential to revise their role in this field, providing a more adaptable and comprehensive picture that would help design future clinical trials. To that end, this review will describe the different pathways and functions regulated by HSP27, HSP70, HSP90, and, not least, HSP110 in leukemias and lymphomas.
热休克蛋白（HSPs）是强大的伴侣蛋白，在应激条件下为细胞功能提供支持，同时也维持基本细胞机制的稳态。所有癌细胞都高度依赖热休克蛋白，因为它们必须不断适应内部以及微环境应激才能存活。在实体瘤中，热休克蛋白被认为有助于纠正错误折叠蛋白的折叠、维持致癌途径并防止细胞凋亡。白血病和淋巴瘤也过度表达热休克蛋白，这通常与治疗耐药性相关。因此，热休克蛋白已被提议作为新的治疗靶点。鉴于血液系统恶性肿瘤的特殊生物学特性，有必要重新审视它们在该领域的作用，提供一幅更具适应性和全面性的图景，以帮助设计未来的临床试验。为此，本综述将描述热休克蛋白27、热休克蛋白70、热休克蛋白90，尤其是热休克蛋白110在白血病和淋巴瘤中所调节的不同途径和功能。
