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热休克蛋白90(heat shock protein90,Hsp90)在机体内作为分子伴侣,参与蛋白质的折叠、移位、修复和降解,通过与辅伴侣分子形成超级陪伴装置以调节依附蛋白的生物学活性。近年来研究表明很多癌基因蛋白均为Hsp90的作用靶点,因此抑制Hsp90的功能将促进这些癌基因蛋白的降解,有助于肿瘤的治疗。将Hsp90抑制剂用于白血病治疗的研究,其中格尔德霉素(GA)和17-烯丙胺17-脱甲氧格尔德霉素(17-AAG)可诱导肿瘤细胞凋亡,并能增加其他抗肿瘤药的敏感性。
Heat shock protein 90 (Hsp90), as a chaperone in the body, is involved in the folding, shifting, repairing and degradation of proteins and regulates the biological activity of the adherent protein by forming a super companion device with the partner molecules. In recent years, studies have shown that many oncoproteins are the target of Hsp90, thus inhibiting the function of Hsp90 will promote the degradation of these oncogenes and contribute to the treatment of tumors. Hsp90 inhibitors are used in the research of leukemia treatment, in which geldanamycin (GA) and 17-allylamine 17-demethoxygeldanamycin (17-AAG) can induce tumor cell apoptosis and increase Other anti-cancer drug sensitivity.