Gobbo Jessica, Gaucher-Di-Stasio Caroline, Weidmann Stéphanie, Guzzo Jean, Garrido Carmen
Faculty of Medicine and Pharmacy, INSERM, U-866, Dijon, France.
Methods Mol Biol. 2011;787:137-43. doi: 10.1007/978-1-61779-295-3_11.
Stress-inducible heat-shock proteins (HSPs, like HSP70 and HSP27) are molecular chaperones that -protect cells from stress damage by keeping cellular proteins in a folding competent state and preventing them from irreversible aggregation. HSP27 and HSP70 chaperone activities are useful indicators to test chemical products and physical stress impact on protein denaturation, to select HSP inhibitors, or to -determine the implication of the chaperone function in other HSP activities, such as apoptosis. We have developed two simple and fast chaperone activity tests for HSP27 and HSP70 that we initially set up to test the effect of potential HSP inhibitors obtained after screening of chemical and small molecule libraries. These chaperone quantification tests are based on the capacity of HSP to counteract chemical or thermal protein aggregation.
应激诱导型热休克蛋白（如HSP70和HSP27）是分子伴侣，它们通过使细胞蛋白质保持折叠活性状态并防止其不可逆聚集来保护细胞免受应激损伤。HSP27和HSP70的伴侣活性是测试化学产品和物理应激对蛋白质变性的影响、筛选HSP抑制剂或确定伴侣功能在其他HSP活性（如细胞凋亡）中的作用的有用指标。我们已经开发了两种针对HSP27和HSP70的简单快速的伴侣活性测试，最初是为了测试从化学和小分子文库筛选得到的潜在HSP抑制剂的效果而设立的。这些伴侣定量测试基于HSP对抗化学或热诱导的蛋白质聚集的能力。
