热激蛋白70研究进展

Research Progress in Heat Shock Protein 70

热激蛋白70(HSP70)是广泛存在且高度保守的蛋白,作为伴侣分子能够促进蛋白折叠;HSP70可以通过阻止细胞色素c从线粒体释放,与凋亡诱导因子结合使其不能入核,或者抑制JNK激酶活性调节细胞凋亡;HSP70可以调节细胞周期进程,促进细胞生长,阻止细胞衰老;免疫功能研究表明HSP70是有效的免疫佐剂,可激发抗原特异性的CTL反应,同时细胞外HSP70和膜结合HSP70可激发非特异性免疫反应。

Heat shock protein 70（HSP70） family are a group of evolutionary highly conserved chaperone proteins. HSP70 proteins function as molecular chaperones that assist the folding of newly synthesized polypeptides. HSP70 regulates apoptosis by preventing cytochrome c release from mitochondria, inhibiting the muclear import of apoptosis-inducing factor or suppressing JNK activation. HSP70 regulates the cell cycle progression, promotes cancer cell growth and suppresses senescence. As an effective adjuvant, HSP70 induces antigen-specific CTL response. Extracellular and membrane-bound HSP70 also elicits immune responses.