Ruddon R W, Sherman S A, Bedows E
Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha 68189, USA.
Protein Sci. 1996 Aug;5(8):1443-52. doi: 10.1002/pro.5560050801.
There have been few studies of protein folding in the endoplasmic reticulum of intact mammalian cells. In the one case where the in vivo and in vitro folding pathways of a mammalian secretory protein have been compared, the folding of the human chorionic gonadotropin beta subunit (hCG-beta), the order of formation of the detected folding intermediates is the same. The rate and efficiency with which multidomain proteins such as hCG-beta fold to native structure in intact cells is higher than in vitro, although intracellular rates of folding of the beta subunit can be approached in vitro in the presence of an optimal redox potential and protein disulfide isomerase. Understanding how proteins fold in vivo may provide a new way to diagnose and treat human illnesses that occur due to folding defects.
关于完整哺乳动物细胞内质网中蛋白质折叠的研究很少。在比较哺乳动物分泌蛋白体内和体外折叠途径的一个案例中，即人绒毛膜促性腺激素β亚基（hCG-β）的折叠，所检测到的折叠中间体的形成顺序是相同的。尽管在最佳氧化还原电位和蛋白质二硫键异构酶存在的情况下，体外可以接近β亚基的细胞内折叠速率，但多结构域蛋白如hCG-β在完整细胞中折叠成天然结构的速率和效率高于体外。了解蛋白质在体内如何折叠可能为诊断和治疗因折叠缺陷而发生的人类疾病提供一种新方法。
