Powell Kristina, Zeitlin Pamela L
The Johns Hopkins University School of Medicine, 316 Johns Hopkins Hospital, 600 N Wolfe St, Baltimore, MD 21287, USA.
Adv Drug Deliv Rev. 2002 Dec 5;54(11):1395-408. doi: 10.1016/s0169-409x(02)00148-5.
The deltaF508 mutation in the cystic fibrosis transmembrane regulator (CFTR) gene is the most common mutation in CF. The mutant CFTR protein is defective with respect to multiple functions including cAMP-regulated chloride conductance, nucleotide transport, and regulatory actions on other ion channels. Since the deltaF508 protein is also temperature-sensitive and unstable during translation and folding in the endoplasmic reticulum (ER), most of the nascent chains are targeted for premature proteolysis from the ER. This paper focuses on the events that occur in the ER during folding and reviews potential targets for therapeutic intervention.
囊性纤维化跨膜传导调节因子（CFTR）基因中的ΔF508突变是囊性纤维化（CF）中最常见的突变。突变的CFTR蛋白在多种功能方面存在缺陷，包括cAMP调节的氯离子传导、核苷酸转运以及对其他离子通道的调节作用。由于ΔF508蛋白在内质网（ER）中翻译和折叠过程中对温度敏感且不稳定，大多数新生链会在内质网中被靶向进行过早的蛋白水解。本文重点关注内质网中折叠过程中发生的事件，并综述治疗干预的潜在靶点。
