囊性纤维化突变（ΔF508）不影响囊性纤维化跨膜传导调节因子的氯离子通道活性。

The cystic fibrosis mutation (delta F508) does not influence the chloride channel activity of CFTR.

作者信息

Li C, Ramjeesingh M, Reyes E, Jensen T, Chang X, Rommens J M, Bear C E

机构信息

Research Institute, Hospital for Sick Children, Toronto, Ontario, Canada.

出版信息

Nat Genet. 1993 Apr;3(4):311-6. doi: 10.1038/ng0493-311.

DOI:10.1038/ng0493-311

PMID:7526932

Abstract

The cystic fibrosis transmembrane conductance regulator (CFTR) is a phosphorylation-regulated Cl- channel. In most mammalian cells, the functional consequences of the most common CF mutation, delta F508-CFTR, cannot be assessed as the mutant protein undergoes biosynthetic arrest. However, function can be studied in the baculovirus-insect cell expression system where delta F508-CFTR does not appear to undergo such arrest. Our results show that phosphorylation-regulated Cl- channel activity of delta F508-CFTR is similar to that of wild-type CFTR. This observation was confirmed in comparative studies of purified delta F508-CFTR and CFTR reconstituted in planar lipid bilayers. Therefore, we suggest that this common mutation does not result in a significant alteration in CFTR function.

摘要

囊性纤维化跨膜传导调节因子（CFTR）是一种受磷酸化调节的氯离子通道。在大多数哺乳动物细胞中，由于突变蛋白发生生物合成停滞，无法评估最常见的CF突变（ΔF508 - CFTR）的功能后果。然而，在杆状病毒 - 昆虫细胞表达系统中可以研究其功能，在该系统中ΔF508 - CFTR似乎不会发生这种停滞。我们的结果表明，ΔF508 - CFTR的磷酸化调节氯离子通道活性与野生型CFTR相似。在纯化的ΔF508 - CFTR和重构于平面脂质双分子层中的CFTR的比较研究中证实了这一观察结果。因此，我们认为这种常见突变不会导致CFTR功能发生显著改变。