Goossens M, Fanen P, Costes B, Ghanem N
Laboratoire de Biochimie, Hôpital Henri Mondor, Créteil.
Bull Acad Natl Med. 1993 Mar;177(3):371-80; discussion 380-1.
Cystic fibrosis (CF) is a fatal genetic disease primarily affecting Caucasians. Its etiology is complex, but it is chiefly a disease of electrolyte transport characterized by defects in fluid secretion by several epithelia. In this review are analyzed the data obtained since the cloning of the CF gene and the characterization of its product, the CF transmembrane conductance regulator (CFTR) protein, which has been shown to act like a cAMP-regulated chloride channel. This protein is a member of a family of ATP-binding proteins that are membrane-spanning, are found in a number of prokaryotic and eucaryotic cells, and have two ATP-binding domains. Unique to this family of proteins, the CFTR possesses an additional highly charged domain (the R domain). The majority of CF chromosomes (70%) have a single Phenylalanine codon deletion at position 508 of the protein (delta F508). A large number of other rare mutations (more than 230) have also been identified. This rapid accumulation of data is essential to genetic diagnosis and will aid in understanding the structure and function of the protein.
囊性纤维化（CF）是一种主要影响白种人的致命性遗传疾病。其病因复杂，但主要是一种电解质转运疾病，其特征是多种上皮细胞的液体分泌存在缺陷。在本综述中，分析了自CF基因克隆及其产物囊性纤维化跨膜传导调节因子（CFTR）蛋白的特性被发现以来所获得的数据，该蛋白已被证明具有类似cAMP调节的氯离子通道的作用。这种蛋白质是ATP结合蛋白家族的成员，这些蛋白跨膜存在，在许多原核细胞和真核细胞中都能找到，并且有两个ATP结合结构域。CFTR在这个蛋白质家族中是独特的，它拥有一个额外的高电荷结构域（R结构域）。大多数CF染色体（70%）在该蛋白的第508位有一个苯丙氨酸密码子缺失（ΔF508）。还发现了大量其他罕见突变（超过230种）。这些数据的快速积累对基因诊断至关重要，并将有助于理解该蛋白的结构和功能。
