Tsukaguchi H, Matsubara H, Inada M
Second Department of Internal Medicine, Kansai Medical University, Osaka, Japan.
Kidney Int. 1995 Aug;48(2):554-62. doi: 10.1038/ki.1995.327.
Nephrogenic diabetes insipidus (NDI) is a rare X-linked disorder associated with renal tubule resistance to arginine vasopressin (AVP). To understand the mechanisms of AVP resistance underlying this disorder, we have analyzed the vasopressin V2 receptor gene in two unrelated Japanese kindreds with NDI and expressed the mutants to characterize their functional properties. Direct sequencing revealed two V2 receptor gene mutations: a missense mutation from Arg202 to Cys in the third extracellular domain (R202C) and a single base insertion (G) in two consecutive GGG triplets (nucleotide 804 to 809) in the third cytoplasmic domain, resulting in a frame shift with premature termination at codon 258 (804insG). Transient expression study with COS-7 cells showed that R202C mutation reduced both binding affinity (15%) and capacity (30%), while 804insG mutation abolished binding ability. For further evaluation of the binding ability of the R202C mutant, we expressed the mutants in Chinese hamster ovary (CHO) cells. Although the mutant cell lines produced V2 receptor mRNA comparable levels to the wild-type receptor cell lines, R202C mutant cell lines had no binding ability. Our results suggest an introduction of a new cysteine residue in the extracellular domain and a receptor truncation removing one third of the carboxyl terminus could impair ligand binding activity of the V2 receptor through a post-transcriptional mechanism, thereby causing AVP resistance in the NDI patients.
肾性尿崩症(NDI)是一种罕见的X连锁疾病,与肾小管对精氨酸加压素(AVP)的抵抗有关。为了解该疾病潜在的AVP抵抗机制,我们分析了两个无关的日本NDI家系中的加压素V2受体基因,并表达了突变体以表征其功能特性。直接测序揭示了两个V2受体基因突变:第三个细胞外结构域中从Arg202到Cys的错义突变(R202C),以及第三个细胞质结构域中两个连续的GGG三联体(核苷酸804至809)中的单个碱基插入(G),导致移码并在密码子258处提前终止(804insG)。用COS-7细胞进行的瞬时表达研究表明,R202C突变降低了结合亲和力(15%)和容量(30%),而804insG突变消除了结合能力。为了进一步评估R202C突变体的结合能力,我们在中国仓鼠卵巢(CHO)细胞中表达了这些突变体。尽管突变细胞系产生的V2受体mRNA水平与野生型受体细胞系相当,但R202C突变细胞系没有结合能力。我们的结果表明,在细胞外结构域引入一个新的半胱氨酸残基以及去除三分之一羧基末端的受体截短可能通过转录后机制损害V2受体的配体结合活性,从而导致NDI患者出现AVP抵抗。