Watt V M, Yip C C
Department of Physiology, University of Toronto, Canada.
Biochem Biophys Res Commun. 1989 Oct 31;164(2):671-7. doi: 10.1016/0006-291x(89)91512-x.
Receptors for atrial natriuretic peptide (ANP) are heterogeneous: an approximately 140-kDa receptor exhibits ANP-stimulated guanylate cyclase activity whereas an approximately 65-kDa receptor is thought to act only as a clearance-storage protein. We have used photoaffinity labeling techniques to show that the human cell line, HeLa, contains predominantly the approximately 140-kDa ANP receptor. In contrast, several other cell lines contain primarily the approximately 65-kDa receptor. In HeLa cells, ANP bound specifically to high affinity binding sites (Kd approximately 2 nM) and stimulated a rapid, dose-dependent accumulation of cGMP. These cell lines can thus provide useful models to study the multiple mechanisms of ANP action.
心房利钠肽（ANP）的受体具有异质性：一种约140 kDa的受体表现出ANP刺激的鸟苷酸环化酶活性，而一种约65 kDa的受体被认为仅作为清除 - 储存蛋白起作用。我们使用光亲和标记技术表明，人类细胞系HeLa主要含有约140 kDa的ANP受体。相比之下，其他几种细胞系主要含有约65 kDa的受体。在HeLa细胞中，ANP特异性结合高亲和力结合位点（Kd约为2 nM）并刺激cGMP的快速、剂量依赖性积累。因此，这些细胞系可为研究ANP作用的多种机制提供有用的模型。
