Morishita Y, Sano T, Ando K, Saitoh Y, Kase H, Yamada K, Matsuda Y
Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Ltd., Japan.
Biochem Biophys Res Commun. 1991 May 15;176(3):949-57. doi: 10.1016/0006-291x(91)90374-g.
During the search for ANP receptor ligands of microbial origin, we isolated a novel polysaccharide, HS-142-1, from culture broth of Aureobasidium sp. HS-142-1 inhibited [125I]-rANP binding to ANP receptor in rabbit kidney cortex membranes with an IC50 of 0.3 mu g/ml, but gave no effects on specific binding of [125I]-Endothelin nor [125I]-Angiotensin II to their respective receptors in bovine lung membranes. HS-142-1 competitively and selectively inhibited ANP binding to its guanylyl cyclase-containing receptor purified from solubilized bovine adrenocortical membranes and blocked cGMP production elicited by ANP. HS-142-1 is the first non-peptide antagonist selective for ANP functional receptor and will be a powerful tool to elucidate the physiological functions of ANP.
在寻找微生物来源的心房钠尿肽（ANP）受体配体的过程中，我们从 Aureobasidium sp. 的培养液中分离出一种新型多糖 HS - 142 - 1。HS - 142 - 1 抑制 [125I] - rANP 与兔肾皮质膜中 ANP 受体的结合，IC50 为 0.3 μg/ml，但对 [125I] - 内皮素或 [125I] - 血管紧张素 II 与牛肺膜中各自受体的特异性结合没有影响。HS - 142 - 1 竞争性且选择性地抑制 ANP 与从溶解的牛肾上腺皮质膜中纯化的含鸟苷酸环化酶受体的结合，并阻断 ANP 引发的环磷酸鸟苷（cGMP）生成。HS - 142 - 1 是首个对 ANP 功能受体具有选择性的非肽拮抗剂，将成为阐明 ANP 生理功能的有力工具。
