Itoh H, Nakao K, Kambayashi Y, Hosoda K, Saito Y, Yamada T, Mukoyama M, Arai H, Shirakami G, Suga S
Department of Medicine, Kyoto University School of Medicine, Japan.
Biochem Biophys Res Commun. 1989 Jun 15;161(2):732-9. doi: 10.1016/0006-291x(89)92661-2.
We established a specific radioimmunoassay for the ring structure of "iso-ANP" and detected iso-ANP[23-46]-like immunoreactivity (-LI) in the rat atrium (2.76 +/- 0.5 micrograms/g) and ventricle (13.9 +/- 5.7 ng/g). High performance-gel permeation chromatography revealed that iso-ANP[23-46]-LI in the rat heart was composed of two components with molecular weights of 10K and 5K. In reverse phase-high performance liquid chromatography, the retention times of these components were clearly different from that of synthetic iso-ANP. The 5K peptide was demonstrated to be present in the perfusate from isolated rat hearts and possessed binding ability to ANP receptors. This natriuretic peptide was, however, not detectable in other tissues including the brain. We conclude that the novel cardiac natriuretic peptide distinct from iso-ANP and ANP occurs in the rat heart and is secreted from the heart.
我们建立了一种针对“异-心房钠尿肽(iso-ANP)”环状结构的特异性放射免疫测定法,并在大鼠心房(2.76±0.5微克/克)和心室(13.9±5.7纳克/克)中检测到了类异-ANP[23 - 46]免疫反应性(-LI)。高效凝胶渗透色谱显示,大鼠心脏中的异-ANP[23 - 46]-LI由分子量分别为10K和5K的两种成分组成。在反相高效液相色谱中,这些成分的保留时间与合成异-ANP的保留时间明显不同。已证明5K肽存在于离体大鼠心脏的灌流液中,并且具有与心房钠尿肽受体的结合能力。然而,在包括脑在内的其他组织中未检测到这种利钠肽。我们得出结论,一种不同于异-ANP和心房钠尿肽的新型心脏利钠肽存在于大鼠心脏中并由心脏分泌。