Systematic survery for biologically active peptides in the atrium and pheochromocytoma tissue.

1993年我们发现了肾上腺髓质素（adrenomedullin，AM），并发现了另一种由肾上腺髓质素前体产生的高血压肽肾上腺髓质素前体N端20肽（proadrenomedullin N-terminal 20 peptide，PAMP）。阐明AM是一种新的调节循环和体液平衡的心血管激素。此外，AM在体内外均表现出对心血管的保护作用，提示AM有可能成为治疗心血管疾病和炎症性疾病的新药。因此，发现新的激素并研究其功能具有重要意义。我们同时进行了另一个项目，在猪心房和人嗜铬细胞瘤组织中发现了尚未鉴定的血管活性肽，发现AM可监测大鼠血小板中cAMP的升高。我们利用嗜铬细胞瘤细胞培养过程中cAMP的升高来寻找生物活性肽。使用这种方法，我们从嗜铬细胞瘤组织中分离出几种肽。这些肽分别为VIP、PAC ...更多信息 AP、CGRP和PHM。这些肽是已知的肽，但我们已经分离出新的肽，存在于嗜铬细胞瘤。许多生物活性肽的C-末端具有酰胺结构，这是生物活性所必需的。我们建立了一种新的方法来检测具有C-末端酰胺结构的肽。利用这种方法，我们从心房肌中分离到了一个新的14个氨基酸的肽，其C-端被酰胺化。这种肽被称为amidicin。脒霉素广泛分布于猪的组织中，尤其是在脑垂体、心室和脾脏中含量最高。本文建立了人阿米达霉素的放射免疫分析法，并测定了阿米达霉素在人体组织中的分布。我们发现，人amidicin是丰富的人嗜铬细胞瘤组织。我们从嗜铬细胞瘤中分离纯化了人脒霉素，并测定了其结构。此外，发现阿米卡星以相当高的浓度在人体血液中循环。脒霉素可能是一种新的参与循环调控的多肽。少

We discovered adrenomedullin (AM) in 1993 and found another hypetensive peptide proadrenomedullin N-terminal 20 peptide (PAMP) which is produced from adrenomedullin precursor. We have clarified that AM is a new cardiovascular hormone to regulate circulation and body fluid homeostasis. Further, AM shows protective actions for the heart and blood vessels in vitro and in vivo, suggesting that AM may be a new drugs for cardiovascular and inflammatory diseases. Thus, it is important to discover the new hormone and to study its function. We have concurrently advanced the another project to discover still unidentified vasoactive peptide in the porcine atrium and human pheochromocytoma tissue.AM was discovered monitoring the activity that elevate cAMP in the rat platelet. We have searched biological active peptide using the cAMP elevation in cultured cells from pheochromocytoma. Using this assay, we isolated several peptides from pheochromocytoma tissue. These peptide were found to be VIP, PAC … More AP, CGRP and PHM. These peptides were known peptides, but we have isolated novel peptide which exist in the the pheochromocytoma. Many biologically active peptides has C-terminal amide structure which is essential for biological activity. We have established a novel method to detect a peptide with C-terminal amide structure. Using this method, we have isolated a novel 14 amino acids peptide in the atrium whose C-terminus was amidated. This peptide was termed amidicin. Amidicin is widely distributed in porcine tissue and is especially abundant in pituitary gland, cardiac ventricle and spleen. We have developed radioimmunoassay for human amidicin, and examined the distribution of amidicin in human tissue. We found that human amidicin is abundant in human pheochromocytoma tissue. We purified human amidicin from pheochromocytoma and determined its structure. Furthermore, amidicin was found to circulate in human blood in a considerable concentration. Amidicin may be a possible new peptide participating in circulation control. Less