Schönauer Ria, Els-Heindl Sylvia, Beck-Sickinger Annette G
Faculty of Biosciences, Pharmacy and Psychology, Institute of Biochemistry, Leipzig University, Brüderstraße 34, 04103, Leipzig, Germany.
J Pept Sci. 2017 Jul;23(7-8):472-485. doi: 10.1002/psc.2953. Epub 2017 Feb 2.
Adrenomedullin (ADM) is a 52-amino acid multifunctional peptide, which belongs to the calcitonin gene-related peptide (CGRP) superfamily of vasoactive peptide hormones. ADM exhibits a significant vasodilatory potential and plays a key role in various regulatory mechanisms, predominantly in the cardiovascular and lymphatic system. It exerts its effects by activation of the calcitonin receptor-like receptor associated with one of the receptor activity-modifying proteins 2 or 3. ADM was first isolated from human phaeochromocytoma in 1993. Numerous studies revealed a widespread distribution in various tissues and organs, which is reflected by its multiple physiological roles in health and disease. Because of its anti-inflammatory, anti-apoptotic and proliferative properties, ADM exhibits potent protective functions under diverse pathological conditions, but it is also critically involved in tumor progression. ADM has therefore raised great interest in therapeutic applications and several clinical trials already revealed promising results. However, because the receptor activation mode has not yet been fully elucidated, a rational design of potent and selective ligands is still challenging. Detailed information on the binding mode of ADM from a recently reported crystal structure as well as efforts to improve its plasma stability and bioavailability may help to overcome these limitations in the future. Copyright © 2017 European Peptide Society and John Wiley & Sons, Ltd.
肾上腺髓质素(ADM)是一种由52个氨基酸组成的多功能肽,属于血管活性肽激素的降钙素基因相关肽(CGRP)超家族。ADM具有显著的血管舒张潜力,在多种调节机制中起关键作用,主要是在心血管和淋巴系统中。它通过激活与受体活性修饰蛋白2或3之一相关的降钙素受体样受体来发挥作用。ADM于1993年首次从人嗜铬细胞瘤中分离出来。大量研究表明其在各种组织和器官中广泛分布,这反映在它在健康和疾病中的多种生理作用上。由于其抗炎、抗凋亡和增殖特性,ADM在多种病理条件下具有强大的保护功能,但它也与肿瘤进展密切相关。因此,ADM在治疗应用方面引起了极大的兴趣,一些临床试验已经显示出了有希望的结果。然而,由于受体激活模式尚未完全阐明,合理设计强效和选择性配体仍然具有挑战性。最近报道的晶体结构中关于ADM结合模式的详细信息以及提高其血浆稳定性和生物利用度的努力可能有助于在未来克服这些限制。版权所有© 2017欧洲肽学会和约翰·威利父子有限公司。