腺苷酸环化酶
内科学
内分泌学
血管紧张素II
蛋白激酶A
受体
阿德西9
血管紧张素Ⅱ受体1型
Gsα亚单位
化学
医学
激酶
生物化学
作者
Anja Tetzner,Kinga Gebolys,Christian Meinert,Sabine Klein,Anja Uhlich,Jonel Trebicka,Óscar Villacañas,Thomas Walther
出处
期刊:Hypertension
[Lippincott Williams & Wilkins]
日期:2016-05-24
卷期号:68 (1): 185-194
被引量:121
标识
DOI:10.1161/hypertensionaha.116.07572
摘要
Angiotensin (Ang)-(1-7) has cardiovascular protective effects and is the opponent of the often detrimental Ang II within the renin-angiotensin system. Although it is well accepted that the G-protein-coupled receptor Mas is a receptor for the heptapeptide, the lack in knowing initial signaling molecules stimulated by Ang-(1-7) prevented definitive characterization of ligand/receptor pharmacology as well as identification of further hypothesized receptors for the heptapeptide. The study aimed to identify a second messenger stimulated by Ang-(1-7) allowing confirmation as well as discovery of the heptapeptide's receptors. Ang-(1-7) elevates cAMP concentration in primary cells, such as endothelial or mesangial cells. Using cAMP as readout in receptor-transfected human embryonic kidney (HEK293) cells, we provided pharmacological proof that Mas is a functional receptor for Ang-(1-7). Moreover, we identified the G-protein-coupled receptor MrgD as a second receptor for Ang-(1-7). Consequently, the heptapeptide failed to increase cAMP concentration in primary mesangial cells with genetic deficiency in both Mas and MrgD Mice deficient in MrgD showed an impaired hemodynamic response after Ang-(1-7) administration. Furthermore, we excluded the Ang II type 2 receptor as a receptor for the heptapeptide but discovered that the Ang II type 2 blocker PD123319 can also block Mas and MrgD receptors. Our results lead to an expansion and partial revision of the renin-angiotensin system, by identifying a second receptor for Ang-(1-7), by excluding Ang II type 2 as a receptor for the heptapeptide, and by enforcing the revisit of such publications which concluded Ang II type 2 function by only using PD123319.
科研通智能强力驱动
Strongly Powered by AbleSci AI