Structure–activity relationship study of angiotensin II analogs in terms of β-arrestin-dependent signaling to aldosterone production

Pharmacology Research and Perspectives

Volumn 4, Issue 2, 2016, Pages

  Valero, Thairy Reyes ^a   Sturchler, Emmanuel ^b   Jafferjee, Malika ^a   Rengo, Giuseppe ^c   Magafa, Vassiliki ^d   Cordopatis, Paul ^d   McDonald, Patricia ^b   Koch, Walter J ^e   Lymperopoulos, Anastasios ^a  

^a NOVA SOUTHEASTERN UNIVERSITY   (United States)

^b Translational Research Institute   (United States)

^c IRCCS   (Italy)

^d UNIVERSITY OF PATRAS   (Greece)

^e TEMPLE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Aldosterone; angiotensin II; angiotensin II type 1 receptor; biased ligand; structure activity relationship (SAR); arrestin; post MI HF

Indexed keywords

ALDOSTERONE; ANGIOTENSIN II; BETA ARRESTIN;

ARTICLE; CONTROLLED STUDY; ELECTROCHEMICAL IMPEDANCE SPECTROSCOPY; ENZYME ACTIVATION; HEART FUNCTION; HEMODYNAMICS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HORMONE SYNTHESIS; HUMAN; HUMAN CELL; HYPERALDOSTERONISM; MASS SPECTROMETRY; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION; STRUCTURE ACTIVITY RELATION; WESTERN BLOTTING;

EID: 85020900361     PISSN: None     EISSN: 20521707     Source Type: Journal    
DOI: 10.1002/prp2.226     Document Type: Article

References (30)

1. Balakumar P, Jagadeesh G (2014). Structural determinants for binding, activation, and functional selectivity of the angiotensin AT1 receptor. J Mol Endocrinol 53: R71–R92.
2. Bathgate-Siryk A, Dabul S, Pandya K, Walklett K, Rengo G, Cannavo A, et al. (2014). Negative impact of β -arrestin-1 on post-myocardial infarction heart failure via cardiac and adrenal-dependent neurohormonal mechanisms. Hypertension 63: 404–412.
3. Bomback AS, Klemmer PJ (2007). The incidence and implications of aldosterone breakthrough. Nat Clin Pract Nephrol 3: 486–492.
4. Dabul S, Bathgate-Siryk A, Valero TR, Jafferjee M, Sturchler E, McDonald P, et al. (2015). Suppression of adrenal β arrestin1-dependent aldosterone production by ARBs: head-to-head comparison. Sci Rep 5: 8116.
5. De Gasparo M, Catt KJ, Inagami T, Wright JW, Unger T (2000). International union of pharmacology. XXIII. The angiotensin II receptors. Pharmacol Rev 52: 415–472.
6. Ganguly A, Davis JS (1994). Role of calcium and other mediators in aldosterone secretion from the adrenal glomerulosa cells. Pharmacol Rev 46: 417–447.
7. Holloway AC, Qian H, Pipolo L, Ziogas J, Miura S, Karnik S, et al. (2002). Side-chain substitutions within angiotensin II reveal different requirements for signaling, internalization, and phosphorylation of type 1A angiotensin receptors. Mol Pharmacol 61: 768–777.
8. Luttrell LM, Gesty-Palmer D (2010). Beyond desensitization: physiological relevance of arrestin-dependent signaling. Pharmacol Rev 62: 305–330.
9. Lymperopoulos A, Bathgate A (2013). Arrestins in the cardiovascular system. Prog Mol Biol Transl Sci 118: 297–334.
10. Lymperopoulos A, Rengo G, Zincarelli C, Soltys S, Koch WJ (2008). Modulation of adrenal catecholamine secretion by in vivo gene transfer and manipulation of g protein-coupled receptor kinase-2 activity. Mol Ther 16: 302–307.
11. Lymperopoulos A, Rengo G, Zincarelli C, Kim J, Soltys S, Koch WJ (2009). An adrenal beta-arrestin 1-mediated signaling pathway underlies angiotensin II-induced aldosterone production in vitro and in vivo. Proc Natl Acad Sci USA 106: 5825–5830.
12. Lymperopoulos A, Rengo G, Zincarelli C, Kim J, Koch WJ (2011). Adrenal beta-arrestin 1 inhibition in vivo attenuates post-myocardial infarction progression to heart failure and adverse remodeling via reduction of circulating aldosterone levels. J Am Coll Cardiol 57: 356–365.
13. Lymperopoulos A, Sturchler E, Bathgate-Siryk A, Dabul S, Garcia D, Walklett K, et al. (2014). Different potencies of angiotensin receptor blockers at suppressing adrenal β -Arrestin1-dependent post-myocardial infarction hyperaldosteronism. J Am Coll Cardiol 64: 2805–2806.
14. McGuinness D, Malikzay A, Visconti R, Lin K, Bayne M, Monsma F, et al. (2009). Characterizing cannabinoid CB2 receptor ligands using discoverx pathhunter beta-arrestin assay. J Biomol Screen 14: 49–58.
15. Miura S, Feng YH, Husain A, Karnik SS (1999). Role of aromaticity of agonist switches of angiotensin II in the activation of the AT1 receptor. J Biol Chem 274: 7103–7110.
16. Nikiforovich GV, Zhang M, Yang Q, Jagadeesh G, Chen H-C, Hunyady L, et al. (2006). Interactions between conserved residues in transmembrane helices 2 and 7 during angiotensin AT1 receptor activation. Chem Biol Drug Des 68: 239–249.
17. Peters MF, Knappenberger KS, Wilkins D, Sygowski LA, Lazor LA, Liu J, et al. (2007). Evaluation of cellular dielectric spectroscopy, a whole-cell, label-free technology for drug discovery on Gi-coupled GPCRs. J Biomol Screen 12: 312–319.
18. Qian H, Pipolo L, Thomas WG (2001). Association of β -arrestin 1 with the type 1A angiotensin II receptor involves phosphorylation of the receptor carboxyl terminus and correlates with receptor internalization. Mol Endocrinol 15: 1706–1719.
19. Rainey WE, Saner K, Schimmer BP (2004). Adrenocortical cell lines. Mol Cell Endocrinol 228: 23–38.
20. Salazar NC, Vallejos X, Siryk A, Rengo G, Cannavo A, Liccardo D, et al. (2013). GRK2 blockade with β ARKct is essential for cardiac β 2-adrenergic receptor signaling towards increased contractility. Cell Commun Signal 11: 64.
21. Shukla AK, Violin JD, Whalen EJ, Gesty-Palmer D, Shenoy SK, Lefkowitz RJ (2008). Distinct conformational changes in beta-arrestin report biased agonism at seven-transmembrane receptors. Proc Natl Acad Sci USA 105: 9988–9993.
22. Shukla AK, Manglik A, Kruse AC, Xiao K, Reis RI, Tseng WC, et al. (2013). Structure of active β -arrestin-1 bound to a G-protein-coupled receptor phosphopeptide. Nature 497: 137–141.
23. Soergel DG, Subach RA, Cowan CL, Violin JD, Lark MW (2013). First clinical experience with TRV027: pharmacokinetics and pharmacodynamics in healthy volunteers. J Clin Pharmacol 53: 892–899.
24. Tzakos AG, Gerothanassis IP, Troganis AN (2004). On the structural basis of the hypertensive properties of angiotensin II: a solved mystery or a controversial issue? Curr Top Med Chem 4: 431–444.
25. Violin JD, DeWire SM, Yamashita D, Rominger DH, Nguyen L, Schiller K, et al. (2010). Selectively engaging β -arrestins at the angiotensin II type 1 receptor reduces blood pressure and increases cardiac performance. J Pharmacol Exp Ther 335: 572–579.
26. Violin JD, Soergel DG, Boerrigter G, Burnett JC Jr, Lark MW (2013). GPCR biased ligands as novel heart failure therapeutics. Trends Cardiovasc Med 23: 242–249.
27. Weber KT (2001). Aldosterone in congestive heart failure. N Engl J Med 345: 1689–1697.
28. Wilkes BC, Masaro L, Schiller PW, Carpenter KA (2002). Angiotensin II vs its type I antagonists: conformational requirements for receptor binding assessed from NMR spectroscopic and receptor docking experiments. J Med Chem 45: 4410–4418.
29. Zhang H, Unal H, Gati C, Han GW, Liu W, Zatsepin NA, et al. (2015). Structure of the angiotensin receptor revealed by serial femtosecond crystallography. Cell 161: 833–844.
30. Zimmerman B, Beautrait A, Aguila B, Charles R, Escher E, Claing A, et al. (2012). Differential β -arrestin-dependent conformational signaling and cellular responses revealed by angiotensin analogs. Sci Signal 5: ra33.