CARDIOVASCULAR DISORDERS DUE TO DYSREGULATION OF THE RENIN – ANGEOTENSIN SYSTEM AND THE VASOPRESSINERGIC SYSTEM INTERACTION
Keywords:
Cardiovascular regulation, rennin, angiotensinogen, Ang II receptors.Abstract
Angiotensin II (Ang II) is a member of the renin-angiotensin system (RAS), which forms a cascade of highly active biological compounds regulating a variety of physiological functions. Co-activation of the RAS and the vasopressinergic system (VPS) by the same stimuli, and engagement of the same post-receptor intracellular pathways by Ang II and vasopressin (AVP), favors formation of different types of interactions, which may result in additive, synergistic, or antagonistic effects. Both Ang II and AVP directly participate in the regulation of the cardiovascular system. They also have an impact on several other processes, such as metabolism, stress, emotional disorders, and inflammation, which may exert potent secondary effects on the cardiovascular functions. The main purpose of the present review is to draw attention to the interactions of Ang II and AVP in the regulation of the water-electrolyte balance and blood pressure in healthy individuals and in patients with cardiovascular diseases. Specifically, we give a description of the regulation and function of the RAS and the VPS and we focus on the mechanisms underlying the interactions of Ang II and AVP in cardiovascular regulation and on disturbances of these interactions in cardiovascular diseases.
References
Prieto-Carrasquero MC, Botros FT, Kobori H, Navar LG. Collecting duct renin: a major player in angiotensin II–dependent hypertension. J Am Soc Hypertens. 2009;3(2):96–104.
Sequeira Lopez ML, Pentz ES, Nomasa T, Smithies O, Gomez RA. Renin cells are precursors for multiple cell types that switch to the renin phenotype when homeostasis is threatened. Dev Cell. 2004;6(5):719–28.
Hobart PM, Fogliano M, O'Connor BA, Schaefer IM, Chirgwin JM. Human renin gene: structure and sequence analysis. Proc Natl Acad Sci U S A. 1984;81(16):5026–30.
Morris BJ. Renin, genes, microRNAs, and renal mechanisms involved in hypertension. Hypertension. 2015;65(5):956–62.
Kuoppala A, Lindstedt KA, Saarinen J, Kovanen PT, Kokkonen JO. Inactivation of bradykinin by angiotensin-converting enzyme and by carboxypeptidase N in human plasma. Am J Physiol Heart Circ Physiol. 2000;278(4):H1069–74.
Soubrier F, Wei L, Hubert C, Clauser E, Alhenc-Gelas F, Corvol P. Molecular biology of the angiotensin I converting enzyme: II. Structure-function. Gene polymorphism and clinical implications. J Hypertens. 1993;11(6):599–604.
Donoghue M, Hsieh F, Baronas E, Godbout K, Gosselin M, Stagliano N, et al. A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9. Circ Res. 2000;87(5):E1–9.
Gomez RA, Lynch KR, Chevalier RL, Wilfong N, Everett A, Carey RM, et al. Renin and angiotensinogen gene expression in maturing rat kidney. Am J Physiol Renal Physiol. 1988;254(4):F582–7.
Ingelfinger JR, Zuo WM, Fon EA, Ellison KE, Dzau VJ. In situ hybridization evidence for angiotensinogen messenger RNA in the rat proximal tubule. An hypothesis for the intrarenal renin angiotensin system. J Clin Invest. 1990;85(2):417.
Friis UG, Jensen BL, Sethi S, Andreasen D, Hansen PB, Skøtt O. Control of renin secretion from rat juxtaglomerular cells by cAMP-specific phosphodiesterases. Circ Res. 2002;90(9):996–1003.
Beierwaltes WH. The role of calcium in the regulation of renin secretion. Am J Physiol Renal Physiol. 2010;298(1):F1–11.
Klar J, Sigl M, Obermayer B, Schweda F, Krämer BK, Kurtz A. Calcium inhibits renin gene expression by transcriptional and posttranscriptional mechanisms. Hypertension. 2005;46(6):1340–6.
