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</annotation></qual:qualitativeSpecies></qual:listOfQualitativeSpecies><qual:listOfTransitions><qual:transition qual:id="tr_csa4"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa26" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_csa4_in_0" /><qual:input qual:qualitativeSpecies="sa30" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_csa4_in_1" /><qual:input qual:qualitativeSpecies="sa23" qual:transitionEffect="none" qual:sign="negative" qual:id="tr_csa4_in_2" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="csa4" qual:transitionEffect="assignmentLevel" qual:id="tr_csa4_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><and /><apply><eq /><ci>sa26</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa30</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa23</ci><cn type="integer">0</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body><p>Because AT1R seems to be essential for Ang-II–mediated ACE2 internalization, we also tested whether ACE2 and AT1R physically interact. Coimmunoprecipitation experiments confirmed this dimerization in control conditions (Figure 5B, second lane). However, Ang-II treatment decreased this interaction in a time-dependent manner [...]. PMID:25225202
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</rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_csa5"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa30" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_csa5_in_0" /><qual:input qual:qualitativeSpecies="sa38" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_csa5_in_1" /><qual:input qual:qualitativeSpecies="sa45" qual:transitionEffect="none" qual:sign="negative" qual:id="tr_csa5_in_2" /><qual:input qual:qualitativeSpecies="sa40" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_csa5_in_3" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="csa5" qual:transitionEffect="assignmentLevel" qual:id="tr_csa5_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><or /><apply><and /><apply><eq /><ci>sa30</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa38</ci><cn type="integer">1</cn></apply></apply><apply><and /><apply><eq /><ci>sa38</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa40</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa45</ci><cn type="integer">0</cn></apply></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body><p>Recently, ACE2 was reported as an entry receptor for SARS-CoV-2. In this study, we present the crystal structure of the C-terminal domain of SARS-CoV-2 (SARS-CoV-2-CTD) spike (S) protein in complex with human ACE2 (hACE2), which reveals a hACE2-binding mode similar overall to that observed for SARS-CoV. PMID:32275855
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<p>SARS-CoV-2 can use TMPRSS2 for S protein priming and camostat mesylate, an inhibitor of TMPRSS2, blocks SARS-CoV-2 infection of lung cells. PMID:32142651
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</rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_csa9"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa102" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_csa9_in_0" /><qual:input qual:qualitativeSpecies="sa77" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_csa9_in_1" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="csa9" qual:transitionEffect="assignmentLevel" qual:id="tr_csa9_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><and /><apply><eq /><ci>sa102</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa77</ci><cn type="integer">1</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body><p>The G-protein-coupled receptor Mas, encoded by the Mas proto-oncogene, has been identified as an endogenous receptor for the heptapeptide angiotensin-(1-7); however, the receptor is also suggested to be involved in actions of angiotensin II. The study tested whether this could be mediated indirectly through an interaction with the angiotensin II type 1 receptor, AT1. In transfected mammalian cells, Mas was not activated by angiotensin II; however, AT1 receptor-mediated, angiotensin II-induced production of inositol phosphates and mobilization of intracellular Ca2+ was diminished by 50% after coexpression of Mas, despite a concomitant increase in angiotensin II binding capacity. Mas and the AT1 receptor formed a constitutive hetero-oligomeric complex that was unaffected by the presence of agonists or antagonists of the 2 receptors. In vivo, Mas acts as an antagonist of the AT1 receptor; mice lacking the Mas gene show enhanced angiotensin II-mediated vasoconstriction in mesenteric microvessels. These results demonstrate that Mas can hetero-oligomerize with the AT1 receptor and by so doing inhibit the actions of angiotensin II. PMID:15809376
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Renin provides only one known function, to cleave the 10-amino acid precursor peptide angiotensin I (Ang-I),1 from the N terminus of mature angiotensinogen (AGT). PMID:10585461
</p>
<p>The study characterized Ang-(1-12) metabolism in the serum and kidney of the mRen2.Lewis rat, a model of high circulating renin and ACE expression. Ang-(1-12) processing to serum did not reveal the participation of renin; however, serum ACE readily converted Ang-(1-12) to Ang I with subsequent metabolism to Ang II. Ang I and Ang II forming activities for serum ACE were 102 and 104 fmol/ml/min serum (n=3), respectively, and both products were abolished by the potent ACE inhibitor lisinopril. PMID:22490446
</p>
<p>Apart from Renin, several enzymes were found to cleave angiotensinogen into Ang-I, such as cathepsin D (CTSD), cathepsin G (CTSG), and tonins. PMID:30934934
A human neutrophil protease, initially termed neutral peptide-generating protease, has been shown to cleave angiotensin II directly from angiotensinogen and has been identified as leukocyte cathepsin G. When purified neutrophils were disrupted by nitrogen cavitation and fractionated by differential centrifugation, 44 and 24% of the angiotensin II-generating activity was in the lysosomal and undisrupted cell fractions, respectively. The angiotensin II-generating protease of human neutrophils has been identified as cathepsin G on the basis of subcellular localization, substrate specificity, physicochemical characteristics, and antigenic identity. PMID:6172448
</p>
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</rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa22"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa21" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa22_in_0" /><qual:input qual:qualitativeSpecies="sa30" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa22_in_1" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa22" qual:transitionEffect="assignmentLevel" qual:id="tr_sa22_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><and /><apply><eq /><ci>sa21</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa30</ci><cn type="integer">1</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body><p>Recombinant ACE2 hydrolyzes the carboxy terminal leucine from angiotensin I to generate angiotensin 1-9, which is converted to smaller angiotensin peptides by ACE in vitro and by cardiomyocytes in culture. PMID:10969042
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</p>
<p>ACE2 functions as a carboxypeptidase, cleaving a single residue from angiotensin I (AngI), generating Ang1-9, and a single  residue from angiotensin II (AngII) to generate Ang1-7. The ACE2 homologue ACE, by contrast, cleaves the decapeptide AngI into the  octapeptide AngII. Thus, ACE2 counterbalances the function of ACE and negatively regulates AngII production. To test whether Spike-Fc injections indeed affect the function of the renin-angiotensin system, AngII levels in the lungs of acid- and Spike-Fc–treated mice were analyzed. Acid aspiration increased AngII levels in the lungs of wild-type mice. Notably, the authors observed a further, significant increase in AngII levels in the lung tissue of mice treated with Spike-Fc. PMID:16007097
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Adipocytes express all components of the renin-angiotensin system, and the renin-angiotensin system is involved in obesity and insulin resistance. The aim of this study was to investigate plasma Ang II in obese patients with type 2 diabetes mellitus (T2D) and the change during weight loss. Fifty Japanese obese subjects with T2D were enrolled. After 24 weeks of weight reduction diet, the mean body weight, visceral fat area (VFA), and hemoglobin A(1c) decreased significantly by 2.3%, 7.0%, and 8.3%, respectively. The mean plasma Ang II decreased by 24% and correlated with body weight both at baseline. PMID:19375596
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<p>Overall the findings suggest that Ang-(1-12), not Ang I, is the better substrate for Ang II formation by chymase in adult rats. In addition, this confirms the previous observation that chymase (rather than ACE) is the main hydrolyzing enzyme responsible for Ang II generation from Ang-(1-12) in the adult rat heart. PMID:27465904
Since angiotensin-(1-12) [Ang-(1-12)] is a non-renin dependent alternate precursor for the generation of cardiac Ang peptides in rat tissue, the authors investigated the metabolism of Ang-(1-12) by plasma membranes (PM) isolated from human atrial appendage tissue from nine patients undergoing cardiac surgery for primary control of atrial fibrillation. PM was incubated with highly purified Ang-(1-12) for 1 h with or without renin-angiotensin system (RAS) inhibitors [lisinopril for angiotensin converting enzyme (ACE), SCH39370 for neprilysin (NEP), MLN-4760 for ACE2 and chymostatin for chymase].  In the absence of all RAS inhibitor, Ang-(1-12) was converted into Ang I (2%), Ang II (69%), Ang-(1-7) (5%), and Ang-(1-4) (2%). In the absence of all RAS inhibitor, only 22% of Ang-(1-12) was unmetabolized, whereas, in the presence of the all RAS inhibitors, 98% of Ang-(1-12) remained intact. The relative contribution of selective inhibition of ACE and chymase enzyme showed that Ang-(1-12) was primarily converted into Ang II (65%) by chymase while its hydrolysis into Ang II by ACE was significantly lower or undetectable. PMID:22180785
</p>
<p>Although angiotensin II (Ang II)-forming enzymatic activity in the human left cardiac ventricle is minimally inhibited by angiotensin I (Ang I) converting enzyme inhibitors, over 75% of this activity is inhibited by serine proteinase inhibitors. The authors report the identification and characterization of the major Ang II-forming, neutral serine proteinase, from left ventricular tissues of the human heart. A 115,150-fold purification from human cardiac membranes yielded a purified protein with an Mr of 30,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Based upon its amino-terminal sequence, the major human cardiac Ang II-forming proteinase appears to be a novel member of the chymase subfamily of chymotrypsin-like serine proteinases. Human heart chymase was completely inhibited by the serine proteinase inhibitors, soybean trypsin inhibitor, phenylmethylsulfonyl fluoride, and chymostatin. It was partially inhibited by p-tosyl-L-phenylalanine chloromethyl ketone, but was not inhibited by p-tosyl-L-lysine chloromethyl ketone, and aprotinin. Also, human heart chymase was not inhibited by inhibitors of the other three classes of proteinases. Human heart chymase has a high specificity for the conversion of Ang I to Ang II and the Ang I-carboxyl-terminal dipeptide His-Leu. Human heart chymase did not degrade several peptide hormones, including Ang II, bradykinin, and vasoactive intestinal peptide, nor did it form Ang II from angiotensinogen. The high substrate specificity of human heart chymase for Ang I distinguishes it from other Ang II-forming enzymes including Ang I converting enzyme, tonin, kallikrein, cathepsin G, and other known chymases. PMID:2266130
</p>
<p>This study was undertaken to confirm a previous preliminary observation that hog pancreas kallikrein (EC 3.4.21.35) directly liberated an angiotensin-like substance from human plasma protein Cohn fraction IV-4 at an acidic pH of 4.0-5.0. The amino acid composition of the isolated pressor substance (residues/mol) was: Asp, 1.03; Val, 1.03; Ile, 1.00; Tyr, 0.69; Phe, 1.04; His, 0.91; Arg, 0.86; Pro, 0.86. This composition was identical with that of angiotensin. Since the reaction mixture was not contaminated with common proteolytic enzymes, such as trypsin, chymotrypsin, renin, cathepsin D and proangiotensin-converting enzyme, and other enzymes activated by kallikrein, it is clear that hog kallikrein directly produces angiotensin in vitro. PMID:6555043
</p>
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</p>
<p>The main role of ACE2 is the degradation of Ang II resulting in the formation of angiotensin 1-7 (Ang 1-7) which opposes the actions of Ang II. PMID:22536270
ACE2 metabolizes ANG II to Ang 1-7 in the kidney at neutral and basic pH, while prolylcarboxypeptidase catalyzes the same reaction at acidic pH. PMID:23392115
</p>
<p>Ang I can be cleaved by NEP (MME) to Ang (1–7) in CHO cells transfected with human MME. ACE and NEP hydrolysed Ang I efficiently, whereas ACE2 hydrolysed Ang I only very slowly. PMID:15283675
Angiotensin peptides are metabolized by several subsequent enzymatic steps: First, renin cleaves angiotensinogen, into angiotensin I (Ang I). Ang I can be metabolized by angiotensin-converting enzyme (ACE) resulting in the production of the bioactive octapeptide angiotensin II (Ang II), which interacts with AT1 and AT2 receptors. Alternatively, it can be processed first by ACE2 to the inactive peptide Ang-(1–9) and then by ACE to Ang-(1–7) or by neutral endopeptidase 24.11 (NEP) or prolylendopeptidase (PREP) directly to Ang-(1–7). Ang-(1–7) can also be generated by ACE2 from Ang II and interacts with its receptor Mas. PMID:23463883.
</p>
<p>The metabolism of Ang-(1-12) in renal cortical membranes also revealed the formation of Ang I; however, the main products were Ang-(1-7) and Ang-(1-4) at 129 and 310 fmol/mg/min protein (n=4), respectively. Neprilysin inhibition abolished these products and substantially reduced the overall metabolism of Ang-(1-12). Incubation of Ang-(1-12) with either human or mouse neprilysin revealed identical products. PMID:22490446
</p>
<p>Ang-(1-7) is the main metabolite of angiotensin I in rat hippocampi, and thimet oligopeptidase is the main enzyme involved in the generation of Ang-(1-7). PMID:24041943
</p>
<p>Metabolism of 125I-angiotensin I was investigated. In intact endothelial cells, production of Ang (1-7) was partially blocked by the addition of Z-pro-prolinal,  an inhibitor of prolyl endopeptidase. This confirms that prolyl endopeptidase is partially involved in the generation of Ang-(l-7). PMID:1310484
</p>
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</rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa25"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa79" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa25_in_0" /><qual:input qual:qualitativeSpecies="sa70" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa25_in_1" /><qual:input qual:qualitativeSpecies="sa23" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa25_in_2" /><qual:input qual:qualitativeSpecies="sa51" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa25_in_3" /><qual:input qual:qualitativeSpecies="sa24" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa25_in_4" /><qual:input qual:qualitativeSpecies="sa22" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa25_in_5" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa25" qual:transitionEffect="assignmentLevel" qual:id="tr_sa25_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><or /><apply><and /><apply><eq /><ci>sa79</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa70</ci><cn type="integer">1</cn></apply></apply><apply><and /><apply><or /><apply><eq /><ci>sa23</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa51</ci><cn type="integer">1</cn></apply></apply><apply><eq /><ci>sa79</ci><cn type="integer">1</cn></apply></apply><apply><and /><apply><eq /><ci>sa79</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa24</ci><cn type="integer">1</cn></apply></apply><apply><and /><apply><eq /><ci>sa79</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa22</ci><cn type="integer">1</cn></apply></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body><p>Although treatment with AGTR1 antagonist (losartan) or AGTR2 agonist (CGP42112A) inhibits tumor progression in several cancer cells, their combined treatment has not been reported. PMID:25014541
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<p>Angiotensin II (ANGII) signaling, mediated via angiotensin II receptor type 1 (AGTR1) or type 2 (AGTR2), controls tissue remodeling in fibrosis, but the relevance of AGTR2 remains elusive. PMID:17630322
Chronic activation of the myocardial renin angiotensin system (RAS) elevates the local level of angiotensin II (Ang II) thereby inducing pathological cardiac hypertrophy, which contributes to heart failure. The authors report a novel paracrine mechanism between cardiac fibroblasts (CF)s and cardiomyocytes whereby Ang II induces pathological cardiac hypertrophy. In cultured rat CFs, Ang II treatment enhanced exosome release via the activation of Ang II receptor types 1 (AT1R) and 2 (AT2R), whereas lipopolysaccharide, insulin, endothelin (ET)-1, transforming growth factor beta (TGFbeta)1 or hydrogen peroxide did not. PMID:26497614
ANG (1-7) acts primarily via the G protein-coupled receptor MAS1, and forms ANG (1-5), which signals via MRGPRD. ANG (1-7) can also act via the AGTR2 receptor but with much lower affinity than ANG II. PMID:32333398
Ang A has the same affinity to the AT1 receptor as Ang II, but a higher affinity to the AT2 receptor. PMID:17138938
</p>
<p>ANG (1-7) acts primarily via the G protein-coupled receptor MAS1, and forms ANG (1-5), which signals via MRGPRD. ANG (1-7) can also act via the AGTR2 receptor but with much lower affinity than ANG II. PMID:32333398
The study investigated whether a vasodepressor effect of Ang-(1-7) could be unmasked acutely in conscious spontaneously hypertensive rats (SHR) against a background of angiotensin II type 1 (AT1) receptor blockade. Mean arterial pressure (MAP) and heart rate were measured over a 5-day protocol in various groups of rats randomized to receive the following drug combinations: saline, AT1 receptor (AT1R) antagonist candesartan (0.01 or 0.1 mg/kg IV) alone, Ang-(1-7) (5 pmol/min) alone, candesartan plus Ang-(1-7), and candesartan plus Ang-(1-7) and angiotensin II type 2 (AT2) receptor (AT2R) antagonist PD123319 (50 microg/kg per minute). In Wistar-Kyoto (WKY) rats, saline, Ang-(1-7), or candesartan alone caused no significant alteration in MAP, whereas Ang-(1-7) coadministered with candesartan caused a marked, sustained reduction in MAP. A similar unmasking of a vasodepressor response to Ang-(1-7) during AT1R blockade was observed in SHR. Moreover, the AT(2)R antagonist PD123319 markedly attenuated the enhanced depressor response evoked by the Ang-(1-7)/candesartan combination in SHR and WKY rats. In separate experiments, the bradykinin type 2 receptor antagonist HOE 140 (100 microg/kg IV) or the NO synthase inhibitor Nomega-nitro-L-arginine methyl ester (1 mg/kg IV) abolished the depressor effect of Ang-(1-7) in the presence of candesartan. Collectively, these results suggest that Ang-(1-7) evoked a depressor response during AT1R blockade via activation of AT2R, which involves the bradykinin-NO cascade. PMID:15767466
</p>
<p>Systemic delivery of angiotensin-(1-9) significantly decreased cell death and improved left ventricular recovery after in vivo myocardial infarction. In vitro, angiotensin-(1-9) decreased cell death in isolated neonatal rat ventricular cardiomyocytes subjected to simulated ischemia/reperfusion. The cardioprotective effects of angiotensin-(1-9) were blocked by PD123319 (AT2R antagonist) and Akt inhibitor but not by A779 (Mas antagonist). Angiotensin-(1-9) limits reperfusion-induced cell death by an AT2R- and Akt-dependent mechanism. PMID:30048754
</p>
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</rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa27"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa77" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa27_in_0" /><qual:input qual:qualitativeSpecies="sa32" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa27_in_1" /><qual:input qual:qualitativeSpecies="sa159" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa27_in_2" /><qual:input qual:qualitativeSpecies="sa24" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa27_in_3" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa27" qual:transitionEffect="assignmentLevel" qual:id="tr_sa27_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><or /><apply><and /><apply><eq /><ci>sa77</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa32</ci><cn type="integer">1</cn></apply></apply><apply><and /><apply><eq /><ci>sa77</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa159</ci><cn type="integer">1</cn></apply></apply><apply><and /><apply><eq /><ci>sa77</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa24</ci><cn type="integer">1</cn></apply></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body><p>Angiotensin-(1-5) [Ang-(1-5)], which is a metabolite of Angiotensin-(1-7) [Ang-(1-7)] catalyzed by angiotensin-converting enzyme (ACE), is a pentapeptide of the renin-angiotensin system (RAS). It has been reported that Ang-(1-7) and Ang-(1-9) stimulate the secretion of atrial natriuretic peptide (ANP) via Mas receptor (Mas R) and Ang II type 2 receptor (AT2R), respectively. The effect of Ang-(1-5) on ANP secretion was investigated using isolated perfused beating rat atria. Ang-(1-5) stimulated high pacing frequency-induced ANP secretion in a dose-dependent manner. Ang-(1-5)-induced ANP secretion was attenuated by the pretreatment with an antagonist of Mas R (A-779) but not by an antagonist of AT1R (losartan) or AT2R (PD123,319). PMID:27660028
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<p>In support of this hypothesis we show that the non-peptide MAS agonist AR234960 increases both mRNA and protein levels of CTGF via ERK1/2 signaling in HEK293-MAS cells and adult human cardiac fibroblasts. PMID:29287092
</p>
<p>ANG-(1-7) itself acts on the receptor MAS to influence a range of mechanisms in the heart, kidney, brain, and other tissues. PMID:29351514
Angiotensin (Ang)-(1-7) has cardiovascular protective effects and is the opponent of the often detrimental Ang II within the renin-angiotensin system. 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, the study provided pharmacological proof that Mas is a functional receptor for Ang-(1-7). Moreover, the authors identified the G-protein-coupled receptor MrgD as a second receptor for Ang-(1-7). PMID:27217404
</p>
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</rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa28"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa37" qual:transitionEffect="none" qual:sign="negative" qual:id="tr_sa28_in_0" /><qual:input qual:qualitativeSpecies="sa169" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa28_in_1" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa28" qual:transitionEffect="assignmentLevel" qual:id="tr_sa28_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><and /><apply><eq /><ci>sa169</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa37</ci><cn type="integer">0</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body><p>Addition of estradiol (E2) to HUVEC cells induces a concentration-dependent increase of ACE1 and ACE2 mRNA expression and ACE1, but not ACE2, protein levels. ACE1 and ACE2 enzymatic activities are also induced with E2. These effects were mediated through estrogen receptor alpha activation, since ER antagonists ICI 182780 and MPP completely abolishes the effect of E2. PMID:26562171
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Calcitriol inhibits ACE and AT1R expression, and induces ACE2 expression in LPS-treated rat PMVECs. PMID:28944831
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Addition of estradiol (E2) to HUVEC cells induces a concentration-dependent increase of ACE1 and ACE2 mRNA expression and ACE1, but not ACE2, protein levels. ACE1 and ACE2 enzymatic activities are also induced with E2. These effects were mediated through estrogen receptor alpha activation, since ER antagonists ICI 182780 and MPP completely abolishes the effect of E2. PMID:26562171
Calcitriol inhibits ACE and AT1R expression, and induces ACE2 expression in LPS-treated rat PMVECs. PMID:28944831
Recombinant SARS-CoV spike protein downregulates ACE2 expression and thereby promotes lung injury. PMID:19864379
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<p>By using quantitative translatome and proteomics the authors found that the protein level of ACE2 is mildly reduced after infection. PMID:32408336
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<p>We found age-dependent ACE2 gene expression in nasal epithelium. ACE2 gene expression was lowest (mean log2 counts per million, 2.40; 95% CI, 2.07-2.72) in younger children (n = 45) and increased with age, with mean log2 counts per million of 2.77 (95% CI, 2.64-2.90) for older children (n = 185), 3.02 (95% CI, 2.78-3.26) for young adults (n = 46), and 3.09 (95% CI, 2.83-3.35) for adults (n = 29). PMID:32432657
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<p>The present study explored the signaling mechanism by which ACE2 is regulated under hypertensive conditions. Real-time PCR and immunohistochemistry showed that ACE2 mRNA and protein expression levels were high, whereas ACE expression levels were moderate in both normal kidney and heart. In contrast, patients with hypertension showed marked ACE up-regulation and ACE2 down-regulation in both hypertensive cardiopathy and, particularly, hypertensive nephropathy. PMID:18403595
ACE2 and ACE mRNA levels were measured by real-time PCR in laser microdissected renal biopsies from 13 diabetic and 8 control patients. ACE2 mRNA was significantly reduced by more than half in both the glomeruli and proximal tubules of the diabetic patients compared to controls, but ACE mRNA was increased in both compartments. PMID:19034303
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