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<?xml version='1.0' encoding='utf-8'?>
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/></rdf:Bag></bqbiol:isDescribedBy></rdf:Description></rdf:RDF></annotation></qual:qualitativeSpecies><qual:qualitativeSpecies qual:compartment="comp1" qual:constant="true" qual:id="sa26" qual:maxLevel="1" qual:name="Lisinopril_drug_c1"><annotation><rdf:RDF><rdf:Description rdf:about="#s25"><bqbiol:isDescribedBy><rdf:Bag><rdf:li rdf:resource="urn:casq:function:Lisinopril_drug" /></rdf:Bag></bqbiol:isDescribedBy><bqbiol:isDescribedBy><rdf:Bag><rdf:li rdf:resource="urn:casq:cdid:s25" /></rdf:Bag></bqbiol:isDescribedBy></rdf:Description></rdf:RDF></annotation></qual:qualitativeSpecies><qual:qualitativeSpecies qual:compartment="comp1" qual:constant="true" qual:id="sa28" qual:maxLevel="1" qual:name="CGP42112A_drug"><annotation><rdf:RDF><rdf:Description rdf:about="#s22"><bqbiol:isDescribedBy><rdf:Bag><rdf:li rdf:resource="urn:casq:function:CGP42112A_drug" /></rdf:Bag></bqbiol:isDescribedBy><bqbiol:isDescribedBy><rdf:Bag><rdf:li rdf:resource="urn:casq:cdid:s22" /></rdf:Bag></bqbiol:isDescribedBy></rdf:Description></rdf:RDF></annotation></qual:qualitativeSpecies></qual:listOfQualitativeSpecies><qual:listOfTransitions><qual:transition qual:id="tr_sa2"><qual:listOfInputs><qual:input qual:id="tr_sa2_in_0" qual:qualitativeSpecies="sa17" qual:sign="negative" qual:transitionEffect="none" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:id="tr_sa2_out" qual:qualitativeSpecies="sa2" qual:transitionEffect="assignmentLevel" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><eq /><ci>sa17</ci><cn type="integer">0</cn></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body><p>In wild-type mice, inhibition of 1,25-dihydroxyvitamin D(3) [1,25(OH)(2)D(3)] synthesis also led to an increase in renin expression, whereas 1,25(OH)(2)D(3) injection led to renin suppression. PMID:12122115
</p>
</body></html></notes></qual:transition><qual:transition qual:id="tr_sa3"><qual:listOfInputs><qual:input qual:id="tr_sa3_in_0" qual:qualitativeSpecies="sa1" qual:sign="positive" qual:transitionEffect="none" /><qual:input qual:id="tr_sa3_in_1" qual:qualitativeSpecies="sa2" qual:sign="positive" qual:transitionEffect="none" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:id="tr_sa3_out" qual:qualitativeSpecies="sa3" qual:transitionEffect="assignmentLevel" /></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>sa1</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa2</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>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>
</body></html></notes></qual:transition><qual:transition qual:id="tr_sa4"><qual:listOfInputs><qual:input qual:id="tr_sa4_in_0" qual:qualitativeSpecies="sa3" qual:sign="positive" qual:transitionEffect="none" /><qual:input qual:id="tr_sa4_in_1" qual:qualitativeSpecies="sa5" qual:sign="positive" qual:transitionEffect="none" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:id="tr_sa4_out" qual:qualitativeSpecies="sa4" qual:transitionEffect="assignmentLevel" /></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>sa3</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa5</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 angiotensin I converting enzyme has two important functions: it inactivates bradykinin and converts angiotensin I to angiotensin II. PMID:190881
</p>
</body></html></notes></qual:transition><qual:transition qual:id="tr_sa5"><qual:listOfInputs><qual:input qual:id="tr_sa5_in_0" qual:qualitativeSpecies="sa6" qual:sign="positive" qual:transitionEffect="none" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:id="tr_sa5_out" qual:qualitativeSpecies="sa5" qual:transitionEffect="assignmentLevel" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><eq /><ci>sa6</ci><cn type="integer">1</cn></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body><p>We studied the efficacy of the ACE inhibitor lisinopril in treating overt proteinuria in comparison with the NSAID indomethacin, and evaluated some of the conditions that could influence this antiproteinuric effect. PMID: 2550696
</p>
</body></html></notes></qual:transition><qual:transition qual:id="tr_sa12"><qual:listOfInputs><qual:input qual:id="tr_sa12_in_0" qual:qualitativeSpecies="sa3" qual:sign="positive" qual:transitionEffect="none" /><qual:input qual:id="tr_sa12_in_1" qual:qualitativeSpecies="sa14" qual:sign="positive" qual:transitionEffect="none" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:id="tr_sa12_out" qual:qualitativeSpecies="sa12" qual:transitionEffect="assignmentLevel" /></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>sa3</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa14</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
</p>
</body></html></notes></qual:transition><qual:transition qual:id="tr_sa14"><qual:listOfInputs><qual:input qual:id="tr_sa14_in_0" qual:qualitativeSpecies="sa18" qual:sign="positive" qual:transitionEffect="none" /><qual:input qual:id="tr_sa14_in_1" qual:qualitativeSpecies="sa22" qual:sign="positive" qual:transitionEffect="none" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:id="tr_sa14_out" qual:qualitativeSpecies="sa14" qual:transitionEffect="assignmentLevel" /></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><eq /><ci>sa18</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa22</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>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
</p>
<p>Several lines of evidence indicate that Ang-II–induced ACE2 internalization and lysosomal degradation are mediated by AT1R. First, this effect is blocked by the AT1R blocker losartan. PMID:25225202  
</p>
</body></html></notes></qual:transition><qual:transition qual:id="tr_sa15"><qual:listOfInputs><qual:input qual:id="tr_sa15_in_0" qual:qualitativeSpecies="sa12" qual:sign="positive" qual:transitionEffect="none" /><qual:input qual:id="tr_sa15_in_1" qual:qualitativeSpecies="sa25" qual:sign="positive" qual:transitionEffect="none" /><qual:input qual:id="tr_sa15_in_2" qual:qualitativeSpecies="sa4" qual:sign="positive" qual:transitionEffect="none" /><qual:input qual:id="tr_sa15_in_3" qual:qualitativeSpecies="sa14" qual:sign="positive" qual:transitionEffect="none" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:id="tr_sa15_out" qual:qualitativeSpecies="sa15" qual:transitionEffect="assignmentLevel" /></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>sa12</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa25</ci><cn type="integer">1</cn></apply></apply><apply><and /><apply><eq /><ci>sa4</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa14</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>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
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</body></html></notes></qual:transition><qual:transition qual:id="tr_sa19"><qual:listOfInputs><qual:input qual:id="tr_sa19_in_0" qual:qualitativeSpecies="sa4" qual:sign="positive" qual:transitionEffect="none" /><qual:input qual:id="tr_sa19_in_1" qual:qualitativeSpecies="sa22" qual:sign="positive" qual:transitionEffect="none" /><qual:input qual:id="tr_sa19_in_2" qual:qualitativeSpecies="sa14" qual:sign="positive" qual:transitionEffect="none" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:id="tr_sa19_out" qual:qualitativeSpecies="sa19" qual:transitionEffect="assignmentLevel" /></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><eq /><ci>sa4</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa22</ci><cn type="integer">1</cn></apply><apply><and /><apply><eq /><ci>sa14</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa4</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 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 
</p>
<p>Native Xenopus lung preparations were used for Ussing chamber recordings and apically applied ANGII (10μM) induced a significant increase of short-circuit current (ISC: 8±2%, n=13). Pre-incubation with losartan (LOS), an antagonist of ATR1 prevented the effect of ANGII on ISC. PMID:24530803
</p>
<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 
</p>
</body></html></notes></qual:transition><qual:transition qual:id="tr_sa20"><qual:listOfInputs><qual:input qual:id="tr_sa20_in_0" qual:qualitativeSpecies="sa4" qual:sign="positive" qual:transitionEffect="none" /><qual:input qual:id="tr_sa20_in_1" qual:qualitativeSpecies="sa28" qual:sign="positive" qual:transitionEffect="none" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:id="tr_sa20_out" qual:qualitativeSpecies="sa20" qual:transitionEffect="assignmentLevel" /></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><eq /><ci>sa4</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa28</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>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 
</p>
<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 
</p>
</body></html></notes></qual:transition><qual:transition qual:id="tr_sa21"><qual:listOfInputs><qual:input qual:id="tr_sa21_in_0" qual:qualitativeSpecies="sa15" qual:sign="positive" qual:transitionEffect="none" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:id="tr_sa21_out" qual:qualitativeSpecies="sa21" qual:transitionEffect="assignmentLevel" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><eq /><ci>sa15</ci><cn type="integer">1</cn></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body><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
</p>
</body></html></notes></qual:transition><qual:transition qual:id="tr_sa24"><qual:listOfInputs><qual:input qual:id="tr_sa24_in_0" qual:qualitativeSpecies="sa21" qual:sign="positive" qual:transitionEffect="none" /><qual:input qual:id="tr_sa24_in_1" qual:qualitativeSpecies="sa20" qual:sign="positive" qual:transitionEffect="none" /><qual:input qual:id="tr_sa24_in_2" qual:qualitativeSpecies="sa19" qual:sign="positive" qual:transitionEffect="none" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:id="tr_sa24_out" qual:qualitativeSpecies="sa24" qual:transitionEffect="assignmentLevel" /></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><eq /><ci>sa21</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa20</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa19</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 Mas receptor has also been implicated in the reduction of blood pressure by angiotensin 1-7, and a possible reduction of Mas receptors in the kidney of streptozotocin-induced diabetic rats could be responsible for its lack of response to angiotensin 1-7.PMID:17320855
</p>
<p>AT1R stimulation results in blood pressure elevation, whereas AT2R lowers blood pressure. DOI:10.1530/ERC-19-0314
</p>
<p>AT1R stimulation results in blood pressure elevation, whereas AT2R lowers blood pressure. DOI:10.1530/ERC-19-0314
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</body></html></notes></qual:transition><qual:transition qual:id="tr_sa25"><qual:listOfInputs><qual:input qual:id="tr_sa25_in_0" qual:qualitativeSpecies="sa26" qual:sign="positive" qual:transitionEffect="none" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:id="tr_sa25_out" qual:qualitativeSpecies="sa25" qual:transitionEffect="assignmentLevel" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><eq /><ci>sa26</ci><cn type="integer">1</cn></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body><p>We studied the efficacy of the ACE inhibitor lisinopril in treating overt proteinuria in comparison with the NSAID indomethacin, and evaluated some of the conditions that could influence this antiproteinuric effect. PMID: 2550696
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