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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Hydrolysis of Angiotensin Peptides by Human Angiotensin I–Converting Enzyme and the Resensitization of B<sub>2</sub> Kinin Receptors</title><author><name sortKey="Chen, Zhenlong" sort="Chen, Zhenlong" uniqKey="Chen Z" first="Zhenlong" last="Chen">Zhenlong Chen</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">16246972</idno><idno type="pmc">1564276</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1564276</idno><idno type="RBID">PMC:1564276</idno><idno type="doi">10.1161/01.HYP.0000188905.20884.63</idno><date when="2005">2005</date><idno type="wicri:Area/Pmc/Corpus">000774</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000774</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Hydrolysis of Angiotensin Peptides by Human Angiotensin I–Converting Enzyme and the Resensitization of B<sub>2</sub> Kinin Receptors</title><author><name sortKey="Chen, Zhenlong" sort="Chen, Zhenlong" uniqKey="Chen Z" first="Zhenlong" last="Chen">Zhenlong Chen</name></author></analytic><series><title level="j">Hypertension</title><idno type="ISSN">0194-911X</idno><idno type="eISSN">1524-4563</idno><imprint><date when="2005">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p id="P1">We measured the cleavage of angiotensin I (Ang I) metabolites by angiotensin I– converting enzyme (ACE) in cultured cells and examined how they augment actions of bradykinin B<sub>2</sub> receptor agonists. Monolayers of Chinese hamster ovary cells transfected to stably express human ACE and bradykinin B<sub>2</sub> receptors coupled to green fluorescent protein (B<sub>2</sub>GFP) or to express only coupled B<sub>2</sub>GFP receptors. We used 2 ACE-resistant bradykinin analogues to activate the B<sub>2</sub> receptors. We used high-performance liquid chromatography to analyze the peptides cleaved by ACE on cell monolayers and found that Ang 1-9 was hydrolyzed 18× slower than Ang I and ≈30% slower than Ang 1-7. Ang 1-7 was cleaved to Ang 1-5. Although μmol/L concentrations of slowly cleaved substrates Ang 1-7 and Ang 1-9 inhibit ACE, they resensitize the desensitized B<sub>2</sub>GFP receptors in nmol/L concentration, independent of ACE inhibition. This is reflected by release of arachidonic acid through a mechanism involving cross-talk between ACE and B<sub>2</sub> receptors. When ACE was not expressed, the Ang 1-9, Ang 1-7 peptides were inactive. Inhibitors of protein kinase C-α, phosphatases and Tyr-kinase blocked this resensitization activity, but not basal B<sub>2</sub> activation by bradykinin. Ang 1-9 and Ang 1-7 enhance bradykinin activity, probably by acting as endogenous allosteric modifiers of the ACE and B<sub>2</sub> receptor complex. Consequently, when ACE inhibitors block conversion of Ang I, other enzymes can still release Ang I metabolites to enhance the efficacy of ACE inhibitors.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
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<front><journal-meta><journal-id journal-id-type="nlm-journal-id">7906255</journal-id><journal-id journal-id-type="pubmed-jr-id">4217</journal-id><journal-id journal-id-type="nlm-ta">Hypertension</journal-id><journal-title>Hypertension</journal-title><issn pub-type="ppub">0194-911X</issn><issn pub-type="epub">1524-4563</issn></journal-meta><article-meta><article-id pub-id-type="pmid">16246972</article-id><article-id pub-id-type="pmc">1564276</article-id><article-id pub-id-type="doi">10.1161/01.HYP.0000188905.20884.63</article-id><article-id pub-id-type="manuscript">NIHMS6405</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>Hydrolysis of Angiotensin Peptides by Human Angiotensin I–Converting Enzyme and the Resensitization of B<sub>2</sub> Kinin Receptors</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Chen</surname><given-names>Zhenlong</given-names></name></contrib><aff id="A1">From the Department of Pharmacology, University of Illinois College of Medicine, Chicago.</aff></contrib-group><contrib-group><contrib contrib-type="author"><name><surname>Tan</surname><given-names>Fulong</given-names></name></contrib><contrib contrib-type="author"><name><surname>Erdös</surname><given-names>Ervin G.</given-names></name></contrib><aff id="A2">From the Departments of Pharmacology and Anesthesiology, University of Illinois College of Medicine, Chicago.</aff></contrib-group><contrib-group><contrib contrib-type="author"><name><surname>Deddish</surname><given-names>Peter A.</given-names></name></contrib><aff id="A3">From the Departments of Pharmacology, Anatomy and Cell Biology, University of Illinois College of Medicine, Chicago.</aff></contrib-group><author-notes><corresp id="CR1">Correspondence to Ervin G. Erdös, MD, Professor, Department of Pharmacology, 835 S Wolcott (MC 868), Chicago, IL 60612. E-mail <email>EGErdos@uic.edu</email></corresp></author-notes><pub-date pub-type="nihms-submitted"><day>5</day><month>9</month><year>2006</year></pub-date><pub-date pub-type="epub"><day>24</day><month>10</month><year>2005</year></pub-date><pub-date pub-type="ppub"><month>12</month><year>2005</year></pub-date><pub-date pub-type="pmc-release"><day>13</day><month>9</month><year>2006</year></pub-date><volume>46</volume><issue>6</issue><fpage>1368</fpage><lpage>1373</lpage><abstract><p id="P1">We measured the cleavage of angiotensin I (Ang I) metabolites by angiotensin I– converting enzyme (ACE) in cultured cells and examined how they augment actions of bradykinin B<sub>2</sub> receptor agonists. Monolayers of Chinese hamster ovary cells transfected to stably express human ACE and bradykinin B<sub>2</sub> receptors coupled to green fluorescent protein (B<sub>2</sub>GFP) or to express only coupled B<sub>2</sub>GFP receptors. We used 2 ACE-resistant bradykinin analogues to activate the B<sub>2</sub> receptors. We used high-performance liquid chromatography to analyze the peptides cleaved by ACE on cell monolayers and found that Ang 1-9 was hydrolyzed 18× slower than Ang I and ≈30% slower than Ang 1-7. Ang 1-7 was cleaved to Ang 1-5. Although μmol/L concentrations of slowly cleaved substrates Ang 1-7 and Ang 1-9 inhibit ACE, they resensitize the desensitized B<sub>2</sub>GFP receptors in nmol/L concentration, independent of ACE inhibition. This is reflected by release of arachidonic acid through a mechanism involving cross-talk between ACE and B<sub>2</sub> receptors. When ACE was not expressed, the Ang 1-9, Ang 1-7 peptides were inactive. Inhibitors of protein kinase C-α, phosphatases and Tyr-kinase blocked this resensitization activity, but not basal B<sub>2</sub> activation by bradykinin. Ang 1-9 and Ang 1-7 enhance bradykinin activity, probably by acting as endogenous allosteric modifiers of the ACE and B<sub>2</sub> receptor complex. Consequently, when ACE inhibitors block conversion of Ang I, other enzymes can still release Ang I metabolites to enhance the efficacy of ACE inhibitors.</p></abstract><kwd-group><kwd>angiotensin</kwd><kwd>angiotensin-converting enzyme</kwd><kwd>bradykinin</kwd><kwd>enalapril</kwd><kwd>protein kinases</kwd></kwd-group><contract-num rid="HL1">R01 HL068580-04</contract-num><contract-num rid="HL1">R01 HL068580-03</contract-num><contract-num rid="HL1">R01 HL068580-02</contract-num><contract-num rid="HL1">R01 HL068580-01</contract-num><contract-num rid="HL1">R01 HL036473-20</contract-num><contract-num rid="HL1">R01 HL036473-19</contract-num><contract-num rid="HL1">R01 HL036473-18</contract-num><contract-num rid="HL1">R01 HL036473-17</contract-num><contract-sponsor id="HL1">National Heart, Lung, and Blood Institute : NHLBI</contract-sponsor></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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