Discrepancy Between Plasma and Lung Angiotensin-Converting Enzyme Activity in Experimental Congestive Heart Failure A Novel Aspect of Endothelium Dysfunction
The renin-angiotensin and cardiac natriuretic systems play an important role in the pathophysiology of congestive heart failure (CHF). The status of the membrane-bound pulmonary and renal activities of three ectoenzymes involved in the regulation of these systems — angiotensin-converting enzyme (ACE...
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| Veröffentlicht in: | Circulation research 1994-09, Vol.75 (3), p.454-461 |
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| creator | Huang, Huaming Arnal, Jean-François Llorens-Cortes, Catherine Challah, Mireille Alhenc-Gelas, François Corvol, Pierre Michel, Jean-Baptiste |
| description | The renin-angiotensin and cardiac natriuretic systems play an important role in the pathophysiology of congestive heart failure (CHF). The status of the membrane-bound pulmonary and renal activities of three ectoenzymes involved in the regulation of these systems — angiotensin-converting enzyme (ACE), neutral endopeptidase (NEP), and aminopeptidase A (APA) —was investigated in Wistar rats 3 months after induction of myocardial infarction (MI) and in sham-operated (control) rats. Plasma renin activity and ACE activity, plasma angiotensin II (Ang II) levels, and atrial natriuretic factor levels were simultaneously determined. The lung ACE activity was decreased in MI rats compared with control rats (P |
| doi_str_mv | 10.1161/01.RES.75.3.454 |
| format | Article |
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The status of the membrane-bound pulmonary and renal activities of three ectoenzymes involved in the regulation of these systems — angiotensin-converting enzyme (ACE), neutral endopeptidase (NEP), and aminopeptidase A (APA) —was investigated in Wistar rats 3 months after induction of myocardial infarction (MI) and in sham-operated (control) rats. Plasma renin activity and ACE activity, plasma angiotensin II (Ang II) levels, and atrial natriuretic factor levels were simultaneously determined. The lung ACE activity was decreased in MI rats compared with control rats (P<.0001), and this decrease depended on the severity of the heart failure. In contrast, plasma ACE activity was increased in MI rats (P<.01), and this increase was also proportional to the severity of MI. Northern blot analysis showed that the lung ACE mRNA level in severe MI rats was half that of the control rats. Renal ACE activity of the MI rats was not affected, and neither renal or pulmonary NEP nor pulmonary APA activities were altered. Thus, lung ACE gene expression appears to be both organ- and enzyme-specifically regulated during CHF. Whereas plasma renin was increased in heart failure rats, plasma Ang II levels were not different from those of control rats. Thus, decreased lung ACE activity could possibly contribute to keeping plasma Ang II levels in the normal range. The decrease in lung ACE activity and mRNA levels, combined with increased plasma ACE activity, represents a novel aspect of endothelial dysfunction in CHF. This dissociation between the membrane-bound endothelial enzyme and its circulating counterpart emphasizes the importance of simultaneously assessing the circulating and tissue components of the renin-angiotensin system in heart failure.</description><identifier>ISSN: 0009-7330</identifier><identifier>EISSN: 1524-4571</identifier><identifier>DOI: 10.1161/01.RES.75.3.454</identifier><identifier>PMID: 8062419</identifier><identifier>CODEN: CIRUAL</identifier><language>eng</language><publisher>United States: American Heart Association, Inc</publisher><subject>Analysis of Variance ; Angiotensin II - blood ; Animals ; Atrial Natriuretic Factor - blood ; Cell Membrane - enzymology ; Disease Models, Animal ; Endothelium, Vascular - physiopathology ; Gene Expression ; Heart - physiopathology ; Heart Failure - blood ; Heart Failure - enzymology ; Heart Failure - physiopathology ; Kidney - enzymology ; Lung - enzymology ; Male ; Myocardial Infarction - blood ; Myocardial Infarction - enzymology ; Myocardial Infarction - physiopathology ; Organ Size ; Peptidyl-Dipeptidase A - biosynthesis ; Peptidyl-Dipeptidase A - blood ; Peptidyl-Dipeptidase A - metabolism ; Pleural Effusion ; Rats ; Rats, Wistar ; Renin - blood ; RNA, Messenger - metabolism</subject><ispartof>Circulation research, 1994-09, Vol.75 (3), p.454-461</ispartof><rights>1994 American Heart Association, Inc.</rights><rights>Copyright American Heart Association, Inc. Sep 1994</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4417-c20b28b4b20540a420c8565636f1923f7dc94109995bc5e06fb239591c0f57a33</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,3675,27906,27907</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8062419$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Huang, Huaming</creatorcontrib><creatorcontrib>Arnal, Jean-François</creatorcontrib><creatorcontrib>Llorens-Cortes, Catherine</creatorcontrib><creatorcontrib>Challah, Mireille</creatorcontrib><creatorcontrib>Alhenc-Gelas, François</creatorcontrib><creatorcontrib>Corvol, Pierre</creatorcontrib><creatorcontrib>Michel, Jean-Baptiste</creatorcontrib><title>Discrepancy Between Plasma and Lung Angiotensin-Converting Enzyme Activity in Experimental Congestive Heart Failure A Novel Aspect of Endothelium Dysfunction</title><title>Circulation research</title><addtitle>Circ Res</addtitle><description>The renin-angiotensin and cardiac natriuretic systems play an important role in the pathophysiology of congestive heart failure (CHF). The status of the membrane-bound pulmonary and renal activities of three ectoenzymes involved in the regulation of these systems — angiotensin-converting enzyme (ACE), neutral endopeptidase (NEP), and aminopeptidase A (APA) —was investigated in Wistar rats 3 months after induction of myocardial infarction (MI) and in sham-operated (control) rats. Plasma renin activity and ACE activity, plasma angiotensin II (Ang II) levels, and atrial natriuretic factor levels were simultaneously determined. The lung ACE activity was decreased in MI rats compared with control rats (P<.0001), and this decrease depended on the severity of the heart failure. In contrast, plasma ACE activity was increased in MI rats (P<.01), and this increase was also proportional to the severity of MI. Northern blot analysis showed that the lung ACE mRNA level in severe MI rats was half that of the control rats. Renal ACE activity of the MI rats was not affected, and neither renal or pulmonary NEP nor pulmonary APA activities were altered. Thus, lung ACE gene expression appears to be both organ- and enzyme-specifically regulated during CHF. Whereas plasma renin was increased in heart failure rats, plasma Ang II levels were not different from those of control rats. Thus, decreased lung ACE activity could possibly contribute to keeping plasma Ang II levels in the normal range. The decrease in lung ACE activity and mRNA levels, combined with increased plasma ACE activity, represents a novel aspect of endothelial dysfunction in CHF. This dissociation between the membrane-bound endothelial enzyme and its circulating counterpart emphasizes the importance of simultaneously assessing the circulating and tissue components of the renin-angiotensin system in heart failure.</description><subject>Analysis of Variance</subject><subject>Angiotensin II - blood</subject><subject>Animals</subject><subject>Atrial Natriuretic Factor - blood</subject><subject>Cell Membrane - enzymology</subject><subject>Disease Models, Animal</subject><subject>Endothelium, Vascular - physiopathology</subject><subject>Gene Expression</subject><subject>Heart - physiopathology</subject><subject>Heart Failure - blood</subject><subject>Heart Failure - enzymology</subject><subject>Heart Failure - physiopathology</subject><subject>Kidney - enzymology</subject><subject>Lung - enzymology</subject><subject>Male</subject><subject>Myocardial Infarction - blood</subject><subject>Myocardial Infarction - enzymology</subject><subject>Myocardial Infarction - physiopathology</subject><subject>Organ Size</subject><subject>Peptidyl-Dipeptidase A - biosynthesis</subject><subject>Peptidyl-Dipeptidase A - blood</subject><subject>Peptidyl-Dipeptidase A - metabolism</subject><subject>Pleural Effusion</subject><subject>Rats</subject><subject>Rats, Wistar</subject><subject>Renin - blood</subject><subject>RNA, Messenger - metabolism</subject><issn>0009-7330</issn><issn>1524-4571</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkUtvEzEUhUcIVEJhzQrJYsFuUj9nxsuQphQpAsRjbXmcO8kUj53anoThv_S_1lUiFqws3_Pdo6N7iuItwXNCKnKFyfz76se8FnM254I_K2ZEUF5yUZPnxQxjLMuaMfyyeBXjHcaEMyoviosGV5QTOSservtoAuy1MxP6COkI4NA3q-OgkXYbtB7dFi3ctvcJXOxdufTuACH1ebxyf6cB0MKk_tCnCfUOrf7sIfQDuKQtyugWYhYB3YIOCd3o3o4hb6Av_gAWLeIeTEK-y1Ybn3Zg-3FA11PsRpdNvXtdvOi0jfDm_F4Wv25WP5e35frrp8_Lxbo0nJO6NBS3tGl5S7HgWHOKTSMqUbGqI5Kyrt4YyQmWUorWCMBV11ImhSQGd6LWjF0WH06---Dvx5xZDfksYK124Meo6qqqeVM1GXz_H3jnx-ByNkUJ5VhWDc3Q1QkywccYoFP7fBMdJkWwempNYaJya6oWiqncWt54d7Yd2wE2__hzTVnnJ_3obYIQf9vxCEHtQNu0U7llzDChJZEyR8i_8mlUs0dyV6Mx</recordid><startdate>199409</startdate><enddate>199409</enddate><creator>Huang, Huaming</creator><creator>Arnal, Jean-François</creator><creator>Llorens-Cortes, Catherine</creator><creator>Challah, Mireille</creator><creator>Alhenc-Gelas, François</creator><creator>Corvol, Pierre</creator><creator>Michel, Jean-Baptiste</creator><general>American Heart Association, Inc</general><general>Lippincott Williams & Wilkins Ovid Technologies</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QP</scope><scope>7T5</scope><scope>7TK</scope><scope>H94</scope><scope>K9.</scope><scope>7X8</scope></search><sort><creationdate>199409</creationdate><title>Discrepancy Between Plasma and Lung Angiotensin-Converting Enzyme Activity in Experimental Congestive Heart Failure A Novel Aspect of Endothelium Dysfunction</title><author>Huang, Huaming ; Arnal, Jean-François ; Llorens-Cortes, Catherine ; Challah, Mireille ; Alhenc-Gelas, François ; Corvol, Pierre ; Michel, Jean-Baptiste</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4417-c20b28b4b20540a420c8565636f1923f7dc94109995bc5e06fb239591c0f57a33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Analysis of Variance</topic><topic>Angiotensin II - blood</topic><topic>Animals</topic><topic>Atrial Natriuretic Factor - blood</topic><topic>Cell Membrane - enzymology</topic><topic>Disease Models, Animal</topic><topic>Endothelium, Vascular - physiopathology</topic><topic>Gene Expression</topic><topic>Heart - physiopathology</topic><topic>Heart Failure - blood</topic><topic>Heart Failure - enzymology</topic><topic>Heart Failure - physiopathology</topic><topic>Kidney - enzymology</topic><topic>Lung - enzymology</topic><topic>Male</topic><topic>Myocardial Infarction - blood</topic><topic>Myocardial Infarction - enzymology</topic><topic>Myocardial Infarction - physiopathology</topic><topic>Organ Size</topic><topic>Peptidyl-Dipeptidase A - biosynthesis</topic><topic>Peptidyl-Dipeptidase A - blood</topic><topic>Peptidyl-Dipeptidase A - metabolism</topic><topic>Pleural Effusion</topic><topic>Rats</topic><topic>Rats, Wistar</topic><topic>Renin - blood</topic><topic>RNA, Messenger - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Huang, Huaming</creatorcontrib><creatorcontrib>Arnal, Jean-François</creatorcontrib><creatorcontrib>Llorens-Cortes, Catherine</creatorcontrib><creatorcontrib>Challah, Mireille</creatorcontrib><creatorcontrib>Alhenc-Gelas, François</creatorcontrib><creatorcontrib>Corvol, Pierre</creatorcontrib><creatorcontrib>Michel, Jean-Baptiste</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>MEDLINE - Academic</collection><jtitle>Circulation research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Huang, Huaming</au><au>Arnal, Jean-François</au><au>Llorens-Cortes, Catherine</au><au>Challah, Mireille</au><au>Alhenc-Gelas, François</au><au>Corvol, Pierre</au><au>Michel, Jean-Baptiste</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Discrepancy Between Plasma and Lung Angiotensin-Converting Enzyme Activity in Experimental Congestive Heart Failure A Novel Aspect of Endothelium Dysfunction</atitle><jtitle>Circulation research</jtitle><addtitle>Circ Res</addtitle><date>1994-09</date><risdate>1994</risdate><volume>75</volume><issue>3</issue><spage>454</spage><epage>461</epage><pages>454-461</pages><issn>0009-7330</issn><eissn>1524-4571</eissn><coden>CIRUAL</coden><abstract>The renin-angiotensin and cardiac natriuretic systems play an important role in the pathophysiology of congestive heart failure (CHF). The status of the membrane-bound pulmonary and renal activities of three ectoenzymes involved in the regulation of these systems — angiotensin-converting enzyme (ACE), neutral endopeptidase (NEP), and aminopeptidase A (APA) —was investigated in Wistar rats 3 months after induction of myocardial infarction (MI) and in sham-operated (control) rats. Plasma renin activity and ACE activity, plasma angiotensin II (Ang II) levels, and atrial natriuretic factor levels were simultaneously determined. The lung ACE activity was decreased in MI rats compared with control rats (P<.0001), and this decrease depended on the severity of the heart failure. In contrast, plasma ACE activity was increased in MI rats (P<.01), and this increase was also proportional to the severity of MI. Northern blot analysis showed that the lung ACE mRNA level in severe MI rats was half that of the control rats. Renal ACE activity of the MI rats was not affected, and neither renal or pulmonary NEP nor pulmonary APA activities were altered. Thus, lung ACE gene expression appears to be both organ- and enzyme-specifically regulated during CHF. Whereas plasma renin was increased in heart failure rats, plasma Ang II levels were not different from those of control rats. Thus, decreased lung ACE activity could possibly contribute to keeping plasma Ang II levels in the normal range. The decrease in lung ACE activity and mRNA levels, combined with increased plasma ACE activity, represents a novel aspect of endothelial dysfunction in CHF. This dissociation between the membrane-bound endothelial enzyme and its circulating counterpart emphasizes the importance of simultaneously assessing the circulating and tissue components of the renin-angiotensin system in heart failure.</abstract><cop>United States</cop><pub>American Heart Association, Inc</pub><pmid>8062419</pmid><doi>10.1161/01.RES.75.3.454</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Circulation research, 1994-09, Vol.75 (3), p.454-461 |
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| language | eng |
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| source | MEDLINE; American Heart Association; Journals@Ovid Complete; EZB-FREE-00999 freely available EZB journals |
| subjects | Analysis of Variance Angiotensin II - blood Animals Atrial Natriuretic Factor - blood Cell Membrane - enzymology Disease Models, Animal Endothelium, Vascular - physiopathology Gene Expression Heart - physiopathology Heart Failure - blood Heart Failure - enzymology Heart Failure - physiopathology Kidney - enzymology Lung - enzymology Male Myocardial Infarction - blood Myocardial Infarction - enzymology Myocardial Infarction - physiopathology Organ Size Peptidyl-Dipeptidase A - biosynthesis Peptidyl-Dipeptidase A - blood Peptidyl-Dipeptidase A - metabolism Pleural Effusion Rats Rats, Wistar Renin - blood RNA, Messenger - metabolism |
| title | Discrepancy Between Plasma and Lung Angiotensin-Converting Enzyme Activity in Experimental Congestive Heart Failure A Novel Aspect of Endothelium Dysfunction |
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