New perspectives in the renin-angiotensin-aldosterone system (RAAS) II: albumin suppresses angiotensin converting enzyme (ACE) activity in human.

About 8% of the adult population is taking angiotensin-converting enzyme (ACE) inhibitors to treat cardiovascular disease including hypertension, myocardial infarction and heart failure. These drugs decrease mortality by up to one-fifth in these patients. We and others have reported previously that...

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Autores principales:	Miklós Fagyas, Katalin Úri, Ivetta M Siket, Gábor Á Fülöp, Viktória Csató, Andrea Daragó, Judit Boczán, Emese Bányai, István Elek Szentkirályi, Tamás Miklós Maros, Tamás Szerafin, István Édes, Zoltán Papp, Attila Tóth
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/78a9276d4d164f108c0af1165f2aca3a
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spelling	oai:doaj.org-article:78a9276d4d164f108c0af1165f2aca3a2021-11-18T08:25:29ZNew perspectives in the renin-angiotensin-aldosterone system (RAAS) II: albumin suppresses angiotensin converting enzyme (ACE) activity in human.1932-620310.1371/journal.pone.0087844https://doaj.org/article/78a9276d4d164f108c0af1165f2aca3a2014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24691203/?tool=EBIhttps://doaj.org/toc/1932-6203About 8% of the adult population is taking angiotensin-converting enzyme (ACE) inhibitors to treat cardiovascular disease including hypertension, myocardial infarction and heart failure. These drugs decrease mortality by up to one-fifth in these patients. We and others have reported previously that endogenous inhibitory substances suppress serum ACE activity, in vivo, similarly to the ACE inhibitor drugs. Here we have made an effort to identify this endogenous ACE inhibitor substance. ACE was crosslinked with interacting proteins in human sera. The crosslinked products were immunoprecipitated and subjected to Western blot. One of the crosslinked products was recognized by both anti-ACE and anti-HSA (human serum albumin) antibodies. Direct ACE-HSA interaction was confirmed by binding assays using purified ACE and HSA. HSA inhibited human purified (circulating) and human recombinant ACE with potencies (IC50) of 5.7 ± 0.7 and 9.5 ± 1.1 mg/mL, respectively. Effects of HSA on the tissue bound native ACE were tested on human saphenous vein samples. Angiotensin I evoked vasoconstriction was inhibited by HSA in this vascular tissue (maximal force with HSA: 6.14 ± 1.34 mN, without HSA: 13.54 ± 2.63 mN), while HSA was without effects on angiotensin II mediated constrictions (maximal force with HSA: 18.73 ± 2.17 mN, without HSA: 19.22 ± 3.50 mN). The main finding of this study is that HSA was identified as a potent physiological inhibitor of the ACE. The enzymatic activity of ACE appears to be almost completely suppressed by HSA when it is present in its physiological concentration. These data suggest that angiotensin I conversion is limited by low physiological ACE activities, in vivo.Miklós FagyasKatalin ÚriIvetta M SiketGábor Á FülöpViktória CsatóAndrea DaragóJudit BoczánEmese BányaiIstván Elek SzentkirályiTamás Miklós MarosTamás SzerafinIstván ÉdesZoltán PappAttila TóthPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 4, p e87844 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Miklós Fagyas Katalin Úri Ivetta M Siket Gábor Á Fülöp Viktória Csató Andrea Daragó Judit Boczán Emese Bányai István Elek Szentkirályi Tamás Miklós Maros Tamás Szerafin István Édes Zoltán Papp Attila Tóth New perspectives in the renin-angiotensin-aldosterone system (RAAS) II: albumin suppresses angiotensin converting enzyme (ACE) activity in human.
description	About 8% of the adult population is taking angiotensin-converting enzyme (ACE) inhibitors to treat cardiovascular disease including hypertension, myocardial infarction and heart failure. These drugs decrease mortality by up to one-fifth in these patients. We and others have reported previously that endogenous inhibitory substances suppress serum ACE activity, in vivo, similarly to the ACE inhibitor drugs. Here we have made an effort to identify this endogenous ACE inhibitor substance. ACE was crosslinked with interacting proteins in human sera. The crosslinked products were immunoprecipitated and subjected to Western blot. One of the crosslinked products was recognized by both anti-ACE and anti-HSA (human serum albumin) antibodies. Direct ACE-HSA interaction was confirmed by binding assays using purified ACE and HSA. HSA inhibited human purified (circulating) and human recombinant ACE with potencies (IC50) of 5.7 ± 0.7 and 9.5 ± 1.1 mg/mL, respectively. Effects of HSA on the tissue bound native ACE were tested on human saphenous vein samples. Angiotensin I evoked vasoconstriction was inhibited by HSA in this vascular tissue (maximal force with HSA: 6.14 ± 1.34 mN, without HSA: 13.54 ± 2.63 mN), while HSA was without effects on angiotensin II mediated constrictions (maximal force with HSA: 18.73 ± 2.17 mN, without HSA: 19.22 ± 3.50 mN). The main finding of this study is that HSA was identified as a potent physiological inhibitor of the ACE. The enzymatic activity of ACE appears to be almost completely suppressed by HSA when it is present in its physiological concentration. These data suggest that angiotensin I conversion is limited by low physiological ACE activities, in vivo.
format	article
author	Miklós Fagyas Katalin Úri Ivetta M Siket Gábor Á Fülöp Viktória Csató Andrea Daragó Judit Boczán Emese Bányai István Elek Szentkirályi Tamás Miklós Maros Tamás Szerafin István Édes Zoltán Papp Attila Tóth
author_facet	Miklós Fagyas Katalin Úri Ivetta M Siket Gábor Á Fülöp Viktória Csató Andrea Daragó Judit Boczán Emese Bányai István Elek Szentkirályi Tamás Miklós Maros Tamás Szerafin István Édes Zoltán Papp Attila Tóth
author_sort	Miklós Fagyas
title	New perspectives in the renin-angiotensin-aldosterone system (RAAS) II: albumin suppresses angiotensin converting enzyme (ACE) activity in human.
title_short	New perspectives in the renin-angiotensin-aldosterone system (RAAS) II: albumin suppresses angiotensin converting enzyme (ACE) activity in human.
title_full	New perspectives in the renin-angiotensin-aldosterone system (RAAS) II: albumin suppresses angiotensin converting enzyme (ACE) activity in human.
title_fullStr	New perspectives in the renin-angiotensin-aldosterone system (RAAS) II: albumin suppresses angiotensin converting enzyme (ACE) activity in human.
title_full_unstemmed	New perspectives in the renin-angiotensin-aldosterone system (RAAS) II: albumin suppresses angiotensin converting enzyme (ACE) activity in human.
title_sort	new perspectives in the renin-angiotensin-aldosterone system (raas) ii: albumin suppresses angiotensin converting enzyme (ace) activity in human.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/78a9276d4d164f108c0af1165f2aca3a
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New perspectives in the renin-angiotensin-aldosterone system (RAAS) II: albumin suppresses angiotensin converting enzyme (ACE) activity in human.

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