Purification and characterization of angiotensin converting enzyme 2 (ACE2) from murine model of mesangial cell in culture

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dc.contributor.authorAragao, Danielle Sanches [UNIFESP]
dc.contributor.authorCunha, Tatiana de Sousa [UNIFESP]
dc.contributor.authorArita, Danielle Yuri [UNIFESP]
dc.contributor.authorAndrade, Maria Claudina Camargo de [UNIFESP]
dc.contributor.authorFernandes, Adriana Barrinha [UNIFESP]
dc.contributor.authorWatanabe, Ingrid Kazue Mizuno [UNIFESP]
dc.contributor.authorMortara, Renato Arruda [UNIFESP]
dc.contributor.authorCasarini, Dulce Elena [UNIFESP]
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2016-01-24T14:16:54Z
dc.date.available2016-01-24T14:16:54Z
dc.date.issued2011-07-01
dc.description.abstractAngiotensin converting enzyme 2 (ACE2) is a component of the renin-angiotensin system (RAS) which converts Ang II, a potent vasoconstrictor peptide into Ang 1-7, a vasodilator peptide which may act as a negative feedback hormone to the actions of Ang II. the discovery of this enzyme added a new level of complexity to this system. the mesangial cells (MC) have multiple functions in glomerular physiology and pathophysiology and are able to express all components of the RAS. Despite of being localized in these cells, ACE2 has not yet been purified or characterized. in this study ACE2 from mice immortalized MC (IMC) was purified by ion-exchange chromatography. the purified enzyme was identified as a single band around 60-70 kDa on SDS-polyacrylamide gel and by Western blotting using a specific antibody. the optima pH and chloride concentrations were 7.5 and 200 mM, respectively. the N-terminal sequence was homologous with many species ACE2 N-terminal sequences as described in the literature. ACE2 purified from IMC was able to hydrolyze Ang II into Ang 1-7 and the K(m) value for Ang II was determined to be 2.87 +/- 0.76 mu M. in conclusion, we purified and localized, for the first time, ACE2 in MC, which was able to generate Ang 1-7 from Ang II. Ang 1-7 production associated to Ang II degradation by ACE2 may exert a protective effect in the renal hemodynamic. (C) 2011 Elsevier B.V. All rights reserved.en
dc.description.affiliationUniversidade Federal de São Paulo, Div Nephrol, Dept Med, BR-04023900 São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Immunol & Parasitol Div, BR-04023900 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Div Nephrol, Dept Med, BR-04023900 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Immunol & Parasitol Div, BR-04023900 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipIDFAPESP: 05-57543-0
dc.format.extent79-84
dc.identifierhttp://dx.doi.org/10.1016/j.ijbiomac.2011.03.018
dc.identifier.citationInternational Journal of Biological Macromolecules. Amsterdam: Elsevier B.V., v. 49, n. 1, p. 79-84, 2011.
dc.identifier.doi10.1016/j.ijbiomac.2011.03.018
dc.identifier.fileWOS000291840400012.pdf
dc.identifier.issn0141-8130
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/33814
dc.identifier.wosWOS:000291840400012
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofInternational Journal of Biological Macromolecules
dc.rightsinfo:eu-repo/semantics/openAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectACE2en
dc.subjectMesangial cellsen
dc.subjectRenin-angiotensin systemen
dc.titlePurification and characterization of angiotensin converting enzyme 2 (ACE2) from murine model of mesangial cell in cultureen
dc.typeinfo:eu-repo/semantics/article
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