Serine proteases as candidates for proteolytic processing of angiotensin-I converting enzyme

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dc.contributor.author Aragao, Danielle S. [UNIFESP]
dc.contributor.author Andrade, Maria Claudina C. de
dc.contributor.author Ebihara, Fabiana [UNIFESP]
dc.contributor.author Watanabe, Ingrid K. M. [UNIFESP]
dc.contributor.author Magalhaes, Dayane C. B. P. [UNIFESP]
dc.contributor.author Juliano, Maria Aparecida [UNIFESP]
dc.contributor.author Hirata, Izaura Yoshico [UNIFESP]
dc.contributor.author Casarini, Dulce Elena [UNIFESP]
dc.date.accessioned 2016-01-24T14:39:49Z
dc.date.available 2016-01-24T14:39:49Z
dc.date.issued 2015-01-01
dc.identifier http://dx.doi.org/10.1016/j.ijbiomac.2014.09.017
dc.identifier.citation International Journal of Biological Macromolecules. Amsterdam: Elsevier B.V., v. 72, p. 673-679, 2015.
dc.identifier.issn 0141-8130
dc.identifier.uri http://repositorio.unifesp.br/handle/11600/38585
dc.description.abstract Somatic angiotensin-I converting enzyme (sACE) is a broadly distributed peptidase which plays a role in blood pressure and electrolyte homeostasis by the conversion of angiotensin I into angiotensin II. N-domain isoforms (nACE) with 65 and 90 kDa have been described in body fluids, tissues and mesangial cells (MC), and a 90 kDa nACE has been described only in spontaneously hypertensive rats. the aim of this study was to investigate the existence of proteolytic enzymes that may act in the hydrolysis of sACE generating nACEs in MC. After the confirmation of the presence of ACE sheddases in Immortalized MC (IMC), we purified and characterized these enzymes using fluorogenic substrates specifically designed for ACE sheddases. Purified enzyme identified as a serine protease by N-terminal sequence was able to generate nACE. in the present study, we described for the first time the presence of ACE sheddases in IMC, identified as serine proteases able to hydrolyze sACE in vitro. Further investigations are necessary to elucidate the mechanisms responsible for the expression and regulation of ACE sheddases in MC and their roles in the generation of nACEs, especially the 90 kDa form possibly related to hypertension. (C) 2014 Elsevier B.V. All rights reserved. en
dc.description.sponsorship Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.format.extent 673-679
dc.language.iso eng
dc.publisher Elsevier B.V.
dc.relation.ispartof International Journal of Biological Macromolecules
dc.rights Acesso restrito
dc.subject Angiotensin-I converting enzyme en
dc.subject Shedding, Mesangial cells en
dc.title Serine proteases as candidates for proteolytic processing of angiotensin-I converting enzyme en
dc.type Artigo
dc.rights.license http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.contributor.institution Universidade Federal de São Paulo (UNIFESP)
dc.description.affiliation Universidade Federal de São Paulo, Div Nephrol, Dept Med, BR-04023900 São Paulo, SP, Brazil
dc.description.affiliation Universidade Federal de São Paulo, Dept Biophys, BR-04023900 São Paulo, SP, Brazil
dc.description.affiliationUnifesp Universidade Federal de São Paulo, Div Nephrol, Dept Med, BR-04023900 São Paulo, SP, Brazil
dc.description.affiliationUnifesp Universidade Federal de São Paulo, Dept Biophys, BR-04023900 São Paulo, SP, Brazil
dc.description.sponsorshipID FAPESP: 2008/55771-3
dc.description.sponsorshipID FAPESP: 2010/51904-9
dc.identifier.doi 10.1016/j.ijbiomac.2014.09.017
dc.description.source Web of Science
dc.identifier.wos WOS:000347577900087



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