Expression and localization of N-domain ANG I-converting enzymes in mesangial cells in culture from spontaneously hypertensive rats

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dc.contributor.author Andrade, Maria Claudina Camargo de [UNIFESP]
dc.contributor.author Di Marco, Giovana Seno [UNIFESP]
dc.contributor.author Teixeira, Vicente de Paulo Castro [UNIFESP]
dc.contributor.author Mortara, Renato Arruda [UNIFESP]
dc.contributor.author Sabatini, Regiane Angelica [UNIFESP]
dc.contributor.author Pesquero, Joao Bosco [UNIFESP]
dc.contributor.author Boim, Miriam Aparecida [UNIFESP]
dc.contributor.author Carmona, Adriana Karaoglanovic [UNIFESP]
dc.contributor.author Schor, Nestor [UNIFESP]
dc.contributor.author Casarini, Dulce Elena [UNIFESP]
dc.date.accessioned 2016-01-24T12:40:56Z
dc.date.available 2016-01-24T12:40:56Z
dc.date.issued 2006-02-01
dc.identifier http://dx.doi.org/10.1152/ajprenal.00110.2005
dc.identifier.citation American Journal of Physiology-renal Physiology. Bethesda: Amer Physiological Soc, v. 290, n. 2, p. F364-F375, 2006.
dc.identifier.issn 1931-857X
dc.identifier.uri http://repositorio.unifesp.br/handle/11600/28711
dc.description.abstract Expression and localization of N-domain ANG I-converting enzymes in mesangial cells in culture from spontaneously hypertensive rats. Am J Physiol Renal Physiol 290: F364 - F375, 2006. First published August 16, 2005; doi: 10.1152/ajprenal. 00110.2005. - the angiotensin-converting enzyme (ACE) profile in urine of hypertensive patients and spontaneously hypertensive rats (SHR; 90- and 65-kDa N-domain ACEs) is different from that of healthy subjects and Wistar rats (190 and 65 kDa). in addition, four ACE isoforms were purified from mesangial cells (MC) of Wistar rats in the intracellular compartment (130 and 68 kDa) and as secreted forms (130 and 60 kDa). We decided to characterize ACE forms from SHR MC in culture. Analysis of the ACE gene showed that SHR MC are able to express ACE mRNA. the concentrated medium and cell homogenate were separately purified by gel filtration and then subjected to lisinopril-Sepharose chromatography. the molecular masses of purified enzymes, 90 kDa for ACEm1A and 65 kDa for ACEm2A (secreted enzymes) and 90 kDa for ACEInth1A and 65 kDa for ACEInth2A (intracellular), were different from those of Wistar MC. the purified enzymes are Cl(-) dependent, inhibited by enalaprilat and captopril, and able to hydrolyze AcSDKP. Immunofluorescence and cell fractionation followed by Western blotting showed predominant immunoreaction of the 9B9 antiserum for N-domain ACE in the nuclei. the N-domain ACE was localized in the glomerulus from Wistar rats and SHR. ANG II and ANG-(1-7) were localized in the cell cytoplasm and nuclei. the 90-kDa N-domain ACE, described recently as a possible genetic marker of hypertension, was found inside the cell nuclei of SHR MC colocalized with ANG II and ANG-(1 - 7). the presence of ANG II in the cell nuclei could suggest an important role for this peptide in the transcription of new genes. en
dc.format.extent F364-F375
dc.language.iso eng
dc.publisher Amer Physiological Soc
dc.relation.ispartof American Journal of Physiology-renal Physiology
dc.rights Acesso aberto
dc.subject nuclei en
dc.subject hypertension en
dc.subject mesangial cell en
dc.subject regulation of gene expression en
dc.title Expression and localization of N-domain ANG I-converting enzymes in mesangial cells in culture from spontaneously hypertensive rats en
dc.type Artigo
dc.contributor.institution Universidade Federal de São Paulo (UNIFESP)
dc.description.affiliation Universidade Federal de São Paulo, Escola Paulista Med, Dept Med, Disciplina Nefrol, BR-04023900 São Paulo, Brazil
dc.description.affiliation Universidade Federal de São Paulo, Disciplina Parasitol, Dept Microbiol Inumol & Parasitol, BR-04023900 São Paulo, Brazil
dc.description.affiliation Universidade Federal de São Paulo, Dept Biofis, BR-04023900 São Paulo, Brazil
dc.description.affiliationUnifesp Universidade Federal de São Paulo, Escola Paulista Med, Dept Med, Disciplina Nefrol, BR-04023900 São Paulo, Brazil
dc.description.affiliationUnifesp Universidade Federal de São Paulo, Disciplina Parasitol, Dept Microbiol Inumol & Parasitol, BR-04023900 São Paulo, Brazil
dc.description.affiliationUnifesp Universidade Federal de São Paulo, Dept Biofis, BR-04023900 São Paulo, Brazil
dc.identifier.doi 10.1152/ajprenal.00110.2005
dc.description.source Web of Science
dc.identifier.wos WOS:000234531200015



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