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1 Departamento de Medicina, Disciplina de Nefrologia, Universidade Federal de Sao Paulo, Sao Paulo, Sao Paulo, Brazil
2 Departamento de Microbiologia, Imunologia e Parasitologia, Disciplina de Parasitologia, Universidade Federal de Sao Paulo, Sao Paulo, Sao Paulo, Brazil
3 Departamento de Biofisica, Universidade Federal de Sao Paulo, Sao Paulo, Sao Paulo, Brazil
* To whom correspondence should be addressed. E-mail: dulce{at}nefro.epm.br.
Hypertensive patients and SHR presented a different ACE profile (90 and 65 kDa N-domain ACEs) in urine as compared to healthy subjects and Wistar rats (190 and 65 kDa), In addition, four ACE isoforms were purified from mesangial cells (MC) of Wistar rat 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 followed by Lisinopril Sepharose chromatography. The molecular weights of purified enzymes were: ACEm1A, 90 kDa and ACEm2A, 65 kDa (secreted enzymes); ACEInth1A, 90 kDa and ACEInth2A, 65 kDa (intracellular) differing from the Wistar MC. They are Cl- dependent, inhibited by enalaprilat and captopril and able to hydrolyze AcSDKP. The 9B9 antiserum, for N-domain ACE, showed predominant immunoreaction in the nuclei by immunofluorescence and cell fractionation followed by Western blotting. The N-domain ACE was localized in the glomerulus from Wistar and SHR rats. Angiotensin II (AII) and Angiotensin 1-7 (Ang1-7) 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 co-localized with AII and Ang1-7. The presence of AII in the cell nuclei could suggest important role of this peptide in the transcription of new genes.
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