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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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Aragao, Danielle S. [1] ; de Andrade, Maria Claudina C. ; Ebihara, Fabiana [1] ; Watanabe, Ingrid K. M. [1] ; Magalhaes, Dayane C. B. P. [1] ; Juliano, Maria Aparecida [2] ; Hirata, Izaura Yoshico [2] ; Casarini, Dulce Elena [1]
Total Authors: 8
[1] Univ Fed Sao Paulo, Div Nephrol, Dept Med, BR-04023900 Sao Paulo, SP - Brazil
[2] Univ Fed Sao Paulo, Dept Biophys, BR-04023900 Sao Paulo, SP - Brazil
Total Affiliations: 2
Document type: Journal article
Source: International Journal of Biological Macromolecules; v. 72, p. 673-679, JAN 2015.
Web of Science Citations: 3

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. (AU)

FAPESP's process: 10/51904-9 - Renin angiotensin and kallikrein kinin systems in hypertension, obesity, diabetes, desnutrition and sepsis: molecular, cellular and physiopathologic mechanisms
Grantee:Dulce Elena Casarini
Support type: Research Projects - Thematic Grants