دورية أكاديمية

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

التفاصيل البيبلوغرافية
العنوان: Serine proteases as candidates for proteolytic processing of angiotensin-I converting enzyme.
المؤلفون: Aragão DS; Department of Medicine, Nephrology Division, Federal University of São Paulo, Brazil., de Andrade MC; Albert Einstein Research Institute, Brazil., Ebihara F; Department of Medicine, Nephrology Division, Federal University of São Paulo, Brazil., Watanabe IK; Department of Medicine, Nephrology Division, Federal University of São Paulo, Brazil., Magalhães DC; Department of Medicine, Nephrology Division, Federal University of São Paulo, Brazil., Juliano MA; Department of Biophysics, Federal University of São Paulo, Brazil., Hirata IY; Department of Biophysics, Federal University of São Paulo, Brazil., Casarini DE; Department of Medicine, Nephrology Division, Federal University of São Paulo, Brazil. Electronic address: casarini.elena@unifesp.br.
المصدر: International journal of biological macromolecules [Int J Biol Macromol] 2015 Jan; Vol. 72, pp. 673-9. Date of Electronic Publication: 2014 Sep 28.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Elsevier Country of Publication: Netherlands NLM ID: 7909578 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1879-0003 (Electronic) Linking ISSN: 01418130 NLM ISO Abbreviation: Int J Biol Macromol Subsets: MEDLINE
أسماء مطبوعة: Publication: Amsterdam : Elsevier
Original Publication: Guildford, Eng., IPC Science and Technology Press.
مواضيع طبية MeSH: Proteolysis*, Hypertension/*enzymology , Peptidyl-Dipeptidase A/*metabolism , Serine Proteases/*metabolism, Angiotensin I/metabolism ; Angiotensin II/metabolism ; Animals ; Blood Pressure ; Humans ; Hypertension/metabolism ; Mesangial Cells/enzymology ; Mesangial Cells/metabolism ; Peptidyl-Dipeptidase A/biosynthesis ; Protein Isoforms/biosynthesis ; Protein Isoforms/metabolism ; Rats ; Serine Proteases/biosynthesis
مستخلص: 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.
(Copyright © 2014 Elsevier B.V. All rights reserved.)
التعليقات: Erratum in: Int J Biol Macromol. 2015 Nov;81:1099-110.
فهرسة مساهمة: Keywords: Angiotensin-I converting enzyme; Shedding, Mesangial cells
المشرفين على المادة: 0 (Protein Isoforms)
11128-99-7 (Angiotensin II)
9041-90-1 (Angiotensin I)
EC 3.4.- (Serine Proteases)
EC 3.4.15.1 (Peptidyl-Dipeptidase A)
تواريخ الأحداث: Date Created: 20140930 Date Completed: 20150811 Latest Revision: 20160413
رمز التحديث: 20240628
DOI: 10.1016/j.ijbiomac.2014.09.017
PMID: 25263467
قاعدة البيانات: MEDLINE
الوصف
تدمد:1879-0003
DOI:10.1016/j.ijbiomac.2014.09.017