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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.)

Spectroscopic and structural analysis of somatic and N-domain angiotensin I-converting enzyme isoforms from mesangial cells from Wistar and spontaneously hypertensive rats

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Author(s):
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de Andrade, Maria C. C. [1] ; Affonso, Regina [2, 3] ; Fernandes, Fernanda B. [1] ; Febba, Andreia C. [1] ; da Silva, Ismael D. C. G. [3] ; Stella, Regina C. R. [1] ; Marson, Odair [1] ; Jubilut, Guita N. [4] ; Hirata, Izaura Y. [4] ; Carmona, Adriana K. [4] ; Corradi, Hazel [5] ; Acharya, K. Ravi [5] ; Sturrock, Edward D. [6, 7] ; Casarini, Dulce E. [1]
Total Authors: 14
Affiliation:
[1] Univ Fed Sao Paulo, Escola Paulista Med, Dept Med, Disciplina Nefrol, BR-04023900 Sao Paulo - Brazil
[2] IPEN CNEN SP, Sao Paulo - Brazil
[3] Univ Fed Sao Paulo, Dept Obstet & Ginecol, BR-04023900 Sao Paulo - Brazil
[4] Univ Fed Sao Paulo, Dept Biofis, BR-04023900 Sao Paulo - Brazil
[5] Univ Bath, Dept Biol & Biochem, Bath BA2 7AY, Avon - England
[6] Univ Cape Town, Div Med Biochem, ZA-7925 Observatory - South Africa
[7] Univ Cape Town, Inst Infect Dis & Mol Med, ZA-7925 Observatory - South Africa
Total Affiliations: 7
Document type: Journal article
Source: International Journal of Biological Macromolecules; v. 47, n. 2, p. 238-243, AUG 1 2010.
Web of Science Citations: 1
Abstract

Angiotensin I-converting enzyme (ACE) plays a key role in the renin-angiotesin aldosterone cascade. We analysed the secondary structure and structural organization of a purified 65 kDa N-domain ACE (nACE) from Wistar rat mesangial cells, a 90 kDa nACE from spontaneously hypertensive rats and a 130 kDa somatic ACE. The C-terminal alignment of the 65 kDa nACE with rat ACE revealed that the former was truncated at Ser(482), and the sequence of the 90 kDa nACE ended at Pro(629). Protein's secondary structure consisted predominantly of a-helices. The 90 and 65 kDa isoforms were the most stable in guanidine and at low pH, respectively. Enzymatic activity decreased with loss in secondary structure, except in the case of guanidine HCl where the 90 kDa fragment loses its secondary structure faster than its enzymatic activity. We identified and characterized the activity and stability of these isoforms and these findings would be helpful on the understanding of the role of nACE isoforms in hypertension. (C) 2010 Elsevier B.V. All rights reserved. (AU)

FAPESP's process: 02/13290-2 - Angiotensin I: converting enzyme isoform (90 kDa), potential genetic marker of hypertension: processing, molecular and functional characterization, and genetic segregation
Grantee:Dulce Elena Casarini
Support Opportunities: Research Projects - Thematic Grants