ACE activity is modulated by kinin B-2 receptor

ACE activity is modulated by kinin B-2 receptor

Author Sabatini, Regiane Angelica Autor UNIFESP Google Scholar
Guimarães, Paola Bianchi Autor UNIFESP Google Scholar
Fernandes, Liliam Autor UNIFESP Google Scholar
Reis, Felipe Castellani Gomes dos Autor UNIFESP Google Scholar
Bersanetti, Patricia Alessandra Autor UNIFESP Google Scholar
Mori, Marcelo Alves da Silva Autor UNIFESP Google Scholar
Navarro, Alberto Autor UNIFESP Google Scholar
Hilzendeger, Aline Mourão Autor UNIFESP Google Scholar
Santos, Edson Lucas dos Autor UNIFESP Google Scholar
Andrade, Maria C. C. Autor UNIFESP Google Scholar
Chagas, Jair Ribeiro Autor UNIFESP Google Scholar
Pesquero, Jorge L. Google Scholar
Casarini, Dulce Elena Autor UNIFESP Google Scholar
Bader, Michael Autor UNIFESP Google Scholar
Carmona, Adriana Karaoglanovic Autor UNIFESP Google Scholar
Pesquero, João Bosco Autor UNIFESP Google Scholar
Institution Universidade Federal de São Paulo (UNIFESP)
Universidade Federal de Minas Gerais (UFMG)
Max Delbruck Ctr Mol Med
Abstract Angiotensin-converting enzyme (ACE) is an ectoprotein able to modulate the activity of a plethora of compounds, among them angiotensin I and bradykinin. Despite several decades of research, new aspects of the mechanism of action of ACE have been elucidated, expanding our understanding of its role not only in cardiovascular regulation but also in different areas. Recent findings have ascribed an important role for ACE/kinin B-2 receptor heterodimerization in the pharmacological properties of the receptor. in this work, we tested the hypothesis that this interaction also affects ACE enzymatic activity. ACE catalytic activity was analyzed in Chinese hamster ovary cell monolayers coexpressing the somatic form of the enzyme and the receptor coding region using as substrate the fluorescence resonance energy transfer peptide Abz-FRK(Dnp) P-OH. Results show that the coexpression of the kinin B-2 receptor leads to an augmentation in ACE activity. in addition, this effect could be blocked by the B-2 receptor antagonist icatibant. the hypothesis was also tested in endothelial cells, a more physiological system, where both proteins are naturally expressed. Endothelial cells from genetically ablated kinin B-2 receptor mice showed a decreased ACE activity when compared with wild-type mice cells. in summary, this is the first report showing that the ACE/kinin B-2 receptor interaction modulates ACE activity. Taking into account the interplay among ACE, ACE inhibitors, and kinin receptors, we believe that these results will shed new light into the arena of the controversial search for the mechanism controlling these interactions.
Keywords ACE
kinin B-2 receptor
dimerization
enzyme activity
ACE inhibitors
icatibant
Language English
Date 2008-03-01
Published in Hypertension. Philadelphia: Lippincott Williams & Wilkins, v. 51, n. 3, p. 689-695, 2008.
ISSN 0194-911X (Sherpa/Romeo, impact factor)
Publisher Lippincott Williams & Wilkins
Extent 689-695
Origin http://dx.doi.org/10.1161/HYPERTENSIONAHA.107.091181
Access rights Open access Open Access
Type Article
Web of Science ID WOS:000253428200021
URI http://repositorio.unifesp.br/handle/11600/30465

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