Please use this identifier to cite or link to this item: http://repositorio.unifesp.br/handle/11600/33657
Title: Angiotensin II Binding to Angiotensin I-Converting Enzyme Triggers Calcium Signaling
Authors: Guimarães, Paola Bianchi [UNIFESP]
Alvarenga, Erika Costa [UNIFESP]
Siqueira, Paula D. [UNIFESP]
Paredes-Gamero, Edgar Julian [UNIFESP]
Sabatini, Regiane Angelica [UNIFESP]
Morais, Rafael Leite Tavares de [UNIFESP]
Reis, Rosana I.
Santos, Edson L.
Teixeira, Luis Gustavo de Deus [UNIFESP]
Casarini, Dulce Elena [UNIFESP]
Martin, Renan Paulo [UNIFESP]
Shimuta, Suma Imura [UNIFESP]
Carmona, Adriana Karaoglanovic [UNIFESP]
Nakaie, Clovis Ryuichi [UNIFESP]
Jasiulionis, Miriam Galvonas [UNIFESP]
Ferreira, Alice Teixeira [UNIFESP]
Pesquero, Jorge L.
Oliveira, Suzana M. [UNIFESP]
Bader, Michael [UNIFESP]
Costa-Neto, Claudio M.
Pesquero, João Bosco [UNIFESP]
Universidade Federal de São Paulo (UNIFESP)
Universidade de São Paulo (USP)
Fundacao Univ Fed Grande Dourados
Max Delbruck Ctr Mol Med
Keywords: angiotensin I-converting enzyme
ACE
calcium
angiotensin
cells
receptors
Issue Date: 1-May-2011
Publisher: Lippincott Williams & Wilkins
Citation: Hypertension. Philadelphia: Lippincott Williams & Wilkins, v. 57, n. 5, p. 965-U200, 2011.
Abstract: Angiotensin (Ang) I-converting enzyme (ACE) is involved in the control of blood pressure by catalyzing the conversion of Ang I into the vasoconstrictor Ang II and degrading the vasodilator peptide bradykinin. Human ACE also functions as a signal transduction molecule, and the binding of ACE substrates or its inhibitors initiates a series of events. in this study, we examined whether Ang II could bind to ACE generating calcium signaling. Chinese hamster ovary cells transfected with an ACE expression vector reveal that Ang II is able to bind with high affinity to ACE in the absence of the Ang II type 1 and type 2 receptors and to activate intracellular signaling pathways, such as inositol 1,4,5-trisphosphate and calcium. These effects could be blocked by the ACE inhibitor, lisinopril. Calcium mobilization was specific for Ang II, because other ACE substrates or products, namely Ang 1-7, bradykinin, bradykinin 1-5, and N-acetyl-seryl-aspartyl-lysyl-proline, did not trigger this signaling pathway. Moreover, in Tm5, a mouse melanoma cell line endogenously expressing ACE but not Ang II type 1 or type 2 receptors, Ang II increased intracellular calcium and reactive oxygen species. in conclusion, we describe for the first time that Ang II can interact with ACE and evoke calcium and other signaling molecules in cells expressing only ACE. These findings uncover a new mechanism of Ang II action and have implications for the understanding of the renin-Ang system. (Hypertension. 2011;57:965-972.) . Online Data Supplement
URI: http://repositorio.unifesp.br/handle/11600/33657
ISSN: 0194-911X
Other Identifiers: http://dx.doi.org/10.1161/HYPERTENSIONAHA.110.167171
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