Please use this identifier to cite or link to this item: https://ninho.inca.gov.br/jspui/handle/123456789/6572
Title: A scrutiny of the biochemical pathways from Ang II to Ang-(3–4) in renal basolateral membranes
Authors: Axelband, Flavia
Dias, Juliana
Miranda, Filipe
Ferrão, Fernanda Magalhães
Barros, Nilana Meza Tenório de
Carmona, Adriana Karaoglanovic
Morcillo, Lucienne da Silva Lara
Vieyra, Adalberto
Keywords: Peptide Hydrolases
Peptídeo Hidrolases
Angiotensin
Angiotensina
Renal Cell
Células Renais
Péptido Hidrolasas
Células Renales
Membranas basolaterais
Basolateral membranes
Issue Date: 2009
Citation: FERRÃO, Fernanda Magalhães et al. A scrutiny of the biochemical pathways from Ang II to Ang-(3–4) in renal basolateral membranes. Regulatory Peptides, v. 158, p. 47–56, 2009.
Abstract: In a previous paper we demonstrated that Ang-(3-4) counteracts inhibition of the Ca(2+)-ATPase by Ang II in the basolateral membranes of kidney proximal tubules cells (BLM). We have now investigated the enzymatic routs by which Ang II is converted to Ang-(3-4). Membrane-bound angiotensin converting enzyme, aminopeptidases and neprilysin were identified using fluorescent substrates. HPLC showed that Plummer's inhibitor but not Z-pro-prolinal blocks Ang II metabolism, suggesting that carboxypeptidase N catalyzes the conversion Ang II--> Ang-(1-7). Different combinations of bestatin, thiorphan, Plummer's inhibitor, Ang II and Ang-(1-5), and use of short proteolysis times, indicate that Ang-(1-7)--> Ang-(1-5)--> Ang-(1-4)--> Ang-(3-4) is a major route. When Ang III was combined with the same inhibitors, the following pathway was demonstrated: Ang III--> Ang IV--> Ang-(3-4). Ca(2+)-ATPase assays with different Ang II concentrations and different peptidase inhibitors confirm the existence of these pathways in BLM and show that a prolyl-carboxypeptidase may be an alternative catalyst for converting Ang II to Ang-(1-7). Overall, we demonstrated that BLM have all the peptidase machinery required to produce Ang-(3-4) in the vicinity of the Ca(2+)-ATPase, enabling a local RAS axis to effect rapid modulation of active Ca(2+) fluxes.
Description: p. 47–56.: il. p&b.
URI: http://sr-vmlxaph03:8080/jspui/handle/123456789/6572
ISSN: 1873-1686
Appears in Collections:Artigos de Periódicos da área de Farmácia



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