Human erythrocyte acetylcholinesterase in health and disease

Detalhes bibliográficos
Autor(a) principal: Saldanha, Carlota
Data de Publicação: 2017
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10451/34383
Resumo: © 2017 by the author. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
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spelling Human erythrocyte acetylcholinesterase in health and diseaseAcetylcholinesteraseRred blood cellsNitric oxide© 2017 by the author. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).The biochemical properties of erythrocyte or human red blood cell (RBC) membrane acetylcholinesterase (AChE) and its applications on laboratory class and on research are reviewed. Evidence of the biochemical and the pathophysiological properties like the association between the RBC AChE enzyme activity and the clinical and biophysical parameters implicated in several diseases are overviewed, and the achievement of RBC AChE as a biomarker and as a prognostic factor are presented. Beyond its function as an enzyme, a special focus is highlighted in this review for a new function of the RBC AChE, namely a component of the signal transduction pathway of nitric oxide.This work was funded by Fundação para a Ciência e Tecnologia: LISBOA-01-0145-FEDER-007391, project cofunded by FEDER, through POR Lisboa 2020—Programa Operacional Regional de Lisboa, PORTUGAL 2020.MDPIRepositório da Universidade de LisboaSaldanha, Carlota2018-07-30T11:33:46Z20172017-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10451/34383eng2017; pii: E14991420-304910.3390/molecules22091499info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-11-08T16:29:40Zoai:repositorio.ul.pt:10451/34383Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T21:49:06.529292Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Human erythrocyte acetylcholinesterase in health and disease
title Human erythrocyte acetylcholinesterase in health and disease
spellingShingle Human erythrocyte acetylcholinesterase in health and disease
Saldanha, Carlota
Acetylcholinesterase
Rred blood cells
Nitric oxide
title_short Human erythrocyte acetylcholinesterase in health and disease
title_full Human erythrocyte acetylcholinesterase in health and disease
title_fullStr Human erythrocyte acetylcholinesterase in health and disease
title_full_unstemmed Human erythrocyte acetylcholinesterase in health and disease
title_sort Human erythrocyte acetylcholinesterase in health and disease
author Saldanha, Carlota
author_facet Saldanha, Carlota
author_role author
dc.contributor.none.fl_str_mv Repositório da Universidade de Lisboa
dc.contributor.author.fl_str_mv Saldanha, Carlota
dc.subject.por.fl_str_mv Acetylcholinesterase
Rred blood cells
Nitric oxide
topic Acetylcholinesterase
Rred blood cells
Nitric oxide
description © 2017 by the author. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
publishDate 2017
dc.date.none.fl_str_mv 2017
2017-01-01T00:00:00Z
2018-07-30T11:33:46Z
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url http://hdl.handle.net/10451/34383
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 2017; pii: E1499
1420-3049
10.3390/molecules22091499
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