Characterization of placental cholinesterases and activityinduction associated to environmental organophosphateexposure

Autores
Sanchez, Susana; Vera, Berta; Montagna, Cristina; Magnarelli, Gladis
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión aceptada
Descripción
Although non-innervated, the placenta contains both cholinesterases (ChEs), butyryl-cholinesterase (BChE) and acetylcholinesterase (AChE). These enzymes are well-known fortheir multiple molecular forms. In a first approach, we used recognized specific inhibitors,substrate preferences and non-denaturating gel electrophoresis in order to characterize theChE profile of term placenta from uncomplicated pregnancy. Results strongly suggest thatthe predominant cholinesterasic form present was tetrameric BChE.It is well established that both ChEs are targets of cholinesterase-inhibiting organophos-phates (OP), one of the most important classes of chemicals actively applied to theenvironment. However, we have previously reported increased ChEs activity in placenta ofrural residents exposed to OP. In the present work, we have studied: 1) whether this find-ing was reproducible and, 2) whether AChE or BChE up regulation is behind the increase ofplacental ChE activity. The population studied included forty healthy women who live inan agricultural area. Samples were collected during both the OP pulverization period (PP)and the recess period (RP). The placental ChEs activity increased in PP, evidencing repro-ducibility of previous results. The analysis of non-denaturating gels revealed that increasedactivity of total ChE activity in placenta from women exposed to OP may be attributable totetrameric BChE up-regulation.
Fil: Sanchez, Susana. Universidad Nacional del Comahue. Facultad de Ciencias Médicas; Argentina.
Fil: Vera, Berta. Universidad Nacional del Comahue. Facultad de Ingeniería. Departamento de Química. Laboratorio de Investigaciones Bioquímicas, Químicas y de Medio Ambiente; Argentina.
Fil: Vera, Berta. Universidad Nacional del Comahue. Facultad de Ciencias Médicas; Argentina.
Fil: Montagna, Cristina. Universidad Nacional del Comahue. Facultad de Ingeniería. Departamento de Química. Laboratorio de Investigaciones Bioquímicas, Químicas y de Medio Ambiente; Argentina.
Fil: Montagna, Cristina. Universidad Nacional del Comahue. Facultad de Ciencias del Ambiente y Salud; Argentina.
Fil: Magnarelli, Gladis. Universidad Nacional del Comahue. Facultad de Ingeniería. Departamento de Química. Laboratorio de Investigaciones Bioquímicas, Químicas y de Medio Ambiente; Argentina.
Fil: Magnarelli, Gladis. Universidad Nacional del Comahue. Facultad de Ciencias Médicas; Argentina.
Fuente
Toxicology Reports Vol. 2 (2015)
Materia
Placenta
Butyrylcholinesterase
Acetylcholinesterase
Organophosphates
Ciencias Biomédicas
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
Repositorio Digital Institucional (UNCo)
Institución
Universidad Nacional del Comahue
OAI Identificador
oai:rdi.uncoma.edu.ar:uncomaid/15221
Acceder
id RDIUNCO_f2a1fbe3f341ab64b9365e2718ea2122
oai_identifier_str oai:rdi.uncoma.edu.ar:uncomaid/15221
network_acronym_str RDIUNCO
repository_id_str 7108
network_name_str Repositorio Digital Institucional (UNCo)
spelling Characterization of placental cholinesterases and activityinduction associated to environmental organophosphateexposureSanchez, SusanaVera, BertaMontagna, CristinaMagnarelli, GladisPlacentaButyrylcholinesteraseAcetylcholinesteraseOrganophosphatesCiencias BiomédicasAlthough non-innervated, the placenta contains both cholinesterases (ChEs), butyryl-cholinesterase (BChE) and acetylcholinesterase (AChE). These enzymes are well-known fortheir multiple molecular forms. In a first approach, we used recognized specific inhibitors,substrate preferences and non-denaturating gel electrophoresis in order to characterize theChE profile of term placenta from uncomplicated pregnancy. Results strongly suggest thatthe predominant cholinesterasic form present was tetrameric BChE.It is well established that both ChEs are targets of cholinesterase-inhibiting organophos-phates (OP), one of the most important classes of chemicals actively applied to theenvironment. However, we have previously reported increased ChEs activity in placenta ofrural residents exposed to OP. In the present work, we have studied: 1) whether this find-ing was reproducible and, 2) whether AChE or BChE up regulation is behind the increase ofplacental ChE activity. The population studied included forty healthy women who live inan agricultural area. Samples were collected during both the OP pulverization period (PP)and the recess period (RP). The placental ChEs activity increased in PP, evidencing repro-ducibility of previous results. The analysis of non-denaturating gels revealed that increasedactivity of total ChE activity in placenta from women exposed to OP may be attributable totetrameric BChE up-regulation.Fil: Sanchez, Susana. Universidad Nacional del Comahue. Facultad de Ciencias Médicas; Argentina.Fil: Vera, Berta. Universidad Nacional del Comahue. Facultad de Ingeniería. Departamento de Química. Laboratorio de Investigaciones Bioquímicas, Químicas y de Medio Ambiente; Argentina.Fil: Vera, Berta. Universidad Nacional del Comahue. Facultad de Ciencias Médicas; Argentina.Fil: Montagna, Cristina. Universidad Nacional del Comahue. Facultad de Ingeniería. Departamento de Química. Laboratorio de Investigaciones Bioquímicas, Químicas y de Medio Ambiente; Argentina.Fil: Montagna, Cristina. Universidad Nacional del Comahue. Facultad de Ciencias del Ambiente y Salud; Argentina.Fil: Magnarelli, Gladis. Universidad Nacional del Comahue. Facultad de Ingeniería. Departamento de Química. Laboratorio de Investigaciones Bioquímicas, Químicas y de Medio Ambiente; Argentina.Fil: Magnarelli, Gladis. Universidad Nacional del Comahue. Facultad de Ciencias Médicas; Argentina.ElsevierBoard2014-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/acceptedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfpp. 437–442application/pdfhttp://rdi.uncoma.edu.ar/handle/uncomaid/152212214-7500Toxicology Reports Vol. 2 (2015)reponame:Repositorio Digital Institucional (UNCo)instname:Universidad Nacional del Comahueenghttps://www.journals.elsevier.com/toxicology-reportsinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/2025-09-29T14:29:06Zoai:rdi.uncoma.edu.ar:uncomaid/15221instacron:UNCoInstitucionalhttp://rdi.uncoma.edu.ar/Universidad públicaNo correspondehttp://rdi.uncoma.edu.ar/oaimirtha.mateo@biblioteca.uncoma.edu.ar; adriana.acuna@biblioteca.uncoma.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:71082025-09-29 14:29:06.515Repositorio Digital Institucional (UNCo) - Universidad Nacional del Comahuefalse
dc.title.none.fl_str_mv Characterization of placental cholinesterases and activityinduction associated to environmental organophosphateexposure
title Characterization of placental cholinesterases and activityinduction associated to environmental organophosphateexposure
spellingShingle Characterization of placental cholinesterases and activityinduction associated to environmental organophosphateexposure
Sanchez, Susana
Placenta
Butyrylcholinesterase
Acetylcholinesterase
Organophosphates
Ciencias Biomédicas
title_short Characterization of placental cholinesterases and activityinduction associated to environmental organophosphateexposure
title_full Characterization of placental cholinesterases and activityinduction associated to environmental organophosphateexposure
title_fullStr Characterization of placental cholinesterases and activityinduction associated to environmental organophosphateexposure
title_full_unstemmed Characterization of placental cholinesterases and activityinduction associated to environmental organophosphateexposure
title_sort Characterization of placental cholinesterases and activityinduction associated to environmental organophosphateexposure
dc.creator.none.fl_str_mv Sanchez, Susana
Vera, Berta
Montagna, Cristina
Magnarelli, Gladis
author Sanchez, Susana
author_facet Sanchez, Susana
Vera, Berta
Montagna, Cristina
Magnarelli, Gladis
author_role author
author2 Vera, Berta
Montagna, Cristina
Magnarelli, Gladis
author2_role author
author
author
dc.subject.none.fl_str_mv Placenta
Butyrylcholinesterase
Acetylcholinesterase
Organophosphates
Ciencias Biomédicas
topic Placenta
Butyrylcholinesterase
Acetylcholinesterase
Organophosphates
Ciencias Biomédicas
dc.description.none.fl_txt_mv Although non-innervated, the placenta contains both cholinesterases (ChEs), butyryl-cholinesterase (BChE) and acetylcholinesterase (AChE). These enzymes are well-known fortheir multiple molecular forms. In a first approach, we used recognized specific inhibitors,substrate preferences and non-denaturating gel electrophoresis in order to characterize theChE profile of term placenta from uncomplicated pregnancy. Results strongly suggest thatthe predominant cholinesterasic form present was tetrameric BChE.It is well established that both ChEs are targets of cholinesterase-inhibiting organophos-phates (OP), one of the most important classes of chemicals actively applied to theenvironment. However, we have previously reported increased ChEs activity in placenta ofrural residents exposed to OP. In the present work, we have studied: 1) whether this find-ing was reproducible and, 2) whether AChE or BChE up regulation is behind the increase ofplacental ChE activity. The population studied included forty healthy women who live inan agricultural area. Samples were collected during both the OP pulverization period (PP)and the recess period (RP). The placental ChEs activity increased in PP, evidencing repro-ducibility of previous results. The analysis of non-denaturating gels revealed that increasedactivity of total ChE activity in placenta from women exposed to OP may be attributable totetrameric BChE up-regulation.
Fil: Sanchez, Susana. Universidad Nacional del Comahue. Facultad de Ciencias Médicas; Argentina.
Fil: Vera, Berta. Universidad Nacional del Comahue. Facultad de Ingeniería. Departamento de Química. Laboratorio de Investigaciones Bioquímicas, Químicas y de Medio Ambiente; Argentina.
Fil: Vera, Berta. Universidad Nacional del Comahue. Facultad de Ciencias Médicas; Argentina.
Fil: Montagna, Cristina. Universidad Nacional del Comahue. Facultad de Ingeniería. Departamento de Química. Laboratorio de Investigaciones Bioquímicas, Químicas y de Medio Ambiente; Argentina.
Fil: Montagna, Cristina. Universidad Nacional del Comahue. Facultad de Ciencias del Ambiente y Salud; Argentina.
Fil: Magnarelli, Gladis. Universidad Nacional del Comahue. Facultad de Ingeniería. Departamento de Química. Laboratorio de Investigaciones Bioquímicas, Químicas y de Medio Ambiente; Argentina.
Fil: Magnarelli, Gladis. Universidad Nacional del Comahue. Facultad de Ciencias Médicas; Argentina.
description Although non-innervated, the placenta contains both cholinesterases (ChEs), butyryl-cholinesterase (BChE) and acetylcholinesterase (AChE). These enzymes are well-known fortheir multiple molecular forms. In a first approach, we used recognized specific inhibitors,substrate preferences and non-denaturating gel electrophoresis in order to characterize theChE profile of term placenta from uncomplicated pregnancy. Results strongly suggest thatthe predominant cholinesterasic form present was tetrameric BChE.It is well established that both ChEs are targets of cholinesterase-inhibiting organophos-phates (OP), one of the most important classes of chemicals actively applied to theenvironment. However, we have previously reported increased ChEs activity in placenta ofrural residents exposed to OP. In the present work, we have studied: 1) whether this find-ing was reproducible and, 2) whether AChE or BChE up regulation is behind the increase ofplacental ChE activity. The population studied included forty healthy women who live inan agricultural area. Samples were collected during both the OP pulverization period (PP)and the recess period (RP). The placental ChEs activity increased in PP, evidencing repro-ducibility of previous results. The analysis of non-denaturating gels revealed that increasedactivity of total ChE activity in placenta from women exposed to OP may be attributable totetrameric BChE up-regulation.
publishDate 2014
dc.date.none.fl_str_mv 2014-11
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/acceptedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv http://rdi.uncoma.edu.ar/handle/uncomaid/15221
2214-7500
url http://rdi.uncoma.edu.ar/handle/uncomaid/15221
identifier_str_mv 2214-7500
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv https://www.journals.elsevier.com/toxicology-reports
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
pp. 437–442
application/pdf
dc.publisher.none.fl_str_mv Elsevier
Board
publisher.none.fl_str_mv Elsevier
Board
dc.source.none.fl_str_mv Toxicology Reports Vol. 2 (2015)
reponame:Repositorio Digital Institucional (UNCo)
instname:Universidad Nacional del Comahue
reponame_str Repositorio Digital Institucional (UNCo)
collection Repositorio Digital Institucional (UNCo)
instname_str Universidad Nacional del Comahue
repository.name.fl_str_mv Repositorio Digital Institucional (UNCo) - Universidad Nacional del Comahue
repository.mail.fl_str_mv mirtha.mateo@biblioteca.uncoma.edu.ar; adriana.acuna@biblioteca.uncoma.edu.ar
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score 12.559606

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