The epithelial sodium channel and the cell migration

Autores
Marino, Gabriela I.; Kotsias, Basilio A.
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Sodium is the main extracellular cation, and its osmotic pressure is an important determinant of the extracellular fluid volume. We were interested in the expression and functional characteristics of the epithelial sodium channel (ENaC) that mediates the Na+ entry into the cells from the luminal fluid in many reabsorbing epithelia and in the human placenta. Aldosterone is a key regulator of ENaC channel and stimulates protein methylation on the β-subunit of ENaC. Aldosterone and 8Br-cAMP promoted cellular migration in a wound healing model in trophoblastic BeWo cells. Amiloride blocked this effect. Electrophysiological studies showed an increase in ENaC current in the presence of aldosterone. We suggest that aldosterone positively influences wound healing through methylation of ENaC. On the other hand, we found a diminished expression of the three subunits of the ENaC in the membranes of preeclamptic placentas in comparison with the normal ones and this may have consequences for the cell migration and ion transport involved in the pathophysiology of preeclampsia.
Sociedad Argentina de Fisiología
Materia
Ciencias Médicas
ENaC
currents
cell migration
wound healing
BeWo cell line
Preeclampsia
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/131285

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network_name_str SEDICI (UNLP)
spelling The epithelial sodium channel and the cell migrationMarino, Gabriela I.Kotsias, Basilio A.Ciencias MédicasENaCcurrentscell migrationwound healingBeWo cell linePreeclampsiaSodium is the main extracellular cation, and its osmotic pressure is an important determinant of the extracellular fluid volume. We were interested in the expression and functional characteristics of the epithelial sodium channel (ENaC) that mediates the Na+ entry into the cells from the luminal fluid in many reabsorbing epithelia and in the human placenta. Aldosterone is a key regulator of ENaC channel and stimulates protein methylation on the β-subunit of ENaC. Aldosterone and 8Br-cAMP promoted cellular migration in a wound healing model in trophoblastic BeWo cells. Amiloride blocked this effect. Electrophysiological studies showed an increase in ENaC current in the presence of aldosterone. We suggest that aldosterone positively influences wound healing through methylation of ENaC. On the other hand, we found a diminished expression of the three subunits of the ENaC in the membranes of preeclamptic placentas in comparison with the normal ones and this may have consequences for the cell migration and ion transport involved in the pathophysiology of preeclampsia.Sociedad Argentina de Fisiología2013info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf13-25http://sedici.unlp.edu.ar/handle/10915/131285enginfo:eu-repo/semantics/altIdentifier/url/https://pmr.safisiol.org.ar/uploadsarchivos/vol_6_3_marino_and_kotsias_1_.pdfinfo:eu-repo/semantics/altIdentifier/issn/1669-5410info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-10-15T11:24:54Zoai:sedici.unlp.edu.ar:10915/131285Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-10-15 11:24:55.007SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv The epithelial sodium channel and the cell migration
title The epithelial sodium channel and the cell migration
spellingShingle The epithelial sodium channel and the cell migration
Marino, Gabriela I.
Ciencias Médicas
ENaC
currents
cell migration
wound healing
BeWo cell line
Preeclampsia
title_short The epithelial sodium channel and the cell migration
title_full The epithelial sodium channel and the cell migration
title_fullStr The epithelial sodium channel and the cell migration
title_full_unstemmed The epithelial sodium channel and the cell migration
title_sort The epithelial sodium channel and the cell migration
dc.creator.none.fl_str_mv Marino, Gabriela I.
Kotsias, Basilio A.
author Marino, Gabriela I.
author_facet Marino, Gabriela I.
Kotsias, Basilio A.
author_role author
author2 Kotsias, Basilio A.
author2_role author
dc.subject.none.fl_str_mv Ciencias Médicas
ENaC
currents
cell migration
wound healing
BeWo cell line
Preeclampsia
topic Ciencias Médicas
ENaC
currents
cell migration
wound healing
BeWo cell line
Preeclampsia
dc.description.none.fl_txt_mv Sodium is the main extracellular cation, and its osmotic pressure is an important determinant of the extracellular fluid volume. We were interested in the expression and functional characteristics of the epithelial sodium channel (ENaC) that mediates the Na+ entry into the cells from the luminal fluid in many reabsorbing epithelia and in the human placenta. Aldosterone is a key regulator of ENaC channel and stimulates protein methylation on the β-subunit of ENaC. Aldosterone and 8Br-cAMP promoted cellular migration in a wound healing model in trophoblastic BeWo cells. Amiloride blocked this effect. Electrophysiological studies showed an increase in ENaC current in the presence of aldosterone. We suggest that aldosterone positively influences wound healing through methylation of ENaC. On the other hand, we found a diminished expression of the three subunits of the ENaC in the membranes of preeclamptic placentas in comparison with the normal ones and this may have consequences for the cell migration and ion transport involved in the pathophysiology of preeclampsia.
Sociedad Argentina de Fisiología
description Sodium is the main extracellular cation, and its osmotic pressure is an important determinant of the extracellular fluid volume. We were interested in the expression and functional characteristics of the epithelial sodium channel (ENaC) that mediates the Na+ entry into the cells from the luminal fluid in many reabsorbing epithelia and in the human placenta. Aldosterone is a key regulator of ENaC channel and stimulates protein methylation on the β-subunit of ENaC. Aldosterone and 8Br-cAMP promoted cellular migration in a wound healing model in trophoblastic BeWo cells. Amiloride blocked this effect. Electrophysiological studies showed an increase in ENaC current in the presence of aldosterone. We suggest that aldosterone positively influences wound healing through methylation of ENaC. On the other hand, we found a diminished expression of the three subunits of the ENaC in the membranes of preeclamptic placentas in comparison with the normal ones and this may have consequences for the cell migration and ion transport involved in the pathophysiology of preeclampsia.
publishDate 2013
dc.date.none.fl_str_mv 2013
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/131285
url http://sedici.unlp.edu.ar/handle/10915/131285
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://pmr.safisiol.org.ar/uploadsarchivos/vol_6_3_marino_and_kotsias_1_.pdf
info:eu-repo/semantics/altIdentifier/issn/1669-5410
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
dc.format.none.fl_str_mv application/pdf
13-25
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instname:Universidad Nacional de La Plata
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instname_str Universidad Nacional de La Plata
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repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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