Uroguanylin regulates net fluid secretion via the NHE2 isoform of the Na+/H+ exchanger in an intestinal cellular model

Autores
Toriano, Roxana Mabel; Ozu, Marcelo; Politi, María T.; Dorr, Ricardo Alfredo; Curto, Maria de Los Angeles; Capurro, Claudia Graciela
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Uroguanylin (UGN) has been proposed as a key regulator of salt and water intestinal transport. Uroguanylin (UGN) activates cell-surface guanylate cyclase C receptor (GC-C) and modulates cellular function via cyclic GMP (cGMP), thus increasing electrolyte and net water secretion. It has been suggested that the action of UGN could involve the Na+/H+ exchanger, but the actual contribution of this transporter still remains unclear. The objective of our study was to investigate the putative effects of UGN on some members of the Na+/H+ exchanger (NHE) family, as well as to clarify its consequences on transepithelial fluid flow in T84 cells. In order to do so, transepithelial fluid flow (Jv) was studied by optic techniques and intracellular pH (pHi) was measured with a fluorescence method. Results showed that NHE2 is found at the apical membrane and has a major role in Na+ absorption; NHE1 and NHE4 are localized at the basolateral membrane with a house-keeping role in steady state pHi. Cell exposure to apical UGN increases net secretory Jv, without changing short-circuit currents nor transepithelial resistance, and reduces NHE2 activity. Therefore, at physiological pH, the effect on net Jv was produced mainly by a reduction in normal Na+ absorption through NHE2, rather than by the stimulation of electrolyte secretion. Our study shows that the effect of UGN on pHi is GC-C/cGMP-mediated and enhanced by sildenafil, thus involving PDE5 enzyme. Additionally, cell exposure to apical UGN results in intracellular alkalinization, probably due to indirect effects on basolateral NHE1 and NHE4, which have a major role in pHi regulation.
Fil: Toriano, Roxana Mabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Ciencias Fisiológicas. Laboratorio de Biomembranas; Argentina
Fil: Ozu, Marcelo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Ciencias Fisiológicas. Laboratorio de Biomembranas; Argentina
Fil: Politi, María T.. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Ciencias Fisiológicas. Laboratorio de Biomembranas; Argentina
Fil: Dorr, Ricardo Alfredo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Ciencias Fisiológicas. Laboratorio de Biomembranas; Argentina
Fil: Curto, Maria de Los Angeles. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
Fil: Capurro, Claudia Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Ciencias Fisiológicas. Laboratorio de Biomembranas; Argentina
Materia
PERMEABILIDAD AL AGUA
PH INTRACELULAR
UROGUANILIN
CELULAS T84
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/192971
Acceder
id CONICETDig_6c5a85a309c3bbdab5c421ca231f08e3
oai_identifier_str oai:ri.conicet.gov.ar:11336/192971
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Uroguanylin regulates net fluid secretion via the NHE2 isoform of the Na+/H+ exchanger in an intestinal cellular modelToriano, Roxana MabelOzu, MarceloPoliti, María T.Dorr, Ricardo AlfredoCurto, Maria de Los AngelesCapurro, Claudia GracielaPERMEABILIDAD AL AGUAPH INTRACELULARUROGUANILINCELULAS T84https://purl.org/becyt/ford/3.1https://purl.org/becyt/ford/3Uroguanylin (UGN) has been proposed as a key regulator of salt and water intestinal transport. Uroguanylin (UGN) activates cell-surface guanylate cyclase C receptor (GC-C) and modulates cellular function via cyclic GMP (cGMP), thus increasing electrolyte and net water secretion. It has been suggested that the action of UGN could involve the Na+/H+ exchanger, but the actual contribution of this transporter still remains unclear. The objective of our study was to investigate the putative effects of UGN on some members of the Na+/H+ exchanger (NHE) family, as well as to clarify its consequences on transepithelial fluid flow in T84 cells. In order to do so, transepithelial fluid flow (Jv) was studied by optic techniques and intracellular pH (pHi) was measured with a fluorescence method. Results showed that NHE2 is found at the apical membrane and has a major role in Na+ absorption; NHE1 and NHE4 are localized at the basolateral membrane with a house-keeping role in steady state pHi. Cell exposure to apical UGN increases net secretory Jv, without changing short-circuit currents nor transepithelial resistance, and reduces NHE2 activity. Therefore, at physiological pH, the effect on net Jv was produced mainly by a reduction in normal Na+ absorption through NHE2, rather than by the stimulation of electrolyte secretion. Our study shows that the effect of UGN on pHi is GC-C/cGMP-mediated and enhanced by sildenafil, thus involving PDE5 enzyme. Additionally, cell exposure to apical UGN results in intracellular alkalinization, probably due to indirect effects on basolateral NHE1 and NHE4, which have a major role in pHi regulation.Fil: Toriano, Roxana Mabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Ciencias Fisiológicas. Laboratorio de Biomembranas; ArgentinaFil: Ozu, Marcelo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Ciencias Fisiológicas. Laboratorio de Biomembranas; ArgentinaFil: Politi, María T.. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Ciencias Fisiológicas. Laboratorio de Biomembranas; ArgentinaFil: Dorr, Ricardo Alfredo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Ciencias Fisiológicas. Laboratorio de Biomembranas; ArgentinaFil: Curto, Maria de Los Angeles. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; ArgentinaFil: Capurro, Claudia Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Ciencias Fisiológicas. Laboratorio de Biomembranas; ArgentinaKarger2011-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/192971Toriano, Roxana Mabel; Ozu, Marcelo; Politi, María T.; Dorr, Ricardo Alfredo; Curto, Maria de Los Angeles; et al.; Uroguanylin regulates net fluid secretion via the NHE2 isoform of the Na+/H+ exchanger in an intestinal cellular model; Karger; Cellular Physiology and Biochemistry; 28; 8-2011; 733-7421015-8987CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.karger.com/Article/Pdf/335767info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2026-06-10T09:56:35Zoai:ri.conicet.gov.ar:11336/192971instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982026-06-10 09:56:36.16CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Uroguanylin regulates net fluid secretion via the NHE2 isoform of the Na+/H+ exchanger in an intestinal cellular model
title Uroguanylin regulates net fluid secretion via the NHE2 isoform of the Na+/H+ exchanger in an intestinal cellular model
spellingShingle Uroguanylin regulates net fluid secretion via the NHE2 isoform of the Na+/H+ exchanger in an intestinal cellular model
Toriano, Roxana Mabel
PERMEABILIDAD AL AGUA
PH INTRACELULAR
UROGUANILIN
CELULAS T84
title_short Uroguanylin regulates net fluid secretion via the NHE2 isoform of the Na+/H+ exchanger in an intestinal cellular model
title_full Uroguanylin regulates net fluid secretion via the NHE2 isoform of the Na+/H+ exchanger in an intestinal cellular model
title_fullStr Uroguanylin regulates net fluid secretion via the NHE2 isoform of the Na+/H+ exchanger in an intestinal cellular model
title_full_unstemmed Uroguanylin regulates net fluid secretion via the NHE2 isoform of the Na+/H+ exchanger in an intestinal cellular model
title_sort Uroguanylin regulates net fluid secretion via the NHE2 isoform of the Na+/H+ exchanger in an intestinal cellular model
dc.creator.none.fl_str_mv Toriano, Roxana Mabel
Ozu, Marcelo
Politi, María T.
Dorr, Ricardo Alfredo
Curto, Maria de Los Angeles
Capurro, Claudia Graciela
author Toriano, Roxana Mabel
author_facet Toriano, Roxana Mabel
Ozu, Marcelo
Politi, María T.
Dorr, Ricardo Alfredo
Curto, Maria de Los Angeles
Capurro, Claudia Graciela
author_role author
author2 Ozu, Marcelo
Politi, María T.
Dorr, Ricardo Alfredo
Curto, Maria de Los Angeles
Capurro, Claudia Graciela
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv PERMEABILIDAD AL AGUA
PH INTRACELULAR
UROGUANILIN
CELULAS T84
topic PERMEABILIDAD AL AGUA
PH INTRACELULAR
UROGUANILIN
CELULAS T84
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.1
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv Uroguanylin (UGN) has been proposed as a key regulator of salt and water intestinal transport. Uroguanylin (UGN) activates cell-surface guanylate cyclase C receptor (GC-C) and modulates cellular function via cyclic GMP (cGMP), thus increasing electrolyte and net water secretion. It has been suggested that the action of UGN could involve the Na+/H+ exchanger, but the actual contribution of this transporter still remains unclear. The objective of our study was to investigate the putative effects of UGN on some members of the Na+/H+ exchanger (NHE) family, as well as to clarify its consequences on transepithelial fluid flow in T84 cells. In order to do so, transepithelial fluid flow (Jv) was studied by optic techniques and intracellular pH (pHi) was measured with a fluorescence method. Results showed that NHE2 is found at the apical membrane and has a major role in Na+ absorption; NHE1 and NHE4 are localized at the basolateral membrane with a house-keeping role in steady state pHi. Cell exposure to apical UGN increases net secretory Jv, without changing short-circuit currents nor transepithelial resistance, and reduces NHE2 activity. Therefore, at physiological pH, the effect on net Jv was produced mainly by a reduction in normal Na+ absorption through NHE2, rather than by the stimulation of electrolyte secretion. Our study shows that the effect of UGN on pHi is GC-C/cGMP-mediated and enhanced by sildenafil, thus involving PDE5 enzyme. Additionally, cell exposure to apical UGN results in intracellular alkalinization, probably due to indirect effects on basolateral NHE1 and NHE4, which have a major role in pHi regulation.
Fil: Toriano, Roxana Mabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Ciencias Fisiológicas. Laboratorio de Biomembranas; Argentina
Fil: Ozu, Marcelo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Ciencias Fisiológicas. Laboratorio de Biomembranas; Argentina
Fil: Politi, María T.. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Ciencias Fisiológicas. Laboratorio de Biomembranas; Argentina
Fil: Dorr, Ricardo Alfredo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Ciencias Fisiológicas. Laboratorio de Biomembranas; Argentina
Fil: Curto, Maria de Los Angeles. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
Fil: Capurro, Claudia Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina. Universidad de Buenos Aires. Facultad de Medicina. Departamento de Ciencias Fisiológicas. Laboratorio de Biomembranas; Argentina
description Uroguanylin (UGN) has been proposed as a key regulator of salt and water intestinal transport. Uroguanylin (UGN) activates cell-surface guanylate cyclase C receptor (GC-C) and modulates cellular function via cyclic GMP (cGMP), thus increasing electrolyte and net water secretion. It has been suggested that the action of UGN could involve the Na+/H+ exchanger, but the actual contribution of this transporter still remains unclear. The objective of our study was to investigate the putative effects of UGN on some members of the Na+/H+ exchanger (NHE) family, as well as to clarify its consequences on transepithelial fluid flow in T84 cells. In order to do so, transepithelial fluid flow (Jv) was studied by optic techniques and intracellular pH (pHi) was measured with a fluorescence method. Results showed that NHE2 is found at the apical membrane and has a major role in Na+ absorption; NHE1 and NHE4 are localized at the basolateral membrane with a house-keeping role in steady state pHi. Cell exposure to apical UGN increases net secretory Jv, without changing short-circuit currents nor transepithelial resistance, and reduces NHE2 activity. Therefore, at physiological pH, the effect on net Jv was produced mainly by a reduction in normal Na+ absorption through NHE2, rather than by the stimulation of electrolyte secretion. Our study shows that the effect of UGN on pHi is GC-C/cGMP-mediated and enhanced by sildenafil, thus involving PDE5 enzyme. Additionally, cell exposure to apical UGN results in intracellular alkalinization, probably due to indirect effects on basolateral NHE1 and NHE4, which have a major role in pHi regulation.
publishDate 2011
dc.date.none.fl_str_mv 2011-08
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
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://hdl.handle.net/11336/192971
Toriano, Roxana Mabel; Ozu, Marcelo; Politi, María T.; Dorr, Ricardo Alfredo; Curto, Maria de Los Angeles; et al.; Uroguanylin regulates net fluid secretion via the NHE2 isoform of the Na+/H+ exchanger in an intestinal cellular model; Karger; Cellular Physiology and Biochemistry; 28; 8-2011; 733-742
1015-8987
CONICET Digital
CONICET
url http://hdl.handle.net/11336/192971
identifier_str_mv Toriano, Roxana Mabel; Ozu, Marcelo; Politi, María T.; Dorr, Ricardo Alfredo; Curto, Maria de Los Angeles; et al.; Uroguanylin regulates net fluid secretion via the NHE2 isoform of the Na+/H+ exchanger in an intestinal cellular model; Karger; Cellular Physiology and Biochemistry; 28; 8-2011; 733-742
1015-8987
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.karger.com/Article/Pdf/335767
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
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Karger
publisher.none.fl_str_mv Karger
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1867629605375967232
score 12.83248

Publicaciones similares