Aqp9 mediates lactate transport in human placenta as an alternative energy substrate

Autores
Medina Mora, Yollyseth Astrid; Sierra, Matias Nicolas; Anud, Carolina Valeria; Szpilbarg, Natalia; Damiano, Alicia Ermelinda
Año de publicación
2020
Idioma
inglés
Tipo de recurso
documento de conferencia
Estado
versión publicada
Descripción
Emerging evidence shows that placental aquaporin-9 (AQP9) is notinvolved in the transfer of water between the mother and the fetus.However, its role in human placenta is still unknown. AQP9 is anaquaglyceroporin that also permeates other solutes such as lactate. Inbrain, AQP9 may transport lactate as an alternative energy substrate.OBJECTIVE: Our aim was to evaluate the participation of AQP9 inthe lactate transfer across the human placenta.METHODS: This study was approved by the ethics committee of theHospital Nacional Dr. Prof. A. Posadas. Explants from normal termplacentas were cultured in low glucose with or without L-lactate, andin presence and absence of AQP9 inhibitors (0.3 mM HgCl2, a general blocker of AQPs, or 0.5mM Phloretin, to block AQP9). Normalglucose medium was used as control. Cell viability was assessed byMTT assay and LDH release. Apoptosis indexes were analyzed byBax/Bcl-2 protein expression ratio and TUNEL assay.RESULTS: In low glucose medium, MTT decreased while LDHrelease did not change compared to controls, suggesting that celldeath is not due to necrosis. Moreover, Bax/Bcl-2 ratio and apoptoticnuclei increased (n=5, p <0.02) and the blocking of AQP9 did notabrogate apoptosis. However, when explants were cultured in lowglucose medium supplemented with L-lactate, explant viability andapoptotic indexes were similar to controls indicating that L-lactatecould be replacing glucose as an energy substrate. In this case, theblocking of AQP9 resulted in an increase in cell death (n=4, p <0.05),proposing that this protein has a role in lactate transport.CONCLUSION: Our results show that placental AQP9 may havea key role in lactate transport as an alternative energy substrate.Thus, the blocking of lactate transport mediated by AQP9 negativelyaffects the survival of trophoblast cells.
Fil: Medina Mora, Yollyseth Astrid. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Fisiología y Biofísica Bernardo Houssay. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Fisiología y Biofísica Bernardo Houssay; Argentina
Fil: Sierra, Matias Nicolas. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Ciencias Biológicas. Cátedra de Biología Celular y Molecular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Fisiología y Biofísica Bernardo Houssay. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Fisiología y Biofísica Bernardo Houssay; Argentina
Fil: Anud, Carolina Valeria. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Ciencias Biológicas. Cátedra de Biología Celular y Molecular; Argentina
Fil: Szpilbarg, Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Fisiología y Biofísica Bernardo Houssay. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Fisiología y Biofísica Bernardo Houssay; Argentina
Fil: Damiano, Alicia Ermelinda. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Fisiología y Biofísica Bernardo Houssay. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Fisiología y Biofísica Bernardo Houssay; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Ciencias Biológicas. Cátedra de Biología Celular y Molecular; Argentina
LXV Reunión Anual de la Sociedad Argentina de Investigación Clínica; LXVIII Reunión Anual de la Sociedad Argentina de Inmunología y Reunión Anual de la Asociación Argentina de Fisiología
Argentina
Sociedad Argentina de Investigación Clínica
Sociedad Argentina de Inmunología
Asociación Argentina de Fisiología
Materia
AQP9
PLACENTA
LACTATE
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:11336/199439
Acceder
id CONICETDig_55ab575b41ff15d6983e80dddb5a78e3
oai_identifier_str oai:ri.conicet.gov.ar:11336/199439
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Aqp9 mediates lactate transport in human placenta as an alternative energy substrateMedina Mora, Yollyseth AstridSierra, Matias NicolasAnud, Carolina ValeriaSzpilbarg, NataliaDamiano, Alicia ErmelindaAQP9PLACENTALACTATEhttps://purl.org/becyt/ford/3.5https://purl.org/becyt/ford/3Emerging evidence shows that placental aquaporin-9 (AQP9) is notinvolved in the transfer of water between the mother and the fetus.However, its role in human placenta is still unknown. AQP9 is anaquaglyceroporin that also permeates other solutes such as lactate. Inbrain, AQP9 may transport lactate as an alternative energy substrate.OBJECTIVE: Our aim was to evaluate the participation of AQP9 inthe lactate transfer across the human placenta.METHODS: This study was approved by the ethics committee of theHospital Nacional Dr. Prof. A. Posadas. Explants from normal termplacentas were cultured in low glucose with or without L-lactate, andin presence and absence of AQP9 inhibitors (0.3 mM HgCl2, a general blocker of AQPs, or 0.5mM Phloretin, to block AQP9). Normalglucose medium was used as control. Cell viability was assessed byMTT assay and LDH release. Apoptosis indexes were analyzed byBax/Bcl-2 protein expression ratio and TUNEL assay.RESULTS: In low glucose medium, MTT decreased while LDHrelease did not change compared to controls, suggesting that celldeath is not due to necrosis. Moreover, Bax/Bcl-2 ratio and apoptoticnuclei increased (n=5, p <0.02) and the blocking of AQP9 did notabrogate apoptosis. However, when explants were cultured in lowglucose medium supplemented with L-lactate, explant viability andapoptotic indexes were similar to controls indicating that L-lactatecould be replacing glucose as an energy substrate. In this case, theblocking of AQP9 resulted in an increase in cell death (n=4, p <0.05),proposing that this protein has a role in lactate transport.CONCLUSION: Our results show that placental AQP9 may havea key role in lactate transport as an alternative energy substrate.Thus, the blocking of lactate transport mediated by AQP9 negativelyaffects the survival of trophoblast cells.Fil: Medina Mora, Yollyseth Astrid. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Fisiología y Biofísica Bernardo Houssay. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Fisiología y Biofísica Bernardo Houssay; ArgentinaFil: Sierra, Matias Nicolas. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Ciencias Biológicas. Cátedra de Biología Celular y Molecular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Fisiología y Biofísica Bernardo Houssay. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Fisiología y Biofísica Bernardo Houssay; ArgentinaFil: Anud, Carolina Valeria. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Ciencias Biológicas. Cátedra de Biología Celular y Molecular; ArgentinaFil: Szpilbarg, Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Fisiología y Biofísica Bernardo Houssay. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Fisiología y Biofísica Bernardo Houssay; ArgentinaFil: Damiano, Alicia Ermelinda. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Fisiología y Biofísica Bernardo Houssay. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Fisiología y Biofísica Bernardo Houssay; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Ciencias Biológicas. Cátedra de Biología Celular y Molecular; ArgentinaLXV Reunión Anual de la Sociedad Argentina de Investigación Clínica; LXVIII Reunión Anual de la Sociedad Argentina de Inmunología y Reunión Anual de la Asociación Argentina de FisiologíaArgentinaSociedad Argentina de Investigación ClínicaSociedad Argentina de InmunologíaAsociación Argentina de FisiologíaFundación Revista Medicina2020info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectReuniónJournalhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/199439Aqp9 mediates lactate transport in human placenta as an alternative energy substrate; LXV Reunión Anual de la Sociedad Argentina de Investigación Clínica; LXVIII Reunión Anual de la Sociedad Argentina de Inmunología y Reunión Anual de la Asociación Argentina de Fisiología; Argentina; 2020; 206-2060025-7680CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.saic.org.ar/reunion-anualNacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:46:41Zoai:ri.conicet.gov.ar:11336/199439instacron: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:34982025-10-15 15:46:41.334CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Aqp9 mediates lactate transport in human placenta as an alternative energy substrate
title Aqp9 mediates lactate transport in human placenta as an alternative energy substrate
spellingShingle Aqp9 mediates lactate transport in human placenta as an alternative energy substrate
Medina Mora, Yollyseth Astrid
AQP9
PLACENTA
LACTATE
title_short Aqp9 mediates lactate transport in human placenta as an alternative energy substrate
title_full Aqp9 mediates lactate transport in human placenta as an alternative energy substrate
title_fullStr Aqp9 mediates lactate transport in human placenta as an alternative energy substrate
title_full_unstemmed Aqp9 mediates lactate transport in human placenta as an alternative energy substrate
title_sort Aqp9 mediates lactate transport in human placenta as an alternative energy substrate
dc.creator.none.fl_str_mv Medina Mora, Yollyseth Astrid
Sierra, Matias Nicolas
Anud, Carolina Valeria
Szpilbarg, Natalia
Damiano, Alicia Ermelinda
author Medina Mora, Yollyseth Astrid
author_facet Medina Mora, Yollyseth Astrid
Sierra, Matias Nicolas
Anud, Carolina Valeria
Szpilbarg, Natalia
Damiano, Alicia Ermelinda
author_role author
author2 Sierra, Matias Nicolas
Anud, Carolina Valeria
Szpilbarg, Natalia
Damiano, Alicia Ermelinda
author2_role author
author
author
author
dc.subject.none.fl_str_mv AQP9
PLACENTA
LACTATE
topic AQP9
PLACENTA
LACTATE
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.5
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv Emerging evidence shows that placental aquaporin-9 (AQP9) is notinvolved in the transfer of water between the mother and the fetus.However, its role in human placenta is still unknown. AQP9 is anaquaglyceroporin that also permeates other solutes such as lactate. Inbrain, AQP9 may transport lactate as an alternative energy substrate.OBJECTIVE: Our aim was to evaluate the participation of AQP9 inthe lactate transfer across the human placenta.METHODS: This study was approved by the ethics committee of theHospital Nacional Dr. Prof. A. Posadas. Explants from normal termplacentas were cultured in low glucose with or without L-lactate, andin presence and absence of AQP9 inhibitors (0.3 mM HgCl2, a general blocker of AQPs, or 0.5mM Phloretin, to block AQP9). Normalglucose medium was used as control. Cell viability was assessed byMTT assay and LDH release. Apoptosis indexes were analyzed byBax/Bcl-2 protein expression ratio and TUNEL assay.RESULTS: In low glucose medium, MTT decreased while LDHrelease did not change compared to controls, suggesting that celldeath is not due to necrosis. Moreover, Bax/Bcl-2 ratio and apoptoticnuclei increased (n=5, p <0.02) and the blocking of AQP9 did notabrogate apoptosis. However, when explants were cultured in lowglucose medium supplemented with L-lactate, explant viability andapoptotic indexes were similar to controls indicating that L-lactatecould be replacing glucose as an energy substrate. In this case, theblocking of AQP9 resulted in an increase in cell death (n=4, p <0.05),proposing that this protein has a role in lactate transport.CONCLUSION: Our results show that placental AQP9 may havea key role in lactate transport as an alternative energy substrate.Thus, the blocking of lactate transport mediated by AQP9 negativelyaffects the survival of trophoblast cells.
Fil: Medina Mora, Yollyseth Astrid. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Fisiología y Biofísica Bernardo Houssay. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Fisiología y Biofísica Bernardo Houssay; Argentina
Fil: Sierra, Matias Nicolas. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Ciencias Biológicas. Cátedra de Biología Celular y Molecular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Fisiología y Biofísica Bernardo Houssay. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Fisiología y Biofísica Bernardo Houssay; Argentina
Fil: Anud, Carolina Valeria. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Ciencias Biológicas. Cátedra de Biología Celular y Molecular; Argentina
Fil: Szpilbarg, Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Fisiología y Biofísica Bernardo Houssay. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Fisiología y Biofísica Bernardo Houssay; Argentina
Fil: Damiano, Alicia Ermelinda. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Fisiología y Biofísica Bernardo Houssay. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Fisiología y Biofísica Bernardo Houssay; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Ciencias Biológicas. Cátedra de Biología Celular y Molecular; Argentina
LXV Reunión Anual de la Sociedad Argentina de Investigación Clínica; LXVIII Reunión Anual de la Sociedad Argentina de Inmunología y Reunión Anual de la Asociación Argentina de Fisiología
Argentina
Sociedad Argentina de Investigación Clínica
Sociedad Argentina de Inmunología
Asociación Argentina de Fisiología
description Emerging evidence shows that placental aquaporin-9 (AQP9) is notinvolved in the transfer of water between the mother and the fetus.However, its role in human placenta is still unknown. AQP9 is anaquaglyceroporin that also permeates other solutes such as lactate. Inbrain, AQP9 may transport lactate as an alternative energy substrate.OBJECTIVE: Our aim was to evaluate the participation of AQP9 inthe lactate transfer across the human placenta.METHODS: This study was approved by the ethics committee of theHospital Nacional Dr. Prof. A. Posadas. Explants from normal termplacentas were cultured in low glucose with or without L-lactate, andin presence and absence of AQP9 inhibitors (0.3 mM HgCl2, a general blocker of AQPs, or 0.5mM Phloretin, to block AQP9). Normalglucose medium was used as control. Cell viability was assessed byMTT assay and LDH release. Apoptosis indexes were analyzed byBax/Bcl-2 protein expression ratio and TUNEL assay.RESULTS: In low glucose medium, MTT decreased while LDHrelease did not change compared to controls, suggesting that celldeath is not due to necrosis. Moreover, Bax/Bcl-2 ratio and apoptoticnuclei increased (n=5, p <0.02) and the blocking of AQP9 did notabrogate apoptosis. However, when explants were cultured in lowglucose medium supplemented with L-lactate, explant viability andapoptotic indexes were similar to controls indicating that L-lactatecould be replacing glucose as an energy substrate. In this case, theblocking of AQP9 resulted in an increase in cell death (n=4, p <0.05),proposing that this protein has a role in lactate transport.CONCLUSION: Our results show that placental AQP9 may havea key role in lactate transport as an alternative energy substrate.Thus, the blocking of lactate transport mediated by AQP9 negativelyaffects the survival of trophoblast cells.
publishDate 2020
dc.date.none.fl_str_mv 2020
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/conferenceObject
Reunión
Journal
http://purl.org/coar/resource_type/c_5794
info:ar-repo/semantics/documentoDeConferencia
status_str publishedVersion
format conferenceObject
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/199439
Aqp9 mediates lactate transport in human placenta as an alternative energy substrate; LXV Reunión Anual de la Sociedad Argentina de Investigación Clínica; LXVIII Reunión Anual de la Sociedad Argentina de Inmunología y Reunión Anual de la Asociación Argentina de Fisiología; Argentina; 2020; 206-206
0025-7680
CONICET Digital
CONICET
url http://hdl.handle.net/11336/199439
identifier_str_mv Aqp9 mediates lactate transport in human placenta as an alternative energy substrate; LXV Reunión Anual de la Sociedad Argentina de Investigación Clínica; LXVIII Reunión Anual de la Sociedad Argentina de Inmunología y Reunión Anual de la Asociación Argentina de Fisiología; Argentina; 2020; 206-206
0025-7680
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.saic.org.ar/reunion-anual
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
dc.coverage.none.fl_str_mv Nacional
dc.publisher.none.fl_str_mv Fundación Revista Medicina
publisher.none.fl_str_mv Fundación Revista Medicina
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
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