Aquaporin-8-facilitated mitochondrial ammonia transport

Autores
Soria, Leandro Raul; Fanelli, Elena; Altamura, Nicola; Svelto, Maria; Marinelli, Raul Alberto; Calamita, Giuseppe
Año de publicación
2010
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Aquaporin-8 (AQP8) is a membrane channel permeable to water and ammonia. As AQP8 is expressed in the inner mitochondrial membrane of several mammalian tissues, we studied the effect of the AQP8 expression on the mitochondrial transport of ammonia. Recombinant rat AQP8 was expressed in the yeast Saccharomyces cerevisiae. The presence of AQP8 in the inner membrane of yeast mitochondria was demonstrated by subcellular fractionation and immunoblotting analysis. The ammonia transport was determined in isolated mitochondria by stopped flow light scattering using formamide as ammonia analog. We found that the presence of AQP8 increased by threefold mitochondrial formamide transport. AQP8-facilitated mitochondrial formamide transport in rat native tissue was confirmed in liver (a mitochondrial AQP8-expressing tissue) vs. brain (a mitochondrial AQP8 non-expressing tissue). Comparative studies indicated that the AQP8-mediated mitochondrial movement of formamide was markedly higher than that of water. Together, our data suggest that ammonia diffusional transport is a major function formitochondrial AQP8.
Fil: Soria, Leandro Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Fisiología Experimental. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Fisiología Experimental; Argentina
Fil: Fanelli, Elena. Università degli Studi di Bari; Italia
Fil: Altamura, Nicola. Istituto di Biomembrane e Bioenergetica; Italia
Fil: Svelto, Maria. Università degli Studi di Bari; Italia
Fil: Marinelli, Raul Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Fisiología Experimental. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Fisiología Experimental; Argentina
Fil: Calamita, Giuseppe. Università degli Studi di Bari; Italia
Materia
INNER MITOCHONDRIAL MEMBRANE
AMMONIA TRANSPORT
YEAST EXPRESSION SYSTEM
AQUA-AMMONIAPORIN
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:11336/276650
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Aquaporin-8-facilitated mitochondrial ammonia transportSoria, Leandro RaulFanelli, ElenaAltamura, NicolaSvelto, MariaMarinelli, Raul AlbertoCalamita, GiuseppeINNER MITOCHONDRIAL MEMBRANEAMMONIA TRANSPORTYEAST EXPRESSION SYSTEMAQUA-AMMONIAPORINhttps://purl.org/becyt/ford/3.1https://purl.org/becyt/ford/3Aquaporin-8 (AQP8) is a membrane channel permeable to water and ammonia. As AQP8 is expressed in the inner mitochondrial membrane of several mammalian tissues, we studied the effect of the AQP8 expression on the mitochondrial transport of ammonia. Recombinant rat AQP8 was expressed in the yeast Saccharomyces cerevisiae. The presence of AQP8 in the inner membrane of yeast mitochondria was demonstrated by subcellular fractionation and immunoblotting analysis. The ammonia transport was determined in isolated mitochondria by stopped flow light scattering using formamide as ammonia analog. We found that the presence of AQP8 increased by threefold mitochondrial formamide transport. AQP8-facilitated mitochondrial formamide transport in rat native tissue was confirmed in liver (a mitochondrial AQP8-expressing tissue) vs. brain (a mitochondrial AQP8 non-expressing tissue). Comparative studies indicated that the AQP8-mediated mitochondrial movement of formamide was markedly higher than that of water. Together, our data suggest that ammonia diffusional transport is a major function formitochondrial AQP8.Fil: Soria, Leandro Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Fisiología Experimental. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Fisiología Experimental; ArgentinaFil: Fanelli, Elena. Università degli Studi di Bari; ItaliaFil: Altamura, Nicola. Istituto di Biomembrane e Bioenergetica; ItaliaFil: Svelto, Maria. Università degli Studi di Bari; ItaliaFil: Marinelli, Raul Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Fisiología Experimental. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Fisiología Experimental; ArgentinaFil: Calamita, Giuseppe. Università degli Studi di Bari; ItaliaAcademic Press Inc Elsevier Science2010-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/276650Soria, Leandro Raul; Fanelli, Elena; Altamura, Nicola; Svelto, Maria; Marinelli, Raul Alberto; et al.; Aquaporin-8-facilitated mitochondrial ammonia transport; Academic Press Inc Elsevier Science; Biochemical and Biophysical Research Communications; 393; 2; 1-2010; 217-2210006-291XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0006291X10001671info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbrc.2010.01.104info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-12-23T14:32:34Zoai:ri.conicet.gov.ar:11336/276650instacron: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:34982025-12-23 14:32:34.713CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Aquaporin-8-facilitated mitochondrial ammonia transport
title Aquaporin-8-facilitated mitochondrial ammonia transport
spellingShingle Aquaporin-8-facilitated mitochondrial ammonia transport
Soria, Leandro Raul
INNER MITOCHONDRIAL MEMBRANE
AMMONIA TRANSPORT
YEAST EXPRESSION SYSTEM
AQUA-AMMONIAPORIN
title_short Aquaporin-8-facilitated mitochondrial ammonia transport
title_full Aquaporin-8-facilitated mitochondrial ammonia transport
title_fullStr Aquaporin-8-facilitated mitochondrial ammonia transport
title_full_unstemmed Aquaporin-8-facilitated mitochondrial ammonia transport
title_sort Aquaporin-8-facilitated mitochondrial ammonia transport
dc.creator.none.fl_str_mv Soria, Leandro Raul
Fanelli, Elena
Altamura, Nicola
Svelto, Maria
Marinelli, Raul Alberto
Calamita, Giuseppe
author Soria, Leandro Raul
author_facet Soria, Leandro Raul
Fanelli, Elena
Altamura, Nicola
Svelto, Maria
Marinelli, Raul Alberto
Calamita, Giuseppe
author_role author
author2 Fanelli, Elena
Altamura, Nicola
Svelto, Maria
Marinelli, Raul Alberto
Calamita, Giuseppe
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv INNER MITOCHONDRIAL MEMBRANE
AMMONIA TRANSPORT
YEAST EXPRESSION SYSTEM
AQUA-AMMONIAPORIN
topic INNER MITOCHONDRIAL MEMBRANE
AMMONIA TRANSPORT
YEAST EXPRESSION SYSTEM
AQUA-AMMONIAPORIN
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.1
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv Aquaporin-8 (AQP8) is a membrane channel permeable to water and ammonia. As AQP8 is expressed in the inner mitochondrial membrane of several mammalian tissues, we studied the effect of the AQP8 expression on the mitochondrial transport of ammonia. Recombinant rat AQP8 was expressed in the yeast Saccharomyces cerevisiae. The presence of AQP8 in the inner membrane of yeast mitochondria was demonstrated by subcellular fractionation and immunoblotting analysis. The ammonia transport was determined in isolated mitochondria by stopped flow light scattering using formamide as ammonia analog. We found that the presence of AQP8 increased by threefold mitochondrial formamide transport. AQP8-facilitated mitochondrial formamide transport in rat native tissue was confirmed in liver (a mitochondrial AQP8-expressing tissue) vs. brain (a mitochondrial AQP8 non-expressing tissue). Comparative studies indicated that the AQP8-mediated mitochondrial movement of formamide was markedly higher than that of water. Together, our data suggest that ammonia diffusional transport is a major function formitochondrial AQP8.
Fil: Soria, Leandro Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Fisiología Experimental. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Fisiología Experimental; Argentina
Fil: Fanelli, Elena. Università degli Studi di Bari; Italia
Fil: Altamura, Nicola. Istituto di Biomembrane e Bioenergetica; Italia
Fil: Svelto, Maria. Università degli Studi di Bari; Italia
Fil: Marinelli, Raul Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Fisiología Experimental. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Fisiología Experimental; Argentina
Fil: Calamita, Giuseppe. Università degli Studi di Bari; Italia
description Aquaporin-8 (AQP8) is a membrane channel permeable to water and ammonia. As AQP8 is expressed in the inner mitochondrial membrane of several mammalian tissues, we studied the effect of the AQP8 expression on the mitochondrial transport of ammonia. Recombinant rat AQP8 was expressed in the yeast Saccharomyces cerevisiae. The presence of AQP8 in the inner membrane of yeast mitochondria was demonstrated by subcellular fractionation and immunoblotting analysis. The ammonia transport was determined in isolated mitochondria by stopped flow light scattering using formamide as ammonia analog. We found that the presence of AQP8 increased by threefold mitochondrial formamide transport. AQP8-facilitated mitochondrial formamide transport in rat native tissue was confirmed in liver (a mitochondrial AQP8-expressing tissue) vs. brain (a mitochondrial AQP8 non-expressing tissue). Comparative studies indicated that the AQP8-mediated mitochondrial movement of formamide was markedly higher than that of water. Together, our data suggest that ammonia diffusional transport is a major function formitochondrial AQP8.
publishDate 2010
dc.date.none.fl_str_mv 2010-01
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/11336/276650
Soria, Leandro Raul; Fanelli, Elena; Altamura, Nicola; Svelto, Maria; Marinelli, Raul Alberto; et al.; Aquaporin-8-facilitated mitochondrial ammonia transport; Academic Press Inc Elsevier Science; Biochemical and Biophysical Research Communications; 393; 2; 1-2010; 217-221
0006-291X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/276650
identifier_str_mv Soria, Leandro Raul; Fanelli, Elena; Altamura, Nicola; Svelto, Maria; Marinelli, Raul Alberto; et al.; Aquaporin-8-facilitated mitochondrial ammonia transport; Academic Press Inc Elsevier Science; Biochemical and Biophysical Research Communications; 393; 2; 1-2010; 217-221
0006-291X
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.sciencedirect.com/science/article/abs/pii/S0006291X10001671
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbrc.2010.01.104
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
dc.publisher.none.fl_str_mv Academic Press Inc Elsevier Science
publisher.none.fl_str_mv Academic Press Inc Elsevier Science
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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score 12.952241

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