Isolation of a novel aquaglyceroporin from a marine teleost (Sparus auratus) Function and tissue distribution
Autor(a) principal: | |
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Data de Publicação: | 2004 |
Outros Autores: | , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10400.1/5463 |
Resumo: | The aquaporins (formerly called the major intrinsic protein family) are transmembrane channel proteins. The family includes the CHIP group, which are functionally characterised as water channels and the GLP group, which are specialised for glycerol transport. The present study reports the identification and characterisation of a novel GLP family member in a teleost fish, the sea bream Sparus auratus. A sea bream aquaporin (sbAQP) cDNA of 1047·bp and encoding a protein of 298·amino acids was isolated from a kidney cDNA library. Functional characterization of the sbAQP using a Xenopus oocyte assay revealed that the isolated cDNA stimulated osmotic water permeability in a mercury-sensitive manner and also stimulated urea and glycerol uptake. Northern blotting demonstrated that sbAQP was expressed at high levels in the posterior region of the gut, where two transcripts were identified (1.6·kb and 2·kb), and in kidney, where a single transcript was present (2·kb). In situ hybridisation studies with a sbAQP riboprobe revealed its presence in the lamina propria and smooth muscle layer of the posterior region of the gut and in epithelial cells of some kidney tubules. sbAQP was also present in putative chloride cells of the gill. Phylogenetic analysis of sbAQP, including putative GLP genes from Fugu rubripes, revealed that it did not group with any of the previously isolated vertebrate GLPs and instead formed a separate group, suggesting that it may be a novel GLP member. |
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Isolation of a novel aquaglyceroporin from a marine teleost (Sparus auratus) Function and tissue distributionAquaporinGLPIn situ localisationMultiple transcriptsFugu rubripesGastrointestinal tractKidneyTeleost fishSea breamSparus auratusThe aquaporins (formerly called the major intrinsic protein family) are transmembrane channel proteins. The family includes the CHIP group, which are functionally characterised as water channels and the GLP group, which are specialised for glycerol transport. The present study reports the identification and characterisation of a novel GLP family member in a teleost fish, the sea bream Sparus auratus. A sea bream aquaporin (sbAQP) cDNA of 1047·bp and encoding a protein of 298·amino acids was isolated from a kidney cDNA library. Functional characterization of the sbAQP using a Xenopus oocyte assay revealed that the isolated cDNA stimulated osmotic water permeability in a mercury-sensitive manner and also stimulated urea and glycerol uptake. Northern blotting demonstrated that sbAQP was expressed at high levels in the posterior region of the gut, where two transcripts were identified (1.6·kb and 2·kb), and in kidney, where a single transcript was present (2·kb). In situ hybridisation studies with a sbAQP riboprobe revealed its presence in the lamina propria and smooth muscle layer of the posterior region of the gut and in epithelial cells of some kidney tubules. sbAQP was also present in putative chloride cells of the gill. Phylogenetic analysis of sbAQP, including putative GLP genes from Fugu rubripes, revealed that it did not group with any of the previously isolated vertebrate GLPs and instead formed a separate group, suggesting that it may be a novel GLP member.This work was supported by project PRAXIS XXI/2/2.1/BIA/211/94 from the Portuguese National Science and Technology Foundation (FCT), co-financed by EU structural funds, DG-Fisheries Project Q5RS-2002-00784 (CRYOCYTE) and an EU Biotech grant (QLRT2000-00778). C.R.A.S., J.C.R.C. and J.F. were in receipt of FCT fellowships PRAXIS XXI/BPD/22040/99, PRAXIS XXI/BD/19925/99BPD/22033/99, respectively.The Company of BiologistsSapientiaSantos, C. R. A.Estêvão, DulceFuentes, J.Cardoso, João CRFabra, MercedesPassos, A. L.Detmers, F. J.Deen, P. M. T.Cerda, J.Power, Deborah2014-10-24T10:39:05Z20042004-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.1/5463engC. R. A. Santos, M. D. Estêvão, J. Fuentes, J. C. R. Cardoso, M. Fabra, A. L. Passos, F. J. Detmers, P. M. T. Deen, J. Cerdà and D. M. Power, "Isolation of a novel aquaglyceroporin from a marine teleost (Sparus auratus) Function and tissue distribution" in The Journal of Experimental Biology 207, 1217-1227.AUT: DPO00386; MES00382http://dx.doi.org/10.1242/jeb.00867info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-07-24T10:16:40ZPortal AgregadorONG |
dc.title.none.fl_str_mv |
Isolation of a novel aquaglyceroporin from a marine teleost (Sparus auratus) Function and tissue distribution |
title |
Isolation of a novel aquaglyceroporin from a marine teleost (Sparus auratus) Function and tissue distribution |
spellingShingle |
Isolation of a novel aquaglyceroporin from a marine teleost (Sparus auratus) Function and tissue distribution Santos, C. R. A. Aquaporin GLP In situ localisation Multiple transcripts Fugu rubripes Gastrointestinal tract Kidney Teleost fish Sea bream Sparus auratus |
title_short |
Isolation of a novel aquaglyceroporin from a marine teleost (Sparus auratus) Function and tissue distribution |
title_full |
Isolation of a novel aquaglyceroporin from a marine teleost (Sparus auratus) Function and tissue distribution |
title_fullStr |
Isolation of a novel aquaglyceroporin from a marine teleost (Sparus auratus) Function and tissue distribution |
title_full_unstemmed |
Isolation of a novel aquaglyceroporin from a marine teleost (Sparus auratus) Function and tissue distribution |
title_sort |
Isolation of a novel aquaglyceroporin from a marine teleost (Sparus auratus) Function and tissue distribution |
author |
Santos, C. R. A. |
author_facet |
Santos, C. R. A. Estêvão, Dulce Fuentes, J. Cardoso, João CR Fabra, Mercedes Passos, A. L. Detmers, F. J. Deen, P. M. T. Cerda, J. Power, Deborah |
author_role |
author |
author2 |
Estêvão, Dulce Fuentes, J. Cardoso, João CR Fabra, Mercedes Passos, A. L. Detmers, F. J. Deen, P. M. T. Cerda, J. Power, Deborah |
author2_role |
author author author author author author author author author |
dc.contributor.none.fl_str_mv |
Sapientia |
dc.contributor.author.fl_str_mv |
Santos, C. R. A. Estêvão, Dulce Fuentes, J. Cardoso, João CR Fabra, Mercedes Passos, A. L. Detmers, F. J. Deen, P. M. T. Cerda, J. Power, Deborah |
dc.subject.por.fl_str_mv |
Aquaporin GLP In situ localisation Multiple transcripts Fugu rubripes Gastrointestinal tract Kidney Teleost fish Sea bream Sparus auratus |
topic |
Aquaporin GLP In situ localisation Multiple transcripts Fugu rubripes Gastrointestinal tract Kidney Teleost fish Sea bream Sparus auratus |
description |
The aquaporins (formerly called the major intrinsic protein family) are transmembrane channel proteins. The family includes the CHIP group, which are functionally characterised as water channels and the GLP group, which are specialised for glycerol transport. The present study reports the identification and characterisation of a novel GLP family member in a teleost fish, the sea bream Sparus auratus. A sea bream aquaporin (sbAQP) cDNA of 1047·bp and encoding a protein of 298·amino acids was isolated from a kidney cDNA library. Functional characterization of the sbAQP using a Xenopus oocyte assay revealed that the isolated cDNA stimulated osmotic water permeability in a mercury-sensitive manner and also stimulated urea and glycerol uptake. Northern blotting demonstrated that sbAQP was expressed at high levels in the posterior region of the gut, where two transcripts were identified (1.6·kb and 2·kb), and in kidney, where a single transcript was present (2·kb). In situ hybridisation studies with a sbAQP riboprobe revealed its presence in the lamina propria and smooth muscle layer of the posterior region of the gut and in epithelial cells of some kidney tubules. sbAQP was also present in putative chloride cells of the gill. Phylogenetic analysis of sbAQP, including putative GLP genes from Fugu rubripes, revealed that it did not group with any of the previously isolated vertebrate GLPs and instead formed a separate group, suggesting that it may be a novel GLP member. |
publishDate |
2004 |
dc.date.none.fl_str_mv |
2004 2004-01-01T00:00:00Z 2014-10-24T10:39:05Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10400.1/5463 |
url |
http://hdl.handle.net/10400.1/5463 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
C. R. A. Santos, M. D. Estêvão, J. Fuentes, J. C. R. Cardoso, M. Fabra, A. L. Passos, F. J. Detmers, P. M. T. Deen, J. Cerdà and D. M. Power, "Isolation of a novel aquaglyceroporin from a marine teleost (Sparus auratus) Function and tissue distribution" in The Journal of Experimental Biology 207, 1217-1227. AUT: DPO00386; MES00382 http://dx.doi.org/10.1242/jeb.00867 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
The Company of Biologists |
publisher.none.fl_str_mv |
The Company of Biologists |
dc.source.none.fl_str_mv |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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