Cloning, characterisation and tissue distribution of an aquaporin-3 cDNA from fish (Sparus aurata)

Bibliographic Details
Main Author: Santos, CRA
Publication Date: 2001
Other Authors: Fuentes, Juan, Cardoso, João CR, Estêvão, Dulce, Power, Deborah
Language: eng
Source: Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
Download full: http://hdl.handle.net/10400.1/13434
Summary: The major intrinsic protein (MIP) family consists of several transmembrane channel proteins specific for water and neutral solutes. All proteins belonging to the MIP family evolved from two divergent bacterial paralogues, one giving rise to the CHIP group, functionally characterised as water channels and the other to the GLP group, specialised in glycerol transport. Three forms of MIP proteins belonging to the GLP group have been identified in mammals: aquaporin-3 (AQP-3), aquaporin-7 (AQP-7) and aquaporin-9 (AQP-9). We have recently cloned and characterised a GLP cDNA from the marine teleost sea bream (Sparus aurata) and studied its tissue distribution. Phylogenetic analysis revealed it was most like AQP-3 and further studies are now underway to determine its role in hydromineral balance.
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spelling Cloning, characterisation and tissue distribution of an aquaporin-3 cDNA from fish (Sparus aurata)The major intrinsic protein (MIP) family consists of several transmembrane channel proteins specific for water and neutral solutes. All proteins belonging to the MIP family evolved from two divergent bacterial paralogues, one giving rise to the CHIP group, functionally characterised as water channels and the other to the GLP group, specialised in glycerol transport. Three forms of MIP proteins belonging to the GLP group have been identified in mammals: aquaporin-3 (AQP-3), aquaporin-7 (AQP-7) and aquaporin-9 (AQP-9). We have recently cloned and characterised a GLP cDNA from the marine teleost sea bream (Sparus aurata) and studied its tissue distribution. Phylogenetic analysis revealed it was most like AQP-3 and further studies are now underway to determine its role in hydromineral balance.SapientiaSantos, CRAFuentes, JuanCardoso, João CREstêvão, DulcePower, Deborah2020-01-29T14:01:42Z20012001-01-01T00:00:00Zconference objectinfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://hdl.handle.net/10400.1/13434enginfo:eu-repo/semantics/openAccessreponame:Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiainstacron:RCAAP2025-02-18T17:37:15Zoai:sapientia.ualg.pt:10400.1/13434Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireinfo@rcaap.ptopendoar:https://opendoar.ac.uk/repository/71602025-05-28T20:29:10.554785Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiafalse
dc.title.none.fl_str_mv Cloning, characterisation and tissue distribution of an aquaporin-3 cDNA from fish (Sparus aurata)
title Cloning, characterisation and tissue distribution of an aquaporin-3 cDNA from fish (Sparus aurata)
spellingShingle Cloning, characterisation and tissue distribution of an aquaporin-3 cDNA from fish (Sparus aurata)
Santos, CRA
title_short Cloning, characterisation and tissue distribution of an aquaporin-3 cDNA from fish (Sparus aurata)
title_full Cloning, characterisation and tissue distribution of an aquaporin-3 cDNA from fish (Sparus aurata)
title_fullStr Cloning, characterisation and tissue distribution of an aquaporin-3 cDNA from fish (Sparus aurata)
title_full_unstemmed Cloning, characterisation and tissue distribution of an aquaporin-3 cDNA from fish (Sparus aurata)
title_sort Cloning, characterisation and tissue distribution of an aquaporin-3 cDNA from fish (Sparus aurata)
author Santos, CRA
author_facet Santos, CRA
Fuentes, Juan
Cardoso, João CR
Estêvão, Dulce
Power, Deborah
author_role author
author2 Fuentes, Juan
Cardoso, João CR
Estêvão, Dulce
Power, Deborah
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Sapientia
dc.contributor.author.fl_str_mv Santos, CRA
Fuentes, Juan
Cardoso, João CR
Estêvão, Dulce
Power, Deborah
description The major intrinsic protein (MIP) family consists of several transmembrane channel proteins specific for water and neutral solutes. All proteins belonging to the MIP family evolved from two divergent bacterial paralogues, one giving rise to the CHIP group, functionally characterised as water channels and the other to the GLP group, specialised in glycerol transport. Three forms of MIP proteins belonging to the GLP group have been identified in mammals: aquaporin-3 (AQP-3), aquaporin-7 (AQP-7) and aquaporin-9 (AQP-9). We have recently cloned and characterised a GLP cDNA from the marine teleost sea bream (Sparus aurata) and studied its tissue distribution. Phylogenetic analysis revealed it was most like AQP-3 and further studies are now underway to determine its role in hydromineral balance.
publishDate 2001
dc.date.none.fl_str_mv 2001
2001-01-01T00:00:00Z
2020-01-29T14:01:42Z
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