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Aquaporin-11: A channel protein lacking apparent transport function expressed in brain
BACKGROUND: The aquaporins are a family of integral membrane proteins composed of two subfamilies: the orthodox aquaporins, which transport only water, and the aquaglyceroporins, which transport glycerol, urea, or other small solutes. Two recently described aquaporins, numbers 11 and 12, appear to b...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2006
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1475587/ https://www.ncbi.nlm.nih.gov/pubmed/16650285 http://dx.doi.org/10.1186/1471-2091-7-14 |
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author | Gorelick, Daniel A Praetorius, Jeppe Tsunenari, Takashi Nielsen, Søren Agre, Peter |
author_facet | Gorelick, Daniel A Praetorius, Jeppe Tsunenari, Takashi Nielsen, Søren Agre, Peter |
author_sort | Gorelick, Daniel A |
collection | PubMed |
description | BACKGROUND: The aquaporins are a family of integral membrane proteins composed of two subfamilies: the orthodox aquaporins, which transport only water, and the aquaglyceroporins, which transport glycerol, urea, or other small solutes. Two recently described aquaporins, numbers 11 and 12, appear to be more distantly related to the other mammalian aquaporins and aquaglyceroporins. RESULTS: We report on the characterization of Aquaporin-11 (AQP11). AQP11 RNA and protein is found in multiple rat tissues, including kidney, liver, testes and brain. AQP11 has a unique distribution in brain, appearing in Purkinje cell dendrites, hippocampal neurons of CA1 and CA2, and cerebral cortical neurons. Immunofluorescent staining of Purkinje cells indicates that AQP11 is intracellular. Unlike other aquaporins, Xenopus oocytes expressing AQP11 in the plasma membrane failed to transport water, glycerol, urea, or ions. CONCLUSION: AQP11 is functionally distinct from other proteins of the aquaporin superfamily and could represent a new aquaporin subfamily. Further studies are necessary to elucidate the role of AQP11 in the brain. |
format | Text |
id | pubmed-1475587 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2006 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-14755872006-06-08 Aquaporin-11: A channel protein lacking apparent transport function expressed in brain Gorelick, Daniel A Praetorius, Jeppe Tsunenari, Takashi Nielsen, Søren Agre, Peter BMC Biochem Research Article BACKGROUND: The aquaporins are a family of integral membrane proteins composed of two subfamilies: the orthodox aquaporins, which transport only water, and the aquaglyceroporins, which transport glycerol, urea, or other small solutes. Two recently described aquaporins, numbers 11 and 12, appear to be more distantly related to the other mammalian aquaporins and aquaglyceroporins. RESULTS: We report on the characterization of Aquaporin-11 (AQP11). AQP11 RNA and protein is found in multiple rat tissues, including kidney, liver, testes and brain. AQP11 has a unique distribution in brain, appearing in Purkinje cell dendrites, hippocampal neurons of CA1 and CA2, and cerebral cortical neurons. Immunofluorescent staining of Purkinje cells indicates that AQP11 is intracellular. Unlike other aquaporins, Xenopus oocytes expressing AQP11 in the plasma membrane failed to transport water, glycerol, urea, or ions. CONCLUSION: AQP11 is functionally distinct from other proteins of the aquaporin superfamily and could represent a new aquaporin subfamily. Further studies are necessary to elucidate the role of AQP11 in the brain. BioMed Central 2006-05-01 /pmc/articles/PMC1475587/ /pubmed/16650285 http://dx.doi.org/10.1186/1471-2091-7-14 Text en Copyright © 2006 Gorelick et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Gorelick, Daniel A Praetorius, Jeppe Tsunenari, Takashi Nielsen, Søren Agre, Peter Aquaporin-11: A channel protein lacking apparent transport function expressed in brain |
title | Aquaporin-11: A channel protein lacking apparent transport function expressed in brain |
title_full | Aquaporin-11: A channel protein lacking apparent transport function expressed in brain |
title_fullStr | Aquaporin-11: A channel protein lacking apparent transport function expressed in brain |
title_full_unstemmed | Aquaporin-11: A channel protein lacking apparent transport function expressed in brain |
title_short | Aquaporin-11: A channel protein lacking apparent transport function expressed in brain |
title_sort | aquaporin-11: a channel protein lacking apparent transport function expressed in brain |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1475587/ https://www.ncbi.nlm.nih.gov/pubmed/16650285 http://dx.doi.org/10.1186/1471-2091-7-14 |
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