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AQP1 Is Not Only a Water Channel: It Contributes to Cell Migration through Lin7/Beta-Catenin
BACKGROUND: AQP1 belongs to aquaporins family, water-specific, membrane-channel proteins expressed in diverse tissues. Recent papers showed that during angiogenesis, AQP1 is expressed preferentially by microvessels, favoring angiogenesis via the increase of permeability In particular, in AQP1 null m...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2009
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2701997/ https://www.ncbi.nlm.nih.gov/pubmed/19584911 http://dx.doi.org/10.1371/journal.pone.0006167 |
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author | Monzani, Elena Bazzotti, Riccardo Perego, Carla La Porta, Caterina A. M. |
author_facet | Monzani, Elena Bazzotti, Riccardo Perego, Carla La Porta, Caterina A. M. |
author_sort | Monzani, Elena |
collection | PubMed |
description | BACKGROUND: AQP1 belongs to aquaporins family, water-specific, membrane-channel proteins expressed in diverse tissues. Recent papers showed that during angiogenesis, AQP1 is expressed preferentially by microvessels, favoring angiogenesis via the increase of permeability In particular, in AQP1 null mice, endothelial cell migration is impaired without altering their proliferation or adhesion. Therefore, AQP1 has been proposed as a novel promoter of tumor angiogenesis. METHODS/FINDINGS: Using targeted silencing of AQP1 gene expression, an impairment in the organization of F-actin and a reduced migration capacity was demonstrated in human endothelial and melanoma cell lines. Interestingly, we showed, for the first time, that AQP1 co-immunoprecipitated with Lin-7. Lin7-GFP experiments confirmed co-immunoprecipitation. In addition, the knock down of AQP1 decreased the level of expression of Lin-7 and β-catenin and the inhibition of proteasome contrasted partially such a decrease. CONCLUSIONS/SIGNIFICANCE: All together, our findings show that AQP1 plays a role inside the cells through Lin-7/β-catenin interaction. Such a role of AQP1 is the same in human melanoma and endothelial cells, suggesting that AQP1 plays a global physiological role. A model is presented. |
format | Text |
id | pubmed-2701997 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-27019972009-07-08 AQP1 Is Not Only a Water Channel: It Contributes to Cell Migration through Lin7/Beta-Catenin Monzani, Elena Bazzotti, Riccardo Perego, Carla La Porta, Caterina A. M. PLoS One Research Article BACKGROUND: AQP1 belongs to aquaporins family, water-specific, membrane-channel proteins expressed in diverse tissues. Recent papers showed that during angiogenesis, AQP1 is expressed preferentially by microvessels, favoring angiogenesis via the increase of permeability In particular, in AQP1 null mice, endothelial cell migration is impaired without altering their proliferation or adhesion. Therefore, AQP1 has been proposed as a novel promoter of tumor angiogenesis. METHODS/FINDINGS: Using targeted silencing of AQP1 gene expression, an impairment in the organization of F-actin and a reduced migration capacity was demonstrated in human endothelial and melanoma cell lines. Interestingly, we showed, for the first time, that AQP1 co-immunoprecipitated with Lin-7. Lin7-GFP experiments confirmed co-immunoprecipitation. In addition, the knock down of AQP1 decreased the level of expression of Lin-7 and β-catenin and the inhibition of proteasome contrasted partially such a decrease. CONCLUSIONS/SIGNIFICANCE: All together, our findings show that AQP1 plays a role inside the cells through Lin-7/β-catenin interaction. Such a role of AQP1 is the same in human melanoma and endothelial cells, suggesting that AQP1 plays a global physiological role. A model is presented. Public Library of Science 2009-07-08 /pmc/articles/PMC2701997/ /pubmed/19584911 http://dx.doi.org/10.1371/journal.pone.0006167 Text en Monzani et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Monzani, Elena Bazzotti, Riccardo Perego, Carla La Porta, Caterina A. M. AQP1 Is Not Only a Water Channel: It Contributes to Cell Migration through Lin7/Beta-Catenin |
title | AQP1 Is Not Only a Water Channel: It Contributes to Cell Migration through Lin7/Beta-Catenin |
title_full | AQP1 Is Not Only a Water Channel: It Contributes to Cell Migration through Lin7/Beta-Catenin |
title_fullStr | AQP1 Is Not Only a Water Channel: It Contributes to Cell Migration through Lin7/Beta-Catenin |
title_full_unstemmed | AQP1 Is Not Only a Water Channel: It Contributes to Cell Migration through Lin7/Beta-Catenin |
title_short | AQP1 Is Not Only a Water Channel: It Contributes to Cell Migration through Lin7/Beta-Catenin |
title_sort | aqp1 is not only a water channel: it contributes to cell migration through lin7/beta-catenin |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2701997/ https://www.ncbi.nlm.nih.gov/pubmed/19584911 http://dx.doi.org/10.1371/journal.pone.0006167 |
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