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...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2009-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC2701997?pdf=render |
| _version_ | 1819209975798431744 |
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| author | Elena Monzani Riccardo Bazzotti Carla Perego Caterina A M La Porta |
| author_facet | Elena Monzani Riccardo Bazzotti Carla Perego Caterina A M La Porta |
| author_sort | Elena Monzani |
| collection | DOAJ |
| 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 beta-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/beta-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. |
| first_indexed | 2024-12-23T06:03:50Z |
| format | Article |
| id | doaj.art-263b6682becb49be9cbf0d8c51f98f61 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-23T06:03:50Z |
| publishDate | 2009-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-263b6682becb49be9cbf0d8c51f98f612022-12-21T17:57:36ZengPublic Library of Science (PLoS)PLoS ONE1932-62032009-01-0147e616710.1371/journal.pone.0006167AQP1 is not only a water channel: it contributes to cell migration through Lin7/beta-catenin.Elena MonzaniRiccardo BazzottiCarla PeregoCaterina A M La PortaBACKGROUND: 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 beta-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/beta-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.http://europepmc.org/articles/PMC2701997?pdf=render |
| spellingShingle | Elena Monzani Riccardo Bazzotti Carla Perego Caterina A M La Porta AQP1 is not only a water channel: it contributes to cell migration through Lin7/beta-catenin. PLoS ONE |
| 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 |
| url | http://europepmc.org/articles/PMC2701997?pdf=render |
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