Functional characterization and localization of AQP3 in the human colon
Water channels or aquaporins (AQPs) have been identified in a large variety of tissues. Nevertheless, their role in the human gastrointestinal tract, where their action is essential for the reabsorption and secretion of water and electrolytes, is still unclear. The purpose of the present study was t...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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Associação Brasileira de Divulgação Científica
1999-10-01
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| Series: | Brazilian Journal of Medical and Biological Research |
| Subjects: | |
| Online Access: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1999001000018 |
| _version_ | 1819230903203790848 |
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| author | C. Silberstein A. Kierbel G. Amodeo E. Zotta F. Bigi D. Berkowski C. Ibarra |
| author_facet | C. Silberstein A. Kierbel G. Amodeo E. Zotta F. Bigi D. Berkowski C. Ibarra |
| author_sort | C. Silberstein |
| collection | DOAJ |
| description | Water channels or aquaporins (AQPs) have been identified in a large variety of tissues. Nevertheless, their role in the human gastrointestinal tract, where their action is essential for the reabsorption and secretion of water and electrolytes, is still unclear. The purpose of the present study was to investigate the structure and function of water channels expressed in the human colon. A cDNA fragment of about 420 bp with a 98% identity to human AQP3 was amplified from human stomach, small intestine and colon by reverse transcription polymerase chain reaction (RT-PCR) and a transcript of 2.2 kb was expressed more abundantly in colon than in jejunum, ileum and stomach as indicated by Northern blots. Expression of mRNA from the colon of adults and children but not from other gastrointestinal regions in Xenopus oocytes enhanced the osmotic water permeability, and the urea and glycerol transport in a manner sensitive to an antisense AQP3 oligonucleotide, indicating the presence of functional AQP3. Immunocytochemistry and immunofluorescence studies in human colon revealed that the AQP3 protein is restricted to the villus epithelial cells. The immunostaining within these cells was more intense in the apical than in the basolateral membranes. The presence of AQP3 in villus epithelial cells suggests that AQP3 is implicated in water absorption across human colonic surface cells. |
| first_indexed | 2024-12-23T11:36:27Z |
| format | Article |
| id | doaj.art-a16c95ed323a4493aa3b30da943cd61c |
| institution | Directory Open Access Journal |
| issn | 0100-879X 1414-431X |
| language | English |
| last_indexed | 2024-12-23T11:36:27Z |
| publishDate | 1999-10-01 |
| publisher | Associação Brasileira de Divulgação Científica |
| record_format | Article |
| series | Brazilian Journal of Medical and Biological Research |
| spelling | doaj.art-a16c95ed323a4493aa3b30da943cd61c2022-12-21T17:48:38ZengAssociação Brasileira de Divulgação CientíficaBrazilian Journal of Medical and Biological Research0100-879X1414-431X1999-10-0132101303131310.1590/S0100-879X1999001000018Functional characterization and localization of AQP3 in the human colonC. SilbersteinA. KierbelG. AmodeoE. ZottaF. BigiD. BerkowskiC. IbarraWater channels or aquaporins (AQPs) have been identified in a large variety of tissues. Nevertheless, their role in the human gastrointestinal tract, where their action is essential for the reabsorption and secretion of water and electrolytes, is still unclear. The purpose of the present study was to investigate the structure and function of water channels expressed in the human colon. A cDNA fragment of about 420 bp with a 98% identity to human AQP3 was amplified from human stomach, small intestine and colon by reverse transcription polymerase chain reaction (RT-PCR) and a transcript of 2.2 kb was expressed more abundantly in colon than in jejunum, ileum and stomach as indicated by Northern blots. Expression of mRNA from the colon of adults and children but not from other gastrointestinal regions in Xenopus oocytes enhanced the osmotic water permeability, and the urea and glycerol transport in a manner sensitive to an antisense AQP3 oligonucleotide, indicating the presence of functional AQP3. Immunocytochemistry and immunofluorescence studies in human colon revealed that the AQP3 protein is restricted to the villus epithelial cells. The immunostaining within these cells was more intense in the apical than in the basolateral membranes. The presence of AQP3 in villus epithelial cells suggests that AQP3 is implicated in water absorption across human colonic surface cells.http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1999001000018absorptive epitheliumhuman colonwater channelsaquaporinsAQP3 |
| spellingShingle | C. Silberstein A. Kierbel G. Amodeo E. Zotta F. Bigi D. Berkowski C. Ibarra Functional characterization and localization of AQP3 in the human colon Brazilian Journal of Medical and Biological Research absorptive epithelium human colon water channels aquaporins AQP3 |
| title | Functional characterization and localization of AQP3 in the human colon |
| title_full | Functional characterization and localization of AQP3 in the human colon |
| title_fullStr | Functional characterization and localization of AQP3 in the human colon |
| title_full_unstemmed | Functional characterization and localization of AQP3 in the human colon |
| title_short | Functional characterization and localization of AQP3 in the human colon |
| title_sort | functional characterization and localization of aqp3 in the human colon |
| topic | absorptive epithelium human colon water channels aquaporins AQP3 |
| url | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1999001000018 |
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