Background: Several aquaporins (a family of integral membrane proteins) have been recently
identified in the mammalian gastrointestinal tract, and their involvement in the movement of fluid
and small solutes has been suggested. In this direction we investigated, in some regions of the rat
gastrointestinal tract, the presence and localization of aquaporin-6, given its peculiar function as an
ion selective channel.
Results: RT-PCR and immunoblotting experiments showed that aquaporin-6 was expressed in all
the investigated portions of the rat gastrointestinal tract. The RT-PCR experiments showed that
aquaporin-6 transcript was highly expressed in small intestine and rectum, and less in stomach,
caecum and colon. In addition, jejunal mRNA expression was specifically stimulated by feeding.
Immunoblotting analysis showed a major band with a molecular weight of about 55 kDa
corresponding to the aquaporin-6 protein dimer; this band was stronger in the stomach and large
intestine than in the small intestine. Immunoblotting analysis of brush border membrane vesicle
preparations showed an intense signal for aquaporin-6 protein.
The results of in situ hybridization experiments demonstrate that aquaporin-6 transcript is present
in the isthmus, neck and basal regions of the stomach lining, and throughout the crypt-villus axis in
both small and large intestine. In the latter regions, immunohistochemistry revealed strong
aquaporin-6 labelling in the apical membrane of the surface epithelial cells, while weak or no
labelling was observed in the crypt cells. In the stomach, an intense staining was observed in mucous
neck cells and lower signal in principal cells and some parietal cells.
Conclusion: The results indicate that aquaporin-6 is distributed throughout the gastrointestinal
tract. Aquaporin-6 localization at the apical pole of the superficial epithelial cells and its
upregulation by feeding suggest that it may be involved in movements of water and anions through
the epithelium of the villi