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1 Department of Molecular Oral Physiology, The University of Tokushima Graduate School, Institute of Health Biosciences, Tokushima-Shi, Tokushima, Japan; Membrane Biology Section, Gene Therapy Branch, National Institue of Health, National Institute of Dental and Craniofacial Research, Bethesda, Maryland, USA
2 Department of Histology, Nippon Dental University School of Dentistry, Tokyo, Japan
3 Department of Molecular Oral Physiology, The University of Tokushima Graduate School, Institute of Health Biosciences, Tokushima-Shi, Tokushima, Japan; Department of Periodontology, Gadjah Mada University, Faculty of Dentistry, Yogyakarta, Indonesia
4 Department of Molecular Oral Physiology, The University of Tokushima Graduate School, Institute of Health Biosciences, Tokushima-Shi, Tokushima, Japan
* To whom correspondence should be addressed. E-mail: hosoi{at}dent.tokushima-u.ac.jp.
Aquaporin 5 (AQP5), an exocrine-type water channel, was detected in the rat duodenum by Western blotting, and was localized by immunohistochemistry in the secretory granule membranes, as well as in the apical and lateral aspects of the plasma membrane, of Brunner's gland cells. Incubation of duodenal slices with vasoactive intestinal polypeptide (VIP) in vitro significantly increased the amount of AQP5 in the apical membrane fraction in a dose and time-dependent manner, with the amount reaching a plateau at 100 nM VIP and becoming near maximal after a 30-sec incubation. Protein kinase inhibitors, 1-(5-isoquinolinesulfonyl)-2-methylpiperazine dihydrochloride (H-7, 50 µM), and N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide (H-89; PKA-specific, 1 µM) blocked this increase but a PKC-specific inhibitor, calphostin C, did not, implying the involvement of PKA but not PKC in this cellular event. Intravenous injection with VIP (40 µg/ kg body weight) provoked dilation of the lumen of the Brunner's gland at 2 and 7 min, and increased the staining intensity of AQP5 in the apical and lateral membranes. AQP1 (both non-glycosylated and glycosylated forms) was also found to localize in the apical and basolateral membranes of cells of Brunner's gland; VIP, however, did not provoke any significant change in the AQP1 level in the apical membrane, as judged from the results of the above in vitro and in vivo experiments. These results suggest that VIP induced the exocytosis of granule contents and simultaneously caused translocation of AQP5, but not of AQP1, to the apical membrane in Brunner's gland cells.
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