title: Subcellular redistribution of AQP5 by vasoactive intestinal polypeptide in the Brunner's gland of the rat duodenum.
abstract: Aquaporin (AQP)5, an exocrine-type water channel, was detected in the rat duodenum by Western blot analysis, 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-s incubation. Protein kinase inhibitors, 1-(5-isoquinolinesulfonyl)-2-methylpiperazine dihydrochloride (H-7, 50 muM), and N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide (H-89; PKA-specific, 1 muM) blocked this increase, but PKC-specific inhibitor calphostin C did not, implying the involvement of PKA but not PKC in this cellular event. Intravenous injection with VIP (40 mug/kg body wt) 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 nonglycosylated 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.
authors.affiliation: Dept. of Molecular Oral Physiology, Institute of Health Biosciences, The Univ. of Tokushima Graduate School, Tokushima-Shi, Tokushima 770-8504, Japan.
authors.forename: Most Nahid
authors.initials: MN
authors.lastname: Parvin
authors.forename: Shingo
authors.initials: S
authors.lastname: Kurabuchi
authors.forename: Kwartarini
authors.initials: K
authors.lastname: Murdiastuti
authors.forename: Chenjuan
authors.initials: C
authors.lastname: Yao
authors.forename: Chisato
authors.initials: C
authors.lastname: Kosugi-Tanaka
authors.forename: Tetsuya
authors.initials: T
authors.lastname: Akamatsu
authors.forename: Norio
authors.initials: N
authors.lastname: Kanamori
authors.forename: Kazuo
authors.initials: K
authors.lastname: Hosoi
mesh_terms: D000818:Animals; D051398:Aquaporin 1; D051402:Aquaporin 5; D020346:Aquaporins / Q000493:pharmacokinetics* / Q000502:physiology; D002011:Brunner Glands / Q000502:physiology*; D004305:Dose-Response Relationship, Drug; D005089:Exocytosis; D047908:Intracellular Signaling Peptides and Proteins / Q000494:pharmacology; D008297:Male; D008565:Membrane Proteins / Q000493:pharmacokinetics*; D011494:Protein Kinases / Q000494:pharmacology; D051381:Rats; D017207:Rats, Sprague-Dawley; D014660:Vasoactive Intestinal Peptide / Q000494:pharmacology*
chemical_list: C496022:Aqp1 protein, rat; C496040:Aqp5 protein, rat; D051402:Aquaporin 5; D020346:Aquaporins; D047908:Intracellular Signaling Peptides and Proteins; D008565:Membrane Proteins; C015482:protein kinase modulator; D051398:Aquaporin 1; D014660:Vasoactive Intestinal Peptide; D011494:Protein Kinases