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  • Title: Changes of aquaporin 5-distribution during release and reaccumulation of secretory granules in isoproterenol-treated mouse parotid gland.
    Author: Matsuzaki T, Ablimit A, Suzuki T, Aoki T, Hagiwara H, Takata K.
    Journal: J Electron Microsc (Tokyo); 2006 Jun; 55(3):183-9. PubMed ID: 16899467.
    Abstract:
    Water channel aquaporin 5 (AQP5) is present in the apical membrane of the salivary gland acinar cells. We examined changes of AQP5-distribution during the fusion process of secretory granule membranes into the apical membrane and subsequent recovery process in the mouse parotid gland by administering isoproterenol (IPR) in vivo. We performed immunoperoxidase, immunofluorescence and immunoelectron microscopy. In the basal state, AQP5 was localized mainly in the apical membrane of the acinar cell. It was also present in the basolateral membrane to a lesser extent. When IPR was administered to mice, dot-like, vesicle-like and vacuole-like labeling for AQP5 was seen in the subapical regions by light microscopy. By immunoelectron microscopy, AQP5 was localized at both the apical and basolateral plasma membranes in the basal state. At 5 and 30 min after the IPR-administration, acinar lumen became enlarged and small invaginations formed by fusion of secretory granules were seen. AQP5 was positive along the apical plasma membrane and its small invaginations. At 60 min, large invaginations of the lumen were formed. AQP5 remained positive in the membrane of these large invaginations. At 6 h, large invaginations disappeared and AQP5 was localized in the apical plasma membrane. AQP5 was restricted to plasma membranes and continuous invaginations formed by the exocytosis of secretory granules. AQP5 was not detected in the cytoplasm. These observations show that AQP5 does not seem to be endocytosed during the membrane recycling process following the exocytosis.
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