α1-Adrenoceptor-Induced Trafficking of Aquaporin-5 to the Apical Plasma Membrane of Rat Parotid Cells

1999 ◽  
Vol 265 (1) ◽  
pp. 94-100 ◽  
Author(s):  
Yasuko Ishikawa ◽  
Mariusz T. Skowronski ◽  
Noriko Inoue ◽  
Hajime Ishida
Keyword(s):  
Plasma Membrane ◽  
Apical Plasma Membrane ◽  
Aquaporin 5 ◽  
Parotid Cells ◽  
Rat Parotid

scholarly journals GRAMP 100: a membrane protein concentrated on secretory granule membranes and the apical cell surface in exocrine acinar cells.

1992 ◽  
Vol 40 (12) ◽  
pp. 1827-1835 ◽  
Author(s):  
S M Laurie ◽  
M B Mixon ◽  
J D Castle
Keyword(s):  
Plasma Membrane ◽  
Apical Cell ◽  
Reduced Form ◽  
Electron Microscopic Level ◽  
Apical Plasma Membrane ◽  
Cell Fractionation ◽  
Immunocytochemical Localization ◽  
Electron Microscopic ◽  
Common Component ◽  
Rat Parotid

Using a monoclonal antibody (SG10A6) raised against secretion granule membranes of the rat parotid gland, we have identified an antigen that is a common component of both exocrine pancreatic and parotid granule membranes. SG10A6 (an IgM) immunoprecipitates antigen that migrates as a single band (M(r) approximately 80 KD unreduced; M(r) approximately 100 KD reduced) and immunoblots at least two polypeptides that are similar to the reduced and nonreduced immunoprecipitated antigen. This granule-associated membrane polypeptide (GRAMP 100; named for the apparent M(r) in reduced form) is also a prominent component of plasma membrane fractions. Immunocytochemical localization at the electron microscopic level demonstrates the presence of GRAMP 100 on granule membranes, especially condensing vacuoles and exocytotic figures, and the apical plasma membrane. Lower levels of antigen are detected on basolateral plasma membrane and on peri-Golgi membranes that may be part of the endosomal system. Both the cell fractionation and immunocytochemical localization indicate that GRAMP 100 differs in distribution from GRAMP 92 and 30K SCAMPs, two other components of exocrine granule membranes identified with monoclonal antibodies. To date, no polypeptides have been identified with this approach that are exclusive components of exocrine granule membranes.

Gene expression and localization of two types of AQP5 inXenopus tropicalisunder hydration and dehydration

2014 ◽  
Vol 307 (1) ◽  
pp. R44-R56 ◽  
Author(s):  
Yuki Shibata ◽  
Takahiro Sano ◽  
Nobuhito Tsuchiya ◽  
Reiko Okada ◽  
Hiroshi Mochida ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Urinary Bladder ◽  
Apical Plasma Membrane ◽  
Secretory Cells ◽  
Granular Cells ◽  
Aquaporin 5 ◽  
Water Reabsorption ◽  
Molecular Phylogenetic ◽  
Water Secretion ◽  
Hydration And Dehydration

Two types of aquaporin 5 (AQP5) genes ( aqp-xt5a and aqp-xt5b) were identified in the genome of Xenopus tropicalis by synteny comparison and molecular phylogenetic analysis. When the frogs were in water, AQP-xt5a mRNA was expressed in the skin and urinary bladder. The expression of AQP-xt5a mRNA was significantly increased in dehydrated frogs. AQP-xt5b mRNA was also detected in the skin and increased in response to dehydration. Additionally, AQP-xt5b mRNA began to be slightly expressed in the lung and stomach after dehydration. For the pelvic skin of hydrated frogs, immunofluorescence staining localized AQP-xt5a and AQP-xt5b to the cytoplasm of secretory cells of the granular glands and the apical plasma membrane of secretory cells of the small granular glands, respectively. After dehydration, the locations of both AQPs in their respective glands did not change, but AQP-xt5a was visualized in the cytoplasm of secretory cells of the small granular glands. For the urinary bladder, AQP-xt5a was observed in the apical plasma membrane and cytoplasm of a number of granular cells under normal hydration. After dehydration, AQP-xt5a was found in the apical membrane and cytoplasm of most granular cells. Injection of vasotocin into hydrated frogs did not induce these changes in the localization of AQP-xt5a in the small granular glands and urinary bladder, however. The results suggest that AQP-xt5a might be involved in water reabsorption from the urinary bladder during dehydration, whereas AQP-xt5b might play a role in water secretion from the small granular gland.

Activation of muscarinic receptors in rat parotid acinar cells induces AQP5 trafficking to nuclei and apical plasma membrane

2015 ◽  
Vol 1850 (4) ◽  
pp. 784-793 ◽  
Author(s):  
Gota Cho ◽  
Aneta M. Bragiel ◽  
Di Wang ◽  
Tomasz D. Pieczonka ◽  
Mariusz T. Skowronski ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Muscarinic Receptors ◽  
Acinar Cells ◽  
Apical Plasma Membrane ◽  
Parotid Acinar Cells ◽  
Rat Parotid

Immunolocalization of AQP-5 in rat parotid and submandibular salivary glands after stimulation or inhibition of secretion in vivo

2004 ◽  
Vol 287 (1) ◽  
pp. G151-G161 ◽  
Author(s):  
Veronika Gresz ◽  
Tae-Hwan Kwon ◽  
Hong Gong ◽  
Peter Agre ◽  
Martin C. Steward ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Subcellular Localization ◽  
Salivary Glands ◽  
Salivary Secretion ◽  
Apical Plasma Membrane ◽  
Secretory Cells ◽  
Muscarinic Agonist ◽  
Rat Parotid

In vitro studies of cultured salivary gland cells and gland slices have indicated that there may be regulated translocation of aquaporin (AQP)-5 between the apical plasma membrane and intracellular compartments of the secretory cells. However, it remains unknown whether AQP-5 in salivary glands is subject to regulated trafficking in vivo. To examine this possibility, we have investigated the subcellular localization of AQP-5 in rat parotid and submandibular glands fixed in vivo under conditions of stimulated or inhibited salivary secretion. Immunofluorescence and immunoelectron microscopy was used to determine the subcellular distribution of AQP-5 in control conditions following the stimulation of secretion with pilocarpine (a muscarinic agonist) or epinephrine (an α-adrenoceptor agonist) or during inhibition of basal secretion with atropine (a muscarinic antagonist) or phentolamine (an α-adrenoceptor antagonist). Under control conditions, >90% of AQP-5 was associated with the apical plasma membrane of acinar and intercalated duct cells, with only rare gold particles associated with intracellular membrane domains. Pilocarpine treatment dramatically increased saliva production but had no discernible effect on AQP-5 distribution. However, the increased salivary secretion was associated with luminal dilation and the appearance of a markedly punctate AQP-5 labeling pattern due to clustering of AQP-5 at the microvilli (especially evident in the parotid gland) after 10 min of drug injection. No changes in the subcellular localization of AQP-5 were seen in response to epinephrine, atropine, or phentolamine treatment compared with control tissues. Thus AQP-5 is localized predominantly in the apical plasma membrane under control conditions, and neither the onset nor the cessation of secretion is associated in vivo with any significant short-term translocation of AQP-5 between intracellular structures and the apical plasma membrane.

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