Rat Parotid Acinar Cells (rat + parotid_acinar_cell)

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Selected Abstracts


Redistribution of small GTP-binding protein, Rab27B, in rat parotid acinar cells after stimulation with isoproterenol

EUROPEAN JOURNAL OF ORAL SCIENCES, Issue 3 2009
Akane Imai
Small GTP-binding protein, Rab27, has been implicated in the regulation of different types of membrane trafficking, including melanosome transport in melanocytes and regulated secretion events in a wide variety of secretory cells. We have previously shown that Rab27 is involved in the control of isoproterenol (IPR)-induced amylase release from rat parotid acinar cells. Although Rab27 is predominantly localized on secretory granules under resting conditions, changes to its intracellular localization after ,-stimulation have never been elucidated. The present study investigated IPR-induced redistribution of Rab27B in the parotid acinar cells, revealing translocation from secretory granules to the subapical region after 5 min of IPR treatment and then diffusion into the cytosol after 30 min of IPR treatment. Dissociation of Rab27B from the apical plasma membrane is probably mediated through the Rab GDP dissociation inhibitor (GDI) in the cytosol extracting GDP-bound Rab protein from membranes, as a dramatic increase in the amount of the Rab27B,GDI complex in the cytosol was observed 30 min after stimulation with IPR. These results indicate that, in parotid acinar cells, Rab27B is translocated, in a time-dependent manner, from secretory granules into the apical plasma membrane as a result of exposure to IPR, and then into the cytosol through binding with the GDI. [source]


P2X7 receptors in rat parotid acinar cells: formation of large pores

AUTONOMIC & AUTACOID PHARMACOLOGY, Issue 4 2001
Simon J. Gibbons
1 Permeabilization of cells mediated by P2X7 receptors occurs to varied degrees in native and heterologous expression systems. Previous studies on P2X7 receptors in parotid acinar cells suggested that ATP does not permeabilize these cells. 2 Modification of the assay conditions showed that ATP permeabilizes freshly dissociated rat parotid acinar cells to the fluorescent dye YOPRO-1. 3 The pharmacological and physiological properties of this effect indicate that permeabilization is mediated by the P2X7 receptor. Adenosine 5,-triphosphate (ATP) and 3,- O -(4-benzoyl)benzoyl adenosine 5,-triphosphate (BzBzATP) were effective agonists with EC50 values of 49.3 and 0.6 ,M, respectively. 4 Permeabilization was best observed in low divalent cation concentrations and at physiological temperatures. Previous studies failed to detect permeabilization because of the sensitivity of this effect to temperature and divalent cations. 5 An important consideration in understanding the effect of divalent cations is that the fluorescence of YOPRO-1/nucleic acid complexes is directly quenched by addition of divalent cations. This must be considered if quantitative study of the interaction of divalent cations with P2X7 receptors is carried out using fluorescent DNA-binding dyes. 6 In summary, our data show that P2X7 receptors in parotid acinar cells can form large pores in the plasma membrane. This property likely contributes to signalling and may be cytotoxic and have particular significance in damaged or inflamed salivary glands. [source]