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  • Title: Effects of monensin on amylase release from mouse parotid acini.
    Author: Watson EL, Farnham CJ, Friedman J, Farnham W.
    Journal: Am J Physiol; 1981 May; 240(5):C189-92. PubMed ID: 6165249.
    Abstract:
    Isolated mouse parotid acinar cells (acini) were prepared by enzyme digestion, divalent cation depletion, and mechanical shearing. Acini were found to be morphologically intact, i.e., 95% viable as judged by trypan blue exclusion. Amylase release by the cholinergic agonist carbachol, by the beta-adrenergic agonist isoproterenol, and by monensin was similar to responses obtained in mouse parotid fragments. Monensin-stimulated amylase release was associated with enhanced 22Na+ uptake and 45Ca2+ efflux; monensin did not affect 45Ca2+ uptake. In the absence of extracellular Na+, the response to monensin (50 microM) was reduced from 162 +/- 33.5 to 12.4 +/- 0.5%; monensin also failed to stimulate 45Ca2+ efflux. Similar results were obtained with isoproterenol (10(-6) M). The results suggest that Na+ ions may play a role in amylase release possibly by releasing Ca2+ from internal stores.
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