Effects of monensin on amylase release from mouse parotid acini

Am J Physiol. 1981 May;240(5):C189-92. doi: 10.1152/ajpcell.1981.240.5.C189.

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amylases / metabolism*
  • Animals
  • Calcium / physiology
  • Carbachol / pharmacology
  • Furans / pharmacology*
  • In Vitro Techniques
  • Isoproterenol / pharmacology
  • Mice
  • Monensin / pharmacology*
  • Parotid Gland / drug effects
  • Parotid Gland / enzymology*
  • Sodium / physiology

Substances

  • Furans
  • Carbachol
  • Monensin
  • Sodium
  • Amylases
  • Isoproterenol
  • Calcium