Calmodulin activation and calcium regulation of parotid gland adenylate cyclase

M. T. Piascik, M. Babich, K. L. Jacobson, E. L. Watson

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The effect of Ca2+ on the adenylate cyclase activity associated with membranes prepared from mouse parotid gland has been examined. Ca2+ stimulated then inhibited adenylate cyclase activity, with values for half-maximal stimulation and inhibition of 0.6 and 10 μM, respectively. Maximal activation (1.4-fold) was observed at 2 μM free Ca2+. These membranes contained 1.2 μg calmodulin/mg protein. Exogenous calmodulin (0.2-1.2 μg) activated, in a concentration-dependent manner, adenylate cyclase activity, with maximal activation being 2.5-fold at 12 μg calmodulin. Preparation of membranes in 2 mM ethyleneglycol-bis(β-aminoethylether)-N,N,N',N'-tetraacetic acid (EGTA) resulted not only in a significant decrease in calmodulin levels (0.5 μg calmodulin/mg protein) but also in a loss of the ability of Ca2+ to stimulate the enzyme. Exogenous calmodulin restored the ability of Ca2+ to stimulate the adenylate cyclase activity associated with EGTA-treated membranes. Trifluoperazine (50 μM) blocked the ability of Ca2+ to activate adenylate cyclase activity in control membranes. The effect of trifluoperazine could be reversed by exogenous calmodulin (0.5 or 5.0 μg). These data indicate that calmoduin mediates the activation of parotid gland adenylate cyclase by Ca2+ and that Ca2+, at concentrations which stimulate and inhibit amylase secretion, can activate and inhibit adenylate cyclase activity.

Original languageEnglish (US)
JournalAmerican Journal of Physiology - Cell Physiology
Issue number4
StatePublished - 1986
Externally publishedYes


ASJC Scopus subject areas

  • Cell Biology
  • Clinical Biochemistry
  • Physiology

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