Activation and distribution of rat parotid cAMP-dependent protein kinase following beta-adrenergic receptor stimulation in vitro.

The extent of activation of parotid protein kinase A (EC 2.7.1.37) isozymes was determined using dispersed cells and an 8-N3-[32P]-cAMP photoprobe. Cold-trap studies indicated that 40% of type I protein kinase A was activated following maximal beta-adrenergic receptor stimulation, whereas type II activation was less than 20%. Both cytosolic and microsomal type I activation occurred rapidly after stimulation and both remain activated throughout the entire secretory period. The dose-response relationship for the isotypes following beta-adrenergic receptor activation demonstrated a greater extent of type I activation at maximal concentration of agonist. Although protein kinase A may not be the only kinase involved in rat parotid amylase release, these findings add further evidence of a direct regulatory role for this kinase, with type I having potentially a greater role than type II.