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Evidence for the involvement of cAMP-dependent protein kinase in the exocytosis of amylase from parotid acinar cells.

Authors
Type
Published Article
Journal
Journal of biochemistry
Publication Date
Volume
108
Issue
1
Pages
99–102
Identifiers
PMID: 1699933
Source
Medline
License
Unknown

Abstract

To determine the role of cAMP-dependent protein kinase in the exocytosis of amylase from rat parotid acini, I studied the effects of various cAMP analogues on amylase release and protein phosphorylation in saponin-permeabilized parotid cells. The dose-dependent responses of amylase release and protein phosphorylation evoked by cAMP, dibutyryl-cAMP, and 8-chlorophenylthio-cAMP were closely correlated. Furthermore, when the permeabilized cells were incubated with a combination of site-selective cAMP analogues, such as N6-benzoyl-cAMP plus 8-thiomethyl-cAMP (RII-directed) or N6-benzoyl-cAMP plus 8-aminohexylamino-cAMP (RI-directed), synergistic stimulation of amylase release was clearly observed. As reported previously [T. Takuma (1988) Biochem. J. 256, 867-871], however, the protein phosphorylation evoked by 8-chlorophenylthio-cAMP was markedly inhibited by H-8 without a significant decrease in amylase release. These results suggest that cAMP-dependent protein kinase is involved in the regulation of amylase exocytosis, although the role of its catalytic subunit is still uncertain.

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