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J. Biochem, 1990, Vol. 108, No. 1 99-102
© 1990 Japanese Biochemical Society

research-article

Evidence for the Involvement of cAMP-Dependent Protein Kinase in the Exocytosis of Amylase from Parotid Acinar Cells1

Taishin Takuma

Department of Oral Biochemistry, School of Dentistry, Higashi Nippon Gakuen University Tobetsu, Hokkaido 061-02

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 N5-benzoyl-cAMP plus 8-thiomethyl-cAMP (RII-directed) or N5-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.

1This study was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.


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