scholarly journals Role of protein kinase C-δ in isoproterenol-induced amylase release in rat parotid acinar cells

2009 ◽  
Vol 56 (Supplement) ◽  
pp. 368-370 ◽  
Author(s):  
Hiroshi Sugiya ◽  
Keitaro Satoh ◽  
Miwako Matsuki-Fukushima ◽  
Bing Qi ◽  
Ming-Yu Guo ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Acinar Cells ◽  
Amylase Release ◽  
Parotid Acinar Cells ◽  
Kinase C ◽  
Rat Parotid

scholarly journals Two modes of regulation of the phospholipase C-linked substance-P receptor in rat parotid acinar cells

1988 ◽  
Vol 253 (2) ◽  
pp. 459-466 ◽  
Author(s):  
H Sugiya ◽  
J F Obie ◽  
J W Putney
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Substance P ◽  
Acinar Cells ◽  
Control Mechanisms ◽  
Dependent Manner ◽  
Parotid Acinar Cells ◽  
Kinase C ◽  
Substance P Receptor ◽  
Rat Parotid

In rat parotid acinar cells prelabelled with [3H]inositol, substance P (100 nM) induced the formation of [3H]inositol 1,4,5-trisphosphate [Ins(1,4,5)P3]. Ins(1,4,5)P3 reached a maximum 7 s after substance P stimulation, and thereafter decreased and reached a stable value at 60 s. When the cells were exposed to substance P for 10, 30, 60, or 300 s, washed, and re-exposed to this peptide, the formation of [3H]inositol trisphosphate (InsP3) was attenuated in a time-dependent manner. In the cells pretreated as described above, the number of [3H]substance-P-binding sites (Bmax) was also decreased. Possible role(s) of Ca2+ and protein kinase (protein kinase C) control mechanisms in regulating substance P responses were investigated. Desensitization of substance P-induced InsP3 was not affected by the Ca2+ ionophore ionomycin, nor was it dependent on Ca2+ mobilization. On the other hand, in the presence of 4 beta-phorbol 12,13-dibutyrate (PDBu) and 12-O-tetradecanoyl-4 beta-phorbol 13-acetate, known activators of protein kinase C, substance P-induced InsP3 formation was inhibited. However, PDBu had no effect on [3H]substance P binding, whether present during the assay or when cells were pretreated. The persistent desensitization of InsP3 formation induced by substance P was not affected by PDBu. These results suggest that the persistent desensitization of InsP3 formation induced by substance P is a homologous process involving down-regulation of the substance P receptor; the mechanism does not appear to involve, or to be affected by, the Ca2+ or protein kinase C signalling systems. Protein kinase C activation can, however, inhibit substance P-induced InsP3 formation, which may indicate the presence of a negative-feedback control on the substance P pathway.

Phosphorylation of myristoylated alanine-rich C kinase substrate is involved in the cAMP-dependent amylase release in parotid acinar cells

2009 ◽  
Vol 296 (6) ◽  
pp. G1382-G1390 ◽  
Author(s):  
Keitaro Satoh ◽  
Miwako Matsuki-Fukushima ◽  
Bing Qi ◽  
Ming-Yu Guo ◽  
Takanori Narita ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Acinar Cells ◽  
Cellular Migration ◽  
Intracellular Camp ◽  
Dependent Manner ◽  
Amylase Release ◽  
Kinase Substrate ◽  
Parotid Acinar Cells ◽  
Dependent Protein ◽  
Rat Parotid

Myristoylated alanine-rich C kinase substrate (MARCKS) is known as a major cellular substrate for protein kinase C (PKC). MARCKS has been implicated in the regulation of brain development and postnatal survival, cellular migration and adhesion, as well as phagocytosis, endocytosis, and exocytosis. The involvement of MARCKS phosphorylation in secretory function has been reported in Ca2+-mediated exocytosis. In rat parotid acinar cells, the activation of β-adrenergic receptors provokes exocytotic amylase release via accumulation of intracellular cAMP levels. Here, we studied the involvement of MARCKS phosphorylation in the cAMP-dependent amylase release in rat parotid acinar cells. MARCKS protein was detected in rat parotid acinar cells by Western blotting. The β-adrenergic agonist isoproterenol (IPR) induced MARCKS phosphorylation in a time-dependent manner. Translocation of a part of phosphorylated MARCKS from the membrane to the cytosol and enhancement of MARCKS phosphorylation at the apical membrane site induced by IPR were observed by immunohistochemistry. H89, a cAMP-dependent protein kinase (PKA) inhibitor, inhibited the IPR-induced MARCKS phosphorylation. The PKCδ inhibitor rottlerin inhibited the IPR-induced MARCKS phosphorylation and amylase release. IPR activated PKCδ, and the effects of IPR were inhibited by the PKA inhibitors. A MARCKS-related peptide partially inhibited the IPR-induced amylase release. These findings suggest that MARCKS phosphorylation via the activation of PKCδ, which is downstream of PKA activation, is involved in the cAMP-dependent amylase release in parotid acinar cells.

scholarly journals Protein kinase A modulates Ca2+- and protein kinase C-dependent amylase release in permeabilized rat pancreatic acini

1992 ◽  
Vol 287 (2) ◽  
pp. 403-406 ◽  
Author(s):  
A J O'Sullivan ◽  
J D Jamieson
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Response Curve ◽  
Amylase Release ◽  
Pancreatic Acini ◽  
Kinase C ◽  
Pkc Activation ◽  
Kinase A

The role of protein kinase A (PKA) in the release of amylase from permeabilized pancreatic acini was investigated. Addition of cyclic AMP (cAMP) to permeabilized acini resulted in a potentiation of Ca(2+)-dependent amylase release, shifting the Ca2+ dose/response curve leftwards. As with protein kinase C (PKC) activation, this is due to an increase in the time of active discharge. The effect of cAMP was shown to be blocked by two inhibitors of PKA, H89 and the PKI-(5-24)-peptide. At low concentration, cAMP synergizes from phorbol 12-myristate 13-acetate (PMA), while at optimal concentrations cAMP and PMA are additive. PKA and PKC appear to work via similar, but not identical mechanisms.

The role of protein kinase C on amylase secretion from rat parotid gland

1988 ◽  
Vol 150 (3) ◽  
pp. 1309-1314 ◽  
Author(s):  
Hiromi Shimomura ◽  
Akane Terada ◽  
Yoshiaki Hashimoto ◽  
Thomas R. Soderling
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Parotid Gland ◽  
Amylase Secretion ◽  
Kinase C ◽  
Rat Parotid Gland ◽  
Rat Parotid
Sign in / Sign up

Export Citation Format

Share Document