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The initiation of saliva formation by parotid acinar cells,
which comprise the majority of cells in this salivary gland, is
initiated by the release of neurotransmitters (acetylcholine, substance
P) from parasympathetic nerves. In response to substance P and the
muscarinic agonist carbachol, two ligands that activate phospholipase
C-linked receptors, which stimulate fluid secretion, PKC
was
phosphorylated on tyrosine residues. The maximal agonist-dependent
tyrosine phosphorylation occurred within seconds of the addition of
either agonist and then returned rapidly to a smaller increased level.
Phorbol ester also caused a rapid increase in tyrosine phosphorylation,
which reached a maximal level 5 min after the addition of phorbol
12-myristate 13-acetate. The increase in tyrosine phosphorylation of
PKC
was blocked by tyrosine kinase inhibitors genistein and
staurosporine. Ionophore-mediated elevation of
[Ca
]
or activation of
the
-adrenergic receptor, epidermal growth factor receptor, or
insulin receptor did not promote the tyrosine phosphorylation of
PKC. These results indicate that tyrosine phosphorylation plays a
role in early signal transduction events promoted by the activation of
muscarinic and substance P receptors and suggests that the tyrosine
phosphorylation of PKC
has a role in the activation of fluid
secretion by neurotransmitters binding to phospholipase C-linked
receptors.
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