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tyrosine phosphorylation and activity in
salivary and PC-12 cells by Src kinases
Division of Signal Transduction, Department of Medicine, Beth Israel Deaconess Medical Center, Harvard Institutes of Medicine, Boston, Massachusetts 02215
Protein kinase C (PKC) 
becomes tyrosine phosphorylated in rat parotid acinar cells exposed to
muscarinic and substance P receptor agonists, which initiate fluid
secretion in this salivary cell. Here we examine the signaling
components of PKC tyrosine phosphorylation and effects of
phosphorylation on PKC activity. Carbachol- and substance P-promoted
increases in PKC tyrosine phosphorylation were blocked by inhibiting
phospholipase C (PLC) but not by blocking intracellular
Ca2+ concentration elevation, suggesting that
diacylglycerol, rather than D-myo-inositol
1,4,5-trisphosphate production, positively modulated this
phosphorylation. Stimuli-dependent increases in PKC activity in
parotid and PC-12 cells were blocked in vivo by inhibitors of Src
tyrosine kinases. Dephosphorylation of tyrosine residues by PTP1B, a
protein tyrosine phosphatase, reduced the enhanced PKC activity.
Lipid cofactors modified the tyrosine phosphorylation-dependent PKC
activation. Two PKC regulatory sites (Thr-505 and Ser-662) were
constitutively phosphorylated in unstimulated parotid cells, and these
phosphorylations were not altered by stimuli that increased PKC
tyrosine phosphorylation. These results demonstrate that PKC
activity is positively modulated by tyrosine phosphorylation in parotid
and PC-12 cells and suggest that PLC-dependent effects of secretagogues
on salivary cells involve Src-related kinases.
serine/threonine phosphorylation; parotid acinar; protein kinase C
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