Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:2.7.11.13 (
protein kinase C
)
49,245
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
A
putative protein tyrosine phosphatase
inhibitor, phenylarsine oxide (PAO), potentiated phospholipase D (PLD) activity concentration-dependently in [3H] oleic acid-labeled rat basophilic leukemia (RBL-2H3) cells without significant increase in phosphatidylinositol-specific phospholipase C (PI-PLC) activity. Although PAO induced tyrosine phosphorylation of several proteins, both PAO-induced PLD activation and tyrosine phosphorylation were not affected by a protein tyrosine kinase inhibitor, genistein. Another tyrosine kinase inhibitor, herbimycin A, prevented the PAO-induced PLD stimulation but had no effect on protein tyrosine phosphorylation. However, depletion of
protein kinase C
(
PKC
) greatly reduced PAO-stimulated PLD activity. These results indicate that
PKC
but not tyrosine kinase may be involved in PAO-mediated PLD activation.
...
PMID:Potent activation of phospholipase D by phenylarsine oxide in rat basophilic leukemia (RBL-2H3) cells. 813 25
The intracellular localization of
protein kinase C
(
PKC
) is important for the regulation of its biological activity. Recently, it was reported that, whereas phorbol esters such as PMA induce prolonged translocation of
PKC
to the plasma membrane, with physiological stimuli, the translocation of
PKC
is transient and followed by rapid return to the cytoplasm. In addition, this membrane dissociation of
PKC
was shown to require both the kinase activity of
PKC
and the phosphorylation of its carboxyl terminus autophosphorylation sites. However, the detailed molecular mechanism of
PKC
reverse translocation remains obscure. We demonstrated that in porcine polymorphonuclear leucocytes (PMNs), phenylarsine oxide (PAO), a
putative protein tyrosine phosphatase
(PTPase) inhibitor, induced reverse translocation of PMA-stimulated PKCbetaII. Hydrogen peroxide (H(2)O(2)) in combination with vanadate, both of which are PTPase inhibitors, also induced reverse translocation of PKCbetaII. H(2)O(2) or vanadate alone had little effect on PMA-induced PKCbetaII translocation. Furthermore, genistein and ethanol, which are inhibitors of tyrosine kinase and phospholipase D, respectively, prevented the PKCbetaII reverse translocation induced by the PTPase inhibitors. These results indicate, for the first time, that the tyrosine phosphorylation/phospholipase D pathway may be involved in the process of membrane dissociation of
PKC
.
...
PMID:Phenylarsine oxide and H2O2 plus vanadate induce reverse translocation of phorbol-ester-activated PKCbetaII. 1280 32
