scholarly journals Protein kinase C alpha mediates phospholipase D activation by nucleotides and phorbol ester in Madin-Darby canine kidney cells. Stimulation of phospholipase D is independent of activation of polyphosphoinositide-specific phospholipase C and phospholipase A2.

1994 ◽  
Vol 269 (14) ◽  
pp. 10511-10516
Author(s):  
M.A. Balboa ◽  
B.L. Firestein ◽  
C. Godson ◽  
K.S. Bell ◽  
P.A. Insel
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phospholipase D ◽  
Phorbol Ester ◽  
Kidney Cells ◽  
Madin Darby Canine Kidney ◽  
Kinase C ◽  
Darby Canine Kidney ◽  
Canine Kidney ◽  
Stimulation Of

scholarly journals Diacylglycerol generated during sphingomyelin synthesis is involved in protein kinase C activation and cell proliferation in Madin-Darby canine kidney cells

2003 ◽  
Vol 373 (3) ◽  
pp. 917-924 ◽  
Author(s):  
Jorge CERBÓN ◽  
Rosa del Carmen LÓPEZ-SÁNCHEZ
Keyword(s):  
Cell Proliferation ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Fold Increase ◽  
Kidney Cells ◽  
Madin Darby Canine Kidney ◽  
Kinase C ◽  
Pkc Activation ◽  
Darby Canine Kidney ◽  
Canine Kidney

We have investigated the effects of inhibiting sphingomyelin (SM) biosynthesis on cellular diacylglycerol (DAG) content and protein kinase C (PKC) activation during growth initiation in Madin–Darby canine kidney cells. We utilized β-chloroalanine (BCA) to inactivate serine C-palmitoyltransferase, the first enzyme in the sphingolipid biosynthesis pathway. This inactivation prevented growth, but did not affect viability. When the inhibitor was replaced with fresh culture medium, the cells continued their proliferation in a normal way. BCA (2 mM) inhibited [32P]Pi, [3H]palmitic acid and [methyl-3H]choline incorporation into SM, but did not influence the synthesis of other major phospholipids. SM synthesis and DAG generation were decreased by 51% and 47.6% respectively. Particulate PKC activity was not observed in cells incubated with BCA, in contrast with a 5-fold increase in control cells. BCA inhibited 75% of the [3H]thymidine incorporation, and the cells were arrested before the S phase of the cell cycle. Moreover, exogenous d-erythrosphingosine restored SM synthesis, DAG generation and cell proliferation. These data indicate that the contribution of DAG generated during SM synthesis plays an important role in PKC activation and cell proliferation.

Regulation of eicosanoid biosynthesis by phorbol ester in Madin Darby canine kidney cells

1990 ◽  
Vol 259 (4) ◽  
pp. F698-F703 ◽  
Author(s):  
D. W. Coyne ◽  
M. Mordhorst ◽  
A. R. Morrison
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Mdck Cells ◽  
Pge2 Production ◽  
Madin Darby Canine Kidney ◽  
Kinase C ◽  
Protein Kinase C Inhibitor ◽  
Peptide Agonist ◽  
Darby Canine Kidney ◽  
Canine Kidney

We assessed the effects of the peptide agonist, bradykinin (BK), and phorbol myristate acetate (PMA) on prostaglandin E2 (PGE2) production, cyclooxygenase (COX) activity and mass, and arachidonic acid (AA) release in Madin Darby canine kidney (MDCK) cells. PMA stimulated PGE2 production by increasing both AA release and the activity of COX. Using [35S]methionine labeling and immunoprecipitation, we demonstrated that the increased COX activity is due to new COX synthesis. Actinomycin D and cycloheximide blocked the PMA-stimulated COX activity but not AA release. Both PMA-stimulated AA release and COX activity were reduced by the protein kinase C inhibitor staurosporine (STP). Glucocorticoids failed to alter PMA- or BK-stimulated PGE2 production was reduced by STP, indicating BK acts in part through protein kinase C activation. BK increased PGE2 production in PMA-treated cells, suggesting a protein kinase C-independent mechanism of action as well. BK did not stimulate any change in COX activity. We conclude that in MDCK cells PMA, but not BK, can stimulate both AA release and COX synthesis. Stimulation of COX synthesis requires either prolonged activation of protein kinase C and/or an additional nonprotein kinase C-mediated effect of PMA.

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