Inhibition of calcium-activated, phospholipid-dependent protein kinase (protein kinase C) activity in sphingolipidoses

1991 ◽  
Vol 14 (3) ◽  
pp. 393-396 ◽  
Author(s):  
A. Boneh
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Dependent Protein Kinase ◽  
Kinase C ◽  
Protein Kinase C Activity ◽  
Dependent Protein

scholarly journals Involvement of calcium-sensitive phospholipid-dependent protein kinase in control of acid secretion by isolated rat parietal cells

1985 ◽  
Vol 232 (2) ◽  
pp. 609-611 ◽  
Author(s):  
N G Anderson ◽  
P J Hanson
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Acid Secretion ◽  
Phorbol Esters ◽  
Inhibitory Effect ◽  
Dependent Protein Kinase ◽  
Kinase C ◽  
Protein Kinase C Activity ◽  
Dependent Protein ◽  
Isolated Rat

The relative potency with which phorbol esters inhibited histamine-stimulated aminopyrine accumulation (an index of acid secretion) paralleled that which has been established for the activation of purified protein kinase C. The inhibitory effect of 1-oleoyl-2-acetylglycerol on aminopyrine accumulation stimulated by various secretagogues was similar to that of 12-O-tetradecanoylphorbol 13-acetate. Protein kinase C activity was present in a parietal-cell-enriched fraction. In conclusion, protein kinase C could be involved in mechanisms regulating gastric acid secretion.

Calcium-dependent Protein Kinase Reactions Associated with Parotid Gland Secretory Granule Membranes

1987 ◽  
Vol 66 (2) ◽  
pp. 557-563 ◽  
Author(s):  
F. Dowd ◽  
E.L. Watson ◽  
Y.-S. Lau ◽  
J. Justin ◽  
J. Pasieniuk ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Secretory Granule ◽  
Dependent Protein Kinase ◽  
Calcium Dependent ◽  
Kinase C ◽  
Protein Kinase C Activity ◽  
Granule Membrane ◽  
Dependent Protein ◽  
Calcium Dependent Protein Kinase

Rat parotid secretory granule membranes were examined for the presence of calcium-dependent protein kinase activities and kinase substrates. Protein kinase C (C-kinase), which is stimulated by certain phospholipids, was present in the membranes, as indicated by its ability to catalyze the phosphorylation of histone. Two substrates for protein kinase C were seen in the granule membranes. The cytosolic fraction from the cell contained kinase activity, which was stimulated by phosphatidylserine and which caused the phosphorylation of two granule membrane polypeptides. In addition, when both granule membranes and cytosol were incubated together, phosphorylation of the cytosolic substrates was inhibited, indicating that the granule membrane substrates were phosphorylated preferentially. The results indicate that the granule membranes may react with cytosolic protein kinase C activity in a way which would direct an intracellular calcium and diacylglycerol signal toward the granule membrane. Since these signals occur during stimulation by various agonists, the mechanism may contribute to secretion.

scholarly journals Assay of protein kinase C with an N-bromosuccinimide-cleavage fragment of histone H1

1985 ◽  
Vol 231 (2) ◽  
pp. 489-492 ◽  
Author(s):  
B Glynn ◽  
J Colliton ◽  
J McDermott ◽  
L A Witters
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Peptide Substrate ◽  
Reverse Phase ◽  
Histone Fraction ◽  
Dependent Protein Kinase ◽  
Tissue Extracts ◽  
Kinase C ◽  
Protein Kinase C Activity ◽  
Dependent Protein

N-Bromosuccinimide cleavage of a lysine-rich histone fraction (histone III-S) yields a peptide substrate, purified by reverse-phase h.p.l.c., for the Ca2+ + phospholipid-dependent protein kinase (protein kinase C). This substrate displays no reactivity with the cyclic AMP-dependent protein kinase, and may prove useful for the detection of protein kinase C activity in crude tissue extracts.

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