scholarly journals Mitochondrial calcium sequestration and protein kinase C cooperate in the regulation of cortical F-actin disassembly and secretion in bovine chromaffin cells

2004 ◽  
Vol 560 (1) ◽  
pp. 63-76 ◽  
Author(s):  
I. Cuchillo-Ibáñez ◽  
T. Lejen ◽  
A. Albillos ◽  
S. D. Rosé ◽  
R. Olivares ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Chromaffin Cells ◽  
Mitochondrial Calcium ◽  
Calcium Sequestration ◽  
Kinase C ◽  
Bovine Chromaffin Cells

scholarly journals Effect of secretagogues on chromogranin A synthesis in bovine cultured chromaffin cells. Possible regulation by protein kinase C

1989 ◽  
Vol 260 (3) ◽  
pp. 915-922 ◽  
Author(s):  
J P Simon ◽  
M F Bader ◽  
D Aunis
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Chromogranin A ◽  
Chromaffin Cells ◽  
Cell Types ◽  
Term Treatment ◽  
Synthesis Rate ◽  
Kinase C ◽  
Long Term Treatment ◽  
Bovine Chromaffin Cells

Chromogranin A is a major component of storage granules in many different secretory cell types. After [35S]methionine labelling of proteins from cultured bovine chromaffin cells, chromogranin A was immunoprecipitated with specific antibodies, and the radioactivity incorporated into chromogranin A was determined and used as an index of its synthesis rate. Depolarization of cells with nicotine or high K+ evoked a Ca2+-dependent increase in chromogranin A synthesis, whereas muscarine, which does not evoke significant Ca2+ influx from bovine chromaffin cells, had no effect on chromogranin A synthesis. Forskolin, an activator of adenylate cyclase, affected neither the basal nor the nicotine-stimulated rate of chromogranin A synthesis. In contrast, 12-O-tetradecanoylphorbol 13-acetate (TPA), an activator of protein kinase C, significantly enhanced the incorporation of radioactivity into chromogranin A. Sphingosine, an inhibitor of protein kinase C, abolished both nicotine-stimulated and TPA-induced chromogranin A synthesis. In addition, long-term treatment of chromaffin cells with TPA decreased protein kinase C activity and inhibited the nicotine-stimulated chromogranin A synthesis. These results suggest that protein kinase C may play an important role in the control of chromogranin A synthesis.

Intracellular mechanism of Pb(2+)-induced norepinephrine release from bovine chromaffin cells

1993 ◽  
Vol 265 (6) ◽  
pp. C1630-C1636 ◽  
Author(s):  
J. L. Tomsig ◽  
J. B. Suszkiw
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Chromaffin Cells ◽  
Kinase C ◽  
Dopamine Beta Hydroxylase ◽  
Intracellular Mechanism ◽  
Protein Kinase C Inhibitor ◽  
Bovine Chromaffin Cells ◽  
Free Metal ◽  
Analogous Mechanism

The intracellular mechanism of Pb(2+)-induced release of norepinephrine (NE) was investigated in comparison with Ca2+ in bovine chromaffin cells permeabilized with staphylococcal alpha-toxin. Pb2+ activated NE release at considerably lower concentrations [concentration of free metal giving half maximal metal-dependent release (K0.5) 4.6 nM] than Ca2+ (K0.5 2.4 microM). The release of NE was associated with the release of dopamine-beta-hydroxylase but not lactate dehydrogenase. The maximal secretory responses produced by Pb2+ and Ca2+ were similar and nonadditive. Pb(2+)- and Ca(2+)-dependent releases showed a similar requirement for MgATP and were equally enhanced by protein kinase C activator 12-O-tetradecanoylphorbol 13-acetate (TPA) but not by kinase A activator 8-bromoadenosine 3',5'-cyclic monophosphate free base. The protein kinase C inhibitor staurosporine blocked the TPA-stimulated component of secretion but had no effect on the NE release in the absence of TPA. Calmidazolium, an inhibitor of calmodulin, inhibited the secretion evoked by both metals to similar extent. Agents interacting with microtubules (colchicine and vinblastine) or microfilaments (cytochalasin B and phalloidin) had no effect on secretion induced by either metal cation. These observations indicate that both Pb2+ and Ca2+ act at a common site and activate the exocytotic release of NE by an analogous mechanism.

Munc18-1 phosphorylation by protein kinase C potentiates vesicle pool replenishment in bovine chromaffin cells

Neuroscience ◽  
2006 ◽  
Vol 143 (2) ◽  
pp. 487-500 ◽  
Author(s):  
U. Nili ◽  
H. de Wit ◽  
A. Gulyas-Kovacs ◽  
R.F. Toonen ◽  
J.B. Sørensen ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Chromaffin Cells ◽  
Kinase C ◽  
Bovine Chromaffin Cells ◽  
Vesicle Pool

The role of protein kinase C in nicotinic responses of bovine chromaffin cells

1996 ◽  
Vol 311 (1) ◽  
pp. 87-94 ◽  
Author(s):  
Kylie Loneragan ◽  
Tat B. Cheah ◽  
Stephen J. Bunn ◽  
Philip D. Marley
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Chromaffin Cells ◽  
Kinase C ◽  
Bovine Chromaffin Cells

scholarly journals Down-regulation of Na channel α-subunit mRNA by protein kinase C e in adrenal chromaffin cells

1997 ◽  
Vol 73 ◽  
pp. 157
Author(s):  
Toshihiko Yanagita ◽  
Hideyuki Kobayashi ◽  
Keizou Masumoto ◽  
Ryuichi Yamamoto ◽  
Tomoaki Yuhi ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Chromaffin Cells ◽  
Na Channel ◽  
Adrenal Chromaffin Cells ◽  
Down Regulation ◽  
Α Subunit ◽  
Subunit Mrna ◽  
Kinase C ◽  
Adrenal Chromaffin
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