scholarly journals A Persistent Activity-Dependent Facilitation in Chromaffin Cells Is Caused by Ca2+Activation of Protein Kinase C

1999 ◽  
Vol 19 (2) ◽  
pp. 589-598 ◽  
Author(s):  
Corey Smith
1997 ◽  
Vol 73 ◽  
pp. 157
Author(s):  
Toshihiko Yanagita ◽  
Hideyuki Kobayashi ◽  
Keizou Masumoto ◽  
Ryuichi Yamamoto ◽  
Tomoaki Yuhi ◽  
...  

1989 ◽  
Vol 260 (3) ◽  
pp. 915-922 ◽  
Author(s):  
J P Simon ◽  
M F Bader ◽  
D Aunis

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.


1997 ◽  
Vol 73 ◽  
pp. 156
Author(s):  
Ryuichi Yamamoto ◽  
Hideyuki Kobayashi ◽  
Toshihiko Yanagita ◽  
Keizo Masumoto ◽  
Hiroki Yokoo ◽  
...  

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