Stimulation of a histone H4 protein kinase in Triton X-100 lysates of rabbit peritoneal neutrophils pretreated with chemotactic factors: Lack of requirements of calcium mobilization and protein kinase C activation

1990 ◽  
Vol 44 (4) ◽  
pp. 221-228 ◽  
Author(s):  
Chi-Kuang Huang ◽  
Gary R. Laramee ◽  
Munehiro Yamazaki ◽  
Ramadan I. Sha'afi
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Calcium Mobilization ◽  
Histone H4 ◽  
Kinase C ◽  
Chemotactic Factors ◽  
Triton X ◽  
Protein Kinase C Activation ◽  
Stimulation Of

scholarly journals Calcium mobilization and protein kinase C activation are required for cholecystokinin stimulation of pancreatic cholesterol esterase secretion

1995 ◽  
Vol 306 (2) ◽  
pp. 605-608 ◽  
Author(s):  
J Brodt-Eppley ◽  
D Y Hui
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Digestive Enzyme ◽  
Calcium Mobilization ◽  
Cholesterol Esterase ◽  
Ionophore A23187 ◽  
Prolonged Incubation ◽  
Ar42j Cells ◽  
Kinase C ◽  
Stimulation Of

The bile salt-stimulated cholesterol esterase is a digestive enzyme synthesized by the acinar cells of the pancreas. Previous results have shown that cholesterol esterase biosynthesis and secretion in the AR42J pancreatoma cells could be increased 3-5-fold by intestinal hormones such as cholecystokinin (CCK). The purpose of the current study is to explore the signalling mechanism by which CCK stimulation of AR42J cells results in increased biosynthesis and secretion of the cholesterol esterase. The results showed that the CCK-induced cholesterol esterase secretion could be mimicked by addition of the Ca2+ ionophore A23187 or by transient incubation of AR42J cells with the protein kinase C activator phorbol 12-myristate 13-acetate (PMA). Cholesterol esterase stimulation by CCK, A23187 and PMA could be abolished by the calcium chelator BAPTA or by specific protein kinase C inhibitors such as chelerythrine. Additionally, prolonged incubation of AR42J cells with PMA to reduce the protein kinase C level, also reduced CCK-stimulated cholesterol esterase secretion to a level similar to that observed in control cells. Taken together, these data suggested that CCK activation of cholesterol esterase secretion may be mediated by a Ca(2+)-dependent protein kinase C pathway, requiring increases in calcium mobilization and activation of protein kinase C.

Prolactin stimulation of ornithine decarboxylase and mitogenesis in Nb2 node lymphoma cells: The role of protein kinase C and calcium mobilization

1986 ◽  
Vol 12 (1) ◽  
pp. 37-51 ◽  
Author(s):  
Arthur R. Buckley ◽  
David W. Montgomery ◽  
Ruthann Kibler ◽  
Charles W. Putnam ◽  
Charles F. Zukoski ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Ornithine Decarboxylase ◽  
Calcium Mobilization ◽  
Lymphoma Cells ◽  
Kinase C ◽  
Stimulation Of

scholarly journals Involvement of Protein Kinase C Activation in L-Leucine-Induced Stimulation of Protein Synthesis in L6 Myotubes

2003 ◽  
Vol 43 (1-3) ◽  
pp. 97-103 ◽  
Author(s):  
Kazumi Yagasaki ◽  
Naoko Morisaki ◽  
Yoshiro Kitahara ◽  
Atsuhito Miura ◽  
Ryuhei Funabiki
Keyword(s):  
Protein Synthesis ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
L6 Myotubes ◽  
Kinase C ◽  
Protein Kinase C Activation ◽  
Stimulation Of
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