scholarly journals Augmentation of c-fos mRNA expression by activators of protein kinase C in fresh, terminally differentiated resting macrophages.

1987 ◽  
Vol 7 (2) ◽  
pp. 595-599 ◽  
Author(s):  
D Radzioch ◽  
B Bottazzi ◽  
L Varesio
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Calcium Ionophore ◽  
Peritoneal Macrophages ◽  
Biologically Active ◽  
Specific Response ◽  
Tumoricidal Activity ◽  
Differentiated Cells ◽  
Kinase C ◽  
Protein Kinase C Activation

Expression of c-fos mRNA was investigated in fresh, normal peritoneal macrophages (M phi), which are terminally differentiated, nonproliferating cells. The levels of c-fos mRNA were dramatically increased by stimulation with phorbol myristate acetate (PMA), calcium ionophore, or 1-oleoyl-2-acetoyl glycerol (OAG). Induction of c-fos mRNA by all the above agents followed similar kinetics, with a peak of mRNA 30 min after stimulation. These results demonstrate that c-fos mRNA can be augmented in fresh, terminally differentiated cells. Since the stimuli increasing c-fos mRNA are direct or indirect activators of protein kinase C, our data suggest that in M phi c-fos mRNA is controlled by protein kinase C activation. PMA, calcium ionophore, and OAG were biologically active in M phi. PMA and calcium ionophore induced respiratory burst and tumoricidal activity, respectively, whereas OAG and PMA were chemotactic for M phi. Interferons beta and gamma, potent M phi activators eliciting tumoricidal activity, did not alter the levels of c-fos mRNA. These results indicate that c-fos mRNA augmentation is a stimulus-specific rather than a function-specific response connected to activation of protein kinase C.

Augmentation of c-fos mRNA expression by activators of protein kinase C in fresh, terminally differentiated resting macrophages

1987 ◽  
Vol 7 (2) ◽  
pp. 595-599
Author(s):  
D Radzioch ◽  
B Bottazzi ◽  
L Varesio
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Calcium Ionophore ◽  
Peritoneal Macrophages ◽  
Biologically Active ◽  
Specific Response ◽  
Tumoricidal Activity ◽  
Differentiated Cells ◽  
Kinase C ◽  
Protein Kinase C Activation

Expression of c-fos mRNA was investigated in fresh, normal peritoneal macrophages (M phi), which are terminally differentiated, nonproliferating cells. The levels of c-fos mRNA were dramatically increased by stimulation with phorbol myristate acetate (PMA), calcium ionophore, or 1-oleoyl-2-acetoyl glycerol (OAG). Induction of c-fos mRNA by all the above agents followed similar kinetics, with a peak of mRNA 30 min after stimulation. These results demonstrate that c-fos mRNA can be augmented in fresh, terminally differentiated cells. Since the stimuli increasing c-fos mRNA are direct or indirect activators of protein kinase C, our data suggest that in M phi c-fos mRNA is controlled by protein kinase C activation. PMA, calcium ionophore, and OAG were biologically active in M phi. PMA and calcium ionophore induced respiratory burst and tumoricidal activity, respectively, whereas OAG and PMA were chemotactic for M phi. Interferons beta and gamma, potent M phi activators eliciting tumoricidal activity, did not alter the levels of c-fos mRNA. These results indicate that c-fos mRNA augmentation is a stimulus-specific rather than a function-specific response connected to activation of protein kinase C.

Protein kinase C activation accelerates proton extrusion by vacuolar-type H+ -ATPases in murine peritoneal macrophages

FEBS Letters ◽  
1994 ◽  
Vol 350 (1) ◽  
pp. 82-86 ◽  
Author(s):  
Tommy Nordström ◽  
Sergio Grinstein ◽  
Guy F. Brisseau ◽  
Morris F. Manolson ◽  
Ori D. Rotstein
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Peritoneal Macrophages ◽  
Proton Extrusion ◽  
Kinase C ◽  
Murine Peritoneal Macrophages ◽  
Protein Kinase C Activation

ENDOTOXIC LIPID A INDUCES BINDING OF FIBRINOGEN TO HUMAN PLATELETS VIA PROTEIN KINASE C PATHWAY

1987 ◽  
Author(s):  
Sheila Timmons ◽  
Jadwiqa Grabarek ◽  
Jack Hawiqer
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Lipid A ◽  
Human Platelets ◽  
Biologically Active ◽  
Active Principle ◽  
Gram Negative ◽  
Kinase C ◽  
Induced Aggregation ◽  
Protein Kinase C Activation

Endotoxic Lipid A is the biologically active principle of lipopolysaccharide of Gram-negative bacteria, a most frequent cause of sepsis underlying Disseminated Intravascular Coagulation (DIC) and shock. We have shown that endotoxic Lipid A activates Protein Kinase C in human platelets. Phosphorylation of a 47kDa protein (P47), a marker for Protein Kinase C activation, was observed within the first minute of interaction of Lipid A with platelets. This was accompanied by gradual exposure of the receptor for 125I-labeled fibrinogen (F). Binding of 125I-F was saturable and specific. When Lipid X, a precursor of endotoxic Lipid A and its competitive inhibitor, was used, the binding of 125I-F was blocked with 50% inhibition at a 1:1 stoichiometry between Lipid X and Lipid A. At the same time, phosphorylation of P47 was prevented. Since Lipid X constitutes a "half molecule" of Lipid A, we interpret these results as indicative of competitive blocking of endotoxic Lipid A in terms of Protein Kinase C activation and exposure of platelet receptors for fibrinogen. Binding of fibrinogen is necessary for platelet aggregation and endotoxic Lipid A-induced aggregation was also blocked by Lipid X. Endotoxic Lipid A-induced exposure of fibrinogen receptors via the Protein Kinase C pathway can contribute to involvement of platelets in microcirculatory thrombosis observed in patients with DIC and Gram-negative sepsis

Swainsonine Modulation of Protein Kinase C Activity in Murine Peritoneal Macrophages

1990 ◽  
Vol 2 (10) ◽  
pp. 333-338 ◽  
Author(s):  
Pascal Breton ◽  
Amha Asseffa ◽  
Krzysztof Grzegorzewski ◽  
Steven K. Akiyama ◽  
Sandra L. White ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Peritoneal Macrophages ◽  
Kinase C ◽  
Protein Kinase C Activity ◽  
Murine Peritoneal Macrophages

Comparison of the modes of action of Ca2+ ionophore A23187 and thrombin in protein kinase C activation in human platelets

FEBS Letters ◽  
1985 ◽  
Vol 192 (1) ◽  
pp. 4-8 ◽  
Author(s):  
Kimihiko Sano ◽  
Hajime Nakamura ◽  
Tamotsu Matsuo ◽  
Yasuhiro Kawahara ◽  
Hisashi Fukuzaki ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Human Platelets ◽  
Ionophore A23187 ◽  
Modes Of Action ◽  
Kinase C ◽  
Protein Kinase C Activation

scholarly journals Intracellular Calcium Release and Protein Kinase C Activation Stimulate Sonic Hedgehog Gene Expression During Gastric Acid Secretion

2010 ◽  
Vol 139 (6) ◽  
pp. 2061-2071.e2 ◽  
Author(s):  
Mohamad El–Zaatari ◽  
Yana Zavros ◽  
Art Tessier ◽  
Meghna Waghray ◽  
Steve Lentz ◽  
...  
Keyword(s):  
Gene Expression ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Acid Secretion ◽  
Gastric Acid Secretion ◽  
Sonic Hedgehog ◽  
Calcium Release ◽  
Kinase C ◽  
Sonic Hedgehog Gene ◽  
Protein Kinase C Activation
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