Cadmium-induced calcium release and prostaglandin E 2 production in neonatal mouse calvaria are dependent on cox-2 induction and protein kinase C activation

1999 ◽  
Vol 73 (4-5) ◽  
pp. 223-228 ◽  
Author(s):  
Anna Romare ◽  
C. E. Lundholm
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Calcium Release ◽  
Neonatal Mouse ◽  
Prostaglandin E ◽  
Kinase C ◽  
Mouse Calvaria ◽  
Neonatal Mouse Calvaria ◽  
Cox 2 ◽  
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

scholarly journals Thapsigargin potentiates histamine-stimulated HCl secretion in gastric parietal cells but does not mimic cholinergic responses.

1991 ◽  
Vol 2 (1) ◽  
pp. 27-39 ◽  
Author(s):  
C S Chew ◽  
A C Petropoulos
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Intracellular Calcium ◽  
Parietal Cell ◽  
Calcium Release ◽  
Parietal Cells ◽  
Kinase C ◽  
Hcl Secretion ◽  
Protein Kinase C Activation ◽  
Cholinergic Response

The role of calcium in control of HCl secretion by the gastric parietal cell was examined using a recently available intracellular calcium-releasing agent, thapsigargin, which has been shown, in some cell types, to induce sustained elevation of intracellular calcium ([Ca2+]i), an action that appears to be independent of inositol lipid breakdown and protein kinase C activation and to be mediated, at least partially, by selective inhibition of endoplasmic reticulum Ca2(+)-ATPase. Using the calcium-sensitive fluorescent probe, fura-2, in combination with digitized video image analysis of single cells as well as standard fluorimetric techniques, we found that thapsigargin induced sustained elevation of [Ca2+]i in single parietal cells and in parietal cells populations. Chelation of medium calcium led to a transient rise and fall in [Ca2+]i, indicating that the sustained elevation in [Ca2+]i in response to thapsigargin was due to both intracellular calcium release and influx. Although thapsigargin appeared to affect the same calcium pool(s) regulated by the cholinergic agonist, carbachol, and the pattern of thapsigargin-induced increases in [Ca2+]i were similar to the plateau phase of the cholinergic response, thapsigargin did not induce acid secretory responses of the same magnitude as those initiated by carbachol (28 vs 600% of basal). The protein kinase C activator, 12-O-tetradecanoyl phorbol-13-acetate (TPA) potentiated the secretory response to thapsigargin but this combined response also did not attain the same magnitude as the maximal cholinergic response. In the presence but not the absence of medium calcium, thapsigargin potentiated acid secretory responses to histamine, which elevate both cyclic AMP (cAMP) and [Ca2+]i in parietal cells, as well as forskolin and cAMP analogues but had no effect on submaximal and an inhibitory effect on maximal cholinergic stimulation. Furthermore, thapsigargin did not fully mimic potentiating interactions between histamine and carbachol, either in magnitude or in the pattern of temporal response. Assuming that the action of thapsigargin is specific for intracellular calcium release mechanisms, these data suggest that 1) sustained influx of calcium is necessary but not sufficient for cholinergic activation of parietal cell HCl secretion and for potentiating interactions between cAMP-dependent agonists and carbachol; 2) mechanisms in addition to elevated [Ca2+]i and protein kinase C activation may be involved in cholinergic regulation; and 3) increases in [Ca2+]i in response to histamine are not directly involved in the mechanism of histamine-stimulated secretion.

scholarly journals Novel augmentation by bufalin of protein kinase C-induced cyclooxygenase-2 and IL-8 production in human breast cancer cells

2016 ◽  
Vol 23 (1) ◽  
pp. 54-66 ◽  
Author(s):  
Hsiao-Ting Chen ◽  
David Sun ◽  
Yen-Chun Peng ◽  
Pu-Hong Kao ◽  
Yuh-Lin Wu
Keyword(s):  
Breast Cancer ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Cyclooxygenase 2 ◽  
Prostaglandin E ◽  
Mrna Levels ◽  
Kinase C ◽  
Cox 2

Cyclooxygenase-2 (COX-2) and IL-8 are two inflammatory mediators induced by protein kinase C (PKC) via various stimuli. Both contribute significantly to cancer progression. Bufalin, a major active component of the traditional Chinese medicine Chan Su, is known to induce apoptosis in various cancer cells. This study clarifies the role and mechanism of bufalin action during PKC regulation of COX-2/IL-8 expression and investigates the associated impact on breast cancer. Using MB-231 breast cancer cells, bufalin augments PKC induction of COX-2/IL-8 at both the protein and mRNA levels, and the production of prostaglandin E2 (PGE2) and IL-8. The MAPK and NF-κB pathways are involved in both the PKC-mediated and bufalin-promoted PKC regulation of COX-2/IL-8 production. Bufalin increases PKC-induced MAPKs phosphorylation and NF-κB nuclear translocation. PGE2 stimulates the proliferation/migration of breast cancer cells. Furthermore, PKC-induced matrix metalloproteinase 3 expression is enhanced by bufalin. Bufalin significantly enhances breast cancer xenograft growth, which is accompanied by an elevation in COX-2/IL-8 expression. In conclusion, bufalin seems to promote the inflammatory response in vitro and in vivo, and this occurs, at least in part, by targeting the MAPK and NF-κB pathways, which then enhances the growth of breast cancer cells.

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 Protein Kinase C Activation Contributes to Microvascular Barrier Dysfunction in the Heart at Early Stages of Diabetes

2000 ◽  
Vol 87 (5) ◽  
pp. 412-417 ◽  
Author(s):  
Sarah Y. Yuan ◽  
Elena E. Ustinova ◽  
Mack H. Wu ◽  
John H. Tinsley ◽  
Wenjuan Xu ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Barrier Dysfunction ◽  
Early Stages ◽  
Kinase C ◽  
Protein Kinase C Activation
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