Legionella pneumophila inhibits superoxide generation in human monocytes via the down-modulation of α and β protein kinase C isotypes

1994 ◽  
Vol 55 (3) ◽  
pp. 310-312 ◽  
Author(s):  
T. Jacob ◽  
J. C. Escallier ◽  
M. V. Sanguedolce ◽  
C. Chicheportiche ◽  
P. Bongrand ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Legionella Pneumophila ◽  
Human Monocytes ◽  
Superoxide Generation ◽  
Kinase C ◽  
Β Protein

Endotoxin-Induced Tissue Factor in Human Monocytes is Dependent upon Protein Kinase C Activation

1993 ◽  
Vol 70 (05) ◽  
pp. 800-806 ◽  
Author(s):  
C Ternisien ◽  
M Ramani ◽  
V Ollivier ◽  
F Khechai ◽  
T Vu ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Tissue Factor ◽  
Factor Ix ◽  
Transcriptional Level ◽  
Mrna Levels ◽  
Dependent Manner ◽  
Human Monocytes ◽  
Kinase C ◽  
Pkc Activation

SummaryTissue factor (TF) is a transmembrane receptor which, in association with factors VII and Vila, activates factor IX and X, thereby activating the coagulation protease cascades. In response to bacterial lipopolysaccharide (LPS) monocytes transcribe, synthesize and express TF on their surface. We investigated whether LPS-induced TF in human monocytes is mediated by protein kinase C (PKC) activation. The PKC agonists phorbol 12- myristate 13-acetate (PMA) and phorbol 12, 13 dibutyrate (PdBu) were both potent inducers of TF in human monocytes, whereas 4 alpha-12, 13 didecanoate (4 a-Pdd) had no such effect. Both LPS- and PMA-induced TF activity were inhibited, in a concentration dependent manner, by three different PKC inhibitors: H7, staurosporine and calphostin C. TF antigen determination confirmed that LPS-induced cell-surface TF protein levels decreased in parallel to TF functional activity under staurosporine treatment. Moreover, Northern blot analysis of total RNA from LPS- or PMA-stimulated monocytes showed a concentration-dependent decrease in TF mRNA levels in response to H7 and staurosporine. The decay rate of LPS-induced TF mRNA evaluated after the arrest of transcription by actinomycin D was not affected by the addition of staurosporine, suggesting that its inhibitory effect occurred at a transcriptional level. We conclude that LPS-induced production of TF and its mRNA by human monocytes are dependent on PKC activation.

scholarly journals Legionella pneumophila heat-shock protein-induced increase of interleukin-1beta mRNA involves protein kinase C signalling in macrophages

Immunology ◽  
1996 ◽  
Vol 89 (2) ◽  
pp. 281-288 ◽  
Author(s):  
C. RETZLAFF ◽  
Y. YAMAMOTO ◽  
S. OKUBO ◽  
P. S. HOFFMAN ◽  
H. FRIEDMAN ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Heat Shock ◽  
Protein Kinase ◽  
Heat Shock Protein ◽  
Legionella Pneumophila ◽  
Kinase C ◽  
Interleukin 1Beta

scholarly journals Downregulation of c-fms gene expression in human monocytes treated with phorbol esters and colony-stimulating factor 1

Blood ◽  
1989 ◽  
Vol 74 (1) ◽  
pp. 123-129 ◽  
Author(s):  
E Sariban ◽  
K Imamura ◽  
M Sherman ◽  
V Rothwell ◽  
P Pantazis ◽  
...  
Keyword(s):  
Gene Expression ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Phorbol Esters ◽  
Constitutive Expression ◽  
Human Monocytes ◽  
Colony Stimulating Factor ◽  
Protein Levels ◽  
Kinase C ◽  
Stimulating Factor

Abstract The colony-stimulating factor-1 (CSF-1) regulates survival, growth, and differentiation of monocytes by binding to a single class of high- affinity receptors. The CSF-1 receptor is identical to the product of the c-fms protooncogene. The present studies monitored the effects of TPA and CSF-1 on c-fms gene expression in human monocytes. The results demonstrate that TPA downmodulates the constitutive expression of c-fms mRNA to low but detectable levels. Treatment of human monocytes with TPA was similarly associated with decreases in levels of the 138- and 125-Kd c-fms-encoded proteins. However, the kinetics of c-fms protein downmodulation indicated independent effects of TPA on c-fms expression at the RNA and protein levels. Furthermore, c-fms protein levels subsequently recovered despite persistently low levels of c-fms mRNA. Although previous studies demonstrated that c-fms protein is down- regulated in the presence of CSF-1, the present results indicate that CSF-1 also downregulates levels of c-fms mRNA. Moreover, the results indicate that CSF-1 increases protein kinase C activity in the membrane fraction. Together, these findings suggest that c-fms gene expression is differentially regulated at both the RNA and protein levels after activation of protein kinase C in human monocytes treated with TPA and CSF-1.

MAC-1 mediates adherence of human monocytes to endothelium via a protein kinase C dependent mechanism

1990 ◽  
Vol 1052 (1) ◽  
pp. 166-172 ◽  
Author(s):  
Ann-Marie Gladwin ◽  
David G. Hassall ◽  
John F. Martin ◽  
Robert F.G. Booth
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Human Monocytes ◽  
Kinase C ◽  
Dependent Mechanism

Nocardia fractions, NLD and NWSM, induce tumor necrosis factor-α secretion in human monocytes: Role of protein kinase C

1993 ◽  
Vol 23 (7) ◽  
pp. 1582-1587 ◽  
Author(s):  
Jean Louis Mege ◽  
Thiery Jacob ◽  
Pierre Bongrand ◽  
Christian Capo ◽  
Evguenine B. Myssiakine ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Human Monocytes ◽  
Kinase C ◽  
Factor Α ◽  
Necrosis Factor

scholarly journals Role of Protein Kinase C Isoforms in the Regulation of Interleukin-13-induced 15-Lipoxygenase Gene Expression in Human Monocytes

2004 ◽  
Vol 279 (16) ◽  
pp. 15954-15960 ◽  
Author(s):  
Bo Xu ◽  
Ashish Bhattacharjee ◽  
Biswajit Roy ◽  
Gerald M. Feldman ◽  
Martha K. Cathcart
Keyword(s):  
Gene Expression ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Human Monocytes ◽  
Interleukin 13 ◽  
Kinase C ◽  
Lipoxygenase Gene ◽  
Protein Kinase C Isoforms
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