scholarly journals Oxidative Stress Causes Renal Dopamine D1 Receptor Dysfunction and Hypertension via Mechanisms That Involve Nuclear Factor-κB and Protein Kinase C

2007 ◽  
Vol 18 (5) ◽  
pp. 1446-1457 ◽  
Author(s):  
Anees Ahmad Banday ◽  
Fatima Rizwan Fazili ◽  
Mustafa F. Lokhandwala
Keyword(s):  
Oxidative Stress ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Nuclear Factor Κb ◽  
Dopamine D1 Receptor ◽  
D1 Receptor ◽  
Nuclear Factor ◽  
Kinase C ◽  
Renal Dopamine

scholarly journals Activation of Nuclear Factor κB (NF-κB) in Prostate Cancer Is Mediated by Protein Kinase C ϵ (PKCϵ)

2012 ◽  
Vol 287 (44) ◽  
pp. 37570-37582 ◽  
Author(s):  
Rachana Garg ◽  
Jorge Blando ◽  
Carlos J. Perez ◽  
HongBin Wang ◽  
Fernando J. Benavides ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Nuclear Factor Κb ◽  
Nuclear Factor ◽  
Kinase C

Role of Nuclear Factor-κB and Protein Kinase C Signaling in the Expression of the Kinin B1 Receptor in Human Vascular Smooth Muscle Cells

2006 ◽  
Vol 71 (3) ◽  
pp. 949-956 ◽  
Author(s):  
Marie Eve Moreau ◽  
Marie-Thérèse Bawolak ◽  
Guillaume Morissette ◽  
Albert Adam ◽  
François Marceau
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Vascular Smooth Muscle Cells ◽  
Nuclear Factor Κb ◽  
Nuclear Factor ◽  
B1 Receptor ◽  
Kinase C ◽  
Kinin B1 Receptor

scholarly journals Role of endocytosis in the transactivation of nuclear factor-κB by oxidized low-density lipoprotein

2000 ◽  
Vol 350 (3) ◽  
pp. 829-837 ◽  
Author(s):  
Chang-Yeop HAN ◽  
Soo-Young PARK ◽  
Youngmi Kim PAK
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Nuclear Factor Κb ◽  
Low Density ◽  
Nuclear Factor ◽  
Oxidized Low Density Lipoprotein ◽  
Ppar Γ ◽  
Kinase C

Oxidized low-density lipoprotein (oxLDL) has been shown to modulate transactivation by the peroxisome proliferator-activated receptor (PPAR)-γ and by nuclear factor-κB (NF-κB). In the present study, the oxLDL signalling pathways involved in NF-κB transactivation were investigated by utilizing a reporter construct driven by three upstream NF-κB binding sites, and various pharmacological inhibitors. OxLDL and its constituent lysophophatidylcholine (lysoPC) induced a rapid and transient increase in intracellular calcium and stimulated NF-κB transactivation in resting RAW264.7 macrophage cells in an oxidation-dependent manner. NF-κB activation by oxLDL or lysoPC was inhibited by inhibitors of protein kinase C or by a chelator of intracellular calcium. Tyrosine kinase or phosphatidylinositol 3-kinase inhibitors did not block NF-κB transactivation. Furthermore, oxLDL-induced NF-κB activity was abolished by PPAR-γ ligands. When the endocytosis of oxLDL was blocked by cytochalasin B, NF-κB transactivation by oxLDL was synergistically increased, while PPAR transactivation was blocked. These results suggest that oxLDL activates NF-κB in resting macrophages via protein kinase C- and/or calcium-dependent pathways, and that this does not involve the endocytic processing of oxLDL. The endocytosis-dependent activation of PPAR-γ by oxLDL may function as a route of inactivation of the oxLDL-induced NF-κB signal.

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