scholarly journals Protein kinase C activity is required for lipid oxidation of low density lipoprotein by activated human monocytes

1994 ◽  
Vol 269 (26) ◽  
pp. 17508-17515
Author(s):  
Q. Li ◽  
M.K. Cathcart
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Lipid Oxidation ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Low Density ◽  
Human Monocytes ◽  
Kinase C ◽  
Protein Kinase C Activity

3.P.171 The activation of protein kinase C is involved in oxidized low density lipoprotein-induced macrophage growth

1997 ◽  
Vol 134 (1-2) ◽  
pp. 234
Author(s):  
Takeshi Matsumura ◽  
Shozo Kobori ◽  
Masakazu Sakai ◽  
Yoshichika Anami ◽  
Takeshi Biwa ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Low Density ◽  
Oxidized Low Density Lipoprotein ◽  
Kinase C

Oxidized low density lipoprotein-induced LFA-1-dependent adhesion and transendothelial migration of monocytes via the protein kinase C pathway

2002 ◽  
Vol 160 (2) ◽  
pp. 281-288 ◽  
Author(s):  
Shinichiro Mine ◽  
Takahiro Tabata ◽  
Youichiro Wada ◽  
Takeshi Fujisaki ◽  
Takeshi Iida ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Transendothelial Migration ◽  
Low Density ◽  
Oxidized Low Density Lipoprotein ◽  
Kinase C

scholarly journals Loss of Low-Density Lipoprotein Utilization by Regressing Porcine Luteal Cells: Effects of Protein Kinase C Activation1

1995 ◽  
Vol 52 (4) ◽  
pp. 793-797 ◽  
Author(s):  
John D. Brannian ◽  
Heather Christianson ◽  
Sarah Flynn ◽  
Scott G. Kurz
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Low Density ◽  
Luteal Cells ◽  
Kinase C ◽  
Porcine Luteal Cells

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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