Protein Kinase C-Mediated Inhibition of Cyclin A Expression in Human Vascular Endothelial Cells

1993 ◽  
Vol 193 (3) ◽  
pp. 991-998 ◽  
Author(s):  
C. Kosaka ◽  
T. Sasaguri ◽  
J. Masuda ◽  
K. Zen ◽  
K. Shimokado ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Vascular Endothelial Cells ◽  
Cyclin A ◽  
Vascular Endothelial ◽  
Kinase C

The Protein Kinase C Pathway Inhibits the Proliferation of Cultured Vascular Endothelial Cells Reducing Cyclin A Gene Expression

2006 ◽  
Vol 748 (1) ◽  
pp. 538-540
Author(s):  
CHIYA KOSAKA ◽  
TOSHIYUKI SASAGURI ◽  
KATSUHIRO ZEN ◽  
JUNICHI MASUDA ◽  
KENTARO SHIMOKADO ◽  
...  
Keyword(s):  
Gene Expression ◽  
Endothelial Cells ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Vascular Endothelial Cells ◽  
Cyclin A ◽  
Vascular Endothelial ◽  
Kinase C

scholarly journals Cell Growth Regulation through the Protein Kinase C Pathway in Cultured Human Vascular Endothelial Cells

1993 ◽  
Vol 57 (supplementIV) ◽  
pp. 1207-1210 ◽  
Author(s):  
Chiya Kosaka ◽  
Toshiyuki Sasaguri ◽  
Katsuhiro Zen ◽  
Junichi Masuda ◽  
Kentaro Shimokado ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Cell Growth ◽  
Growth Regulation ◽  
Vascular Endothelial Cells ◽  
Vascular Endothelial ◽  
Cell Growth Regulation ◽  
Kinase C

scholarly journals Disturbed flow: p53 SUMOylation in the turnover of endothelial cells

2011 ◽  
Vol 193 (5) ◽  
pp. 805-807 ◽  
Author(s):  
Wakako Takabe ◽  
Noah Alberts-Grill ◽  
Hanjoong Jo
Keyword(s):  
Endothelial Cells ◽  
Blood Flow ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Vascular Endothelial Cells ◽  
Vascular Endothelial ◽  
Protein Inhibitor ◽  
Disturbed Flow ◽  
Antiapoptotic Protein ◽  
Kinase C

Disturbed blood flow induces apoptosis of vascular endothelial cells, which causes atherosclerosis. In this issue, Heo et al. (2011. J. Cell Biol. doi:10.1083/jcb.201010051) sheds light on p53’s role in this phenomenon. Disturbed flow induces peroxynitrite production, which activates protein kinase C ζ and it’s binding to the E3 SUMO (small ubiquitin-like modifier) ligase PIASy (protein inhibitor of activated STATy). This leads to p53 SUMOylation and its export to the cytosol, where it binds to the antiapoptotic protein Bcl-2 to induce apoptosis.

scholarly journals PKC (Protein Kinase C)-δ Modulates AT (Antithrombin) Signaling in Vascular Endothelial Cells

2020 ◽  
Vol 40 (7) ◽  
pp. 1748-1762
Author(s):  
Sumith R. Panicker ◽  
Indranil Biswas ◽  
Hemant Giri ◽  
Xiaofeng Cai ◽  
Alireza R. Rezaie
Keyword(s):  
Endothelial Cells ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Intracellular Signaling ◽  
Vascular Endothelial Cells ◽  
Dominant Negative ◽  
Vascular Endothelial ◽  
Kinase C ◽  
Pkc Protein Kinase C ◽  
Anti Inflammatory

Objective: Native and latent conformers of AT (antithrombin) induce anti-inflammatory and proapoptotic signaling activities, respectively, in vascular endothelial cells by unknown mechanisms. Synd-4 (syndecan-4) has been identified as a receptor that is involved in transmitting signaling activities of AT in endothelial cells. Approach and Results: In this study, we used flow cytometry, signaling assays, immunoblotting and confocal immunofluorescence microscopy to investigate the mechanism of the paradoxical signaling activities of high-affinity heparin (native) and low-affinity heparin (latent) conformers of AT in endothelial cells. We discovered that native AT binds to glycosaminoglycans on vascular endothelial cells via its heparin-binding D-helix to induce anti-inflammatory signaling responses by recruiting PKC (protein kinase C)-δ to the plasma membrane and promoting phosphorylation of the Synd-4 cytoplasmic domain at Ser179. By contrast, the binding of latent AT to endothelial cells to a site(s), which is not competed by the native AT, induces a proapoptotic effect by localizing PKC-δ to the perinuclear/nuclear compartment in endothelial cells. Overexpression of a dominant-negative form of PKC-δ resulted in inhibition of anti-inflammatory and proapoptotic signaling activities of both native and latent AT. Conclusions: These results indicate that the native and latent conformers of AT may exert their distinct intracellular signaling effects through differentially modulating the subcellular localization of PKC-δ in endothelial cells.

Sign in / Sign up

Export Citation Format

Share Document