Requirement for Protein Kinase C θ for Cell Cycle Progression and Formation of Actin Stress Fibers and Filopodia in Vascular Endothelial Cells

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.

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131 Shear stress-induced activation of pinocytois in vascular endothelial cells is mediated by reactive oxygen species and protein kinase C

Proceedings of the JSME Bioengineering Conference and Seminar ◽

10.1299/jsmebs.2004.17.0_257 ◽

2005 ◽

Vol 2004.17 (0) ◽

pp. 257-258

Author(s):

Koichi NIWA ◽

Takeshi KARINO

Keyword(s):

Reactive Oxygen Species ◽

Endothelial Cells ◽

Shear Stress ◽

Protein Kinase C ◽

Protein Kinase ◽

Vascular Endothelial Cells ◽

Reactive Oxygen ◽

Vascular Endothelial ◽

Oxygen Species ◽

Kinase C

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E2F1, B-MYB and Selective Members of Cyclin/CDK Subunits Are Targets for Protein Kinase C-Mediated Bimodal Growth Regulation in Vascular Endothelial Cells

Biochemical and Biophysical Research Communications ◽

10.1006/bbrc.1994.1213 ◽

1994 ◽

Vol 199 (1) ◽

pp. 191-198 ◽

Cited By ~ 24

Author(s):

W. Zhou ◽

N. Takuwa ◽

M. Kumada ◽

Y. Takuwa

Keyword(s):

Endothelial Cells ◽

Protein Kinase C ◽

Protein Kinase ◽

Growth Regulation ◽

Vascular Endothelial Cells ◽

Vascular Endothelial ◽

Kinase C

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Protein Kinase C-Dependent Phosphorylation Regulates the Cell Cycle-Inhibitory Function of the p73 Carboxy Terminus Transactivation Domain

Molecular and Cellular Biology ◽

10.1128/mcb.00585-08 ◽

2009 ◽

Vol 29 (7) ◽

pp. 1814-1825 ◽

Cited By ~ 14

Author(s):

Ulrika Nyman ◽

Pinelopi Vlachos ◽

Anna Cascante ◽

Ola Hermanson ◽

Boris Zhivotovsky ◽

...

Keyword(s):

Cell Cycle ◽

Protein Kinase C ◽

Protein Kinase ◽

Cell Cycle Arrest ◽

Cell Cycle Progression ◽

Transactivation Domain ◽

Carboxy Terminus ◽

Cycle Progression ◽

Cycle Arrest ◽

Kinase C

ABSTRACT The transcription factor p73, a member of the p53 family of proteins, is involved in the regulation of cell cycle progression and apoptosis. However, the regulatory mechanisms controlling the distinct roles for p73 in these two processes have remained unclear. Here, we report that p73 is able to induce cell cycle arrest independently of its amino-terminal transactivation domain, whereas this domain is crucial for p73 proapoptotic functions. We also characterized a second transactivation domain in the carboxy terminus of p73 within amino acid residues 381 to 399. This carboxy terminus transactivation domain was found to preferentially regulate genes involved in cell cycle progression. Moreover, its activity is regulated throughout the cell cycle and modified by protein kinase C-dependent phosphorylation at serine residue 388. Our results suggest that this novel posttranslational modification within the p73 carboxy terminus transactivation domain is involved in the context-specific guidance of p73 toward the selective induction of cell cycle arrest.

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Hydroperoxide-Induced Diacylglycerol Formation and Protein Kinase C Activation in Vascular Endothelial Cells

Archives of Biochemistry and Biophysics ◽

10.1006/abbi.1993.1281 ◽

1993 ◽

Vol 303 (2) ◽

pp. 260-266 ◽

Cited By ~ 81

Author(s):

M.M. Taher ◽

J.G.N. Garcia ◽

V. Natarajan

Keyword(s):

Endothelial Cells ◽

Protein Kinase C ◽

Protein Kinase ◽

Vascular Endothelial Cells ◽

Vascular Endothelial ◽

Kinase C ◽

Protein Kinase C Activation

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

Arteriosclerosis Thrombosis and Vascular Biology ◽

10.1161/atvbaha.120.314479 ◽

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.

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