scholarly journals Protein Kinase C-related Kinase and ROCK Are Required for Thrombin-induced Endothelial Cell Permeability Downstream from Gα12/13 and Gα11/q

2008 ◽  
Vol 283 (44) ◽  
pp. 29888-29896 ◽  
Author(s):  
Julie Gavard ◽  
J. Silvio Gutkind
Keyword(s):  
Protein Kinase C ◽  
Endothelial Cell ◽  
Protein Kinase ◽  
Cell Permeability ◽  
Kinase C ◽  
Endothelial Cell Permeability

Endothelial-cell permeability and protein kinase C in pre-eclampsia

The Lancet ◽  
1998 ◽  
Vol 351 (9107) ◽  
pp. 945-949 ◽  
Author(s):  
Hermann Haller ◽  
Albrecht Hempel ◽  
Volker Homuth ◽  
Anja Mandelkow ◽  
Andreas Busjahn ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Endothelial Cell ◽  
Protein Kinase ◽  
Cell Permeability ◽  
Kinase C ◽  
Endothelial Cell Permeability

scholarly journals Calcium Antagonists Ameliorate Ischemia-Induced Endothelial Cell Permeability by Inhibiting Protein Kinase C

Circulation ◽  
1999 ◽  
Vol 99 (19) ◽  
pp. 2523-2529 ◽  
Author(s):  
Albrecht Hempel ◽  
Carsten Lindschau ◽  
Christian Maasch ◽  
Matthias Mahn ◽  
Rostislav Bychkov ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Endothelial Cell ◽  
Protein Kinase ◽  
Calcium Antagonists ◽  
Cell Permeability ◽  
Kinase C ◽  
Endothelial Cell Permeability ◽  
Inhibiting Protein

d-Glucose and insulin stimulate migration and tubular formation of human endothelial cells in vitro

1999 ◽  
Vol 277 (3) ◽  
pp. E433-E438 ◽  
Author(s):  
Satoshi Shigematsu ◽  
Keishi Yamauchi ◽  
Kohji Nakajima ◽  
Sachiko Iijima ◽  
Toru Aizawa ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Cell Migration ◽  
Endothelial Cell ◽  
Protein Kinase ◽  
Kinase Inhibitor ◽  
Endothelial Cell Migration ◽  
Insulin Effect ◽  
Kinase C ◽  
Tubular Formation ◽  
Stimulation Of

Effects of highd-glucose and insulin on the endothelial cell migration and tubular formation were investigated with the use of ECV304 cells, a clonal human umbilical cord endothelial cell line. Exposure of the cells to highd-glucose resulted in a marked increase in the migration, which was blocked by inhibitors of protein kinase C such as H7 (10 μM) and GF109203X (200 nM). Furthermore, a protein kinase C agonist, phorbol 12-myristate 13-acetate, had an effect similar to that of glucose on ECV304 cells. Glucose stimulation of the migration was additively enhanced by 100 nM insulin, and the insulin effect was found to be unaffected by either PD-98059 or wortmannin, a mitogen-activated protein kinase (MAPK)/extracellular signal-regulated kinase inhibitor and a phosphatidylinositol 3-kinase inhibitor, respectively. Neither did H7 inhibit insulin stimulation of the migration. In contrast, a combination of high d-glucose and insulin, rather than either one alone, promoted tubular formation, which was inhibited by addition of 10 μM PD-98059. Stimulation of ECV304 cells by the combination of highd-glucose and insulin also caused an activation of MAPK, which was again obliterated by the same concentration of PD-98059. In conclusion, human endothelial cell migration and tubular formation are stimulated by highd-glucose and insulin in different ways. In the former reaction, either is effective, a combination of the two results in an additive effect, and activation of protein kinase C is involved. In contrast, tubular formation will only occur in the presence of a combination of highd-glucose and insulin, and MAPK plays an essential role.

scholarly journals Regulation of Thrombin-Induced Lung Endothelial Cell Barrier Disruption by Protein Kinase C Delta

PLoS ONE ◽  
2016 ◽  
Vol 11 (7) ◽  
pp. e0158865 ◽  
Author(s):  
Lishi Xie ◽  
Eddie T. Chiang ◽  
Xiaomin Wu ◽  
Gabriel T. Kelly ◽  
Prasad Kanteti ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Endothelial Cell ◽  
Protein Kinase ◽  
Protein Kinase C Delta ◽  
Barrier Disruption ◽  
Kinase C

scholarly journals Protein kinase C activators suppress stimulation of capillary endothelial cell growth by angiogenic endothelial mitogens.

1987 ◽  
Vol 104 (3) ◽  
pp. 679-687 ◽  
Author(s):  
S R Doctrow ◽  
J Folkman
Keyword(s):  
Cell Proliferation ◽  
Endothelial Cells ◽  
Protein Kinase C ◽  
Endothelial Cell ◽  
Growth Factor ◽  
Protein Kinase ◽  
Cell Growth ◽  
Human Hepatoma ◽  
Kinase C ◽  
Protein Kinase C Activators

The intracellular events regulating endothelial cell proliferation and organization into formalized capillaries are not known. We report that the protein kinase C activator beta-phorbol 12,13-dibutyrate (PDBu) suppresses bovine capillary endothelial (BCE) cell proliferation (K50 = 6 +/- 4 nM) and DNA synthesis in response to human hepatoma-derived growth factor, an angiogenic endothelial mitogen. In contrast, PDBu has no effect on the proliferation of bovine aortic endothelial cells and is mitogenic for bovine aortic smooth muscle and BALB/c 3T3 cells. Several observations indicate that the inhibition of human hepatoma-derived growth factor-stimulated BCE cell growth by PDBu is mediated through protein kinase C. Different phorbol compounds inhibit BCE cell growth according to their potencies as protein kinase C activators (12-O-tetradecanoylphorbol 13-acetate greater than PDBu much greater than beta-phorbol 12,13-diacetate much much greater than beta-phorbol; alpha-phorbol 12,13-dibutyrate; alpha-phorbol 12,13-didecanoate). PDBu binds to a single class of specific, saturable sites on the BCE cell with an apparent Kd of 8 nM, in agreement with reported affinities of PDBu for protein kinase C in other systems. Specific binding of PDBu to BCE cells is displaced by sn-1,2-dioctanoylglycerol, a protein kinase C activator and an analog of the putative second messenger activating this kinase in vivo. The weak protein kinase C activator, sn-1,2-dibutyrylglycerol, does not affect PDBu binding. A cytosolic extract from BCE cells contains a calcium/phosphatidylserine-dependent protein kinase that is activated by sn-1,2-dioctanoylglycerol and PDBu, but not by beta-phorbol. These findings indicate that protein kinase C activation can cause capillary endothelial cells to become desensitized to angiogenic endothelial mitogens. This intracellular regulatory mechanism might be invoked during certain phases of angiogenesis, for example when proliferating endothelial cells become differentiated to organize into nongrowing tubes.

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