scholarly journals Heparanase Induces Endothelial Cell Migration via Protein Kinase B/Akt Activation

2004 ◽  
Vol 279 (22) ◽  
pp. 23536-23541 ◽  
Author(s):  
Svetlana Gingis-Velitski ◽  
Anna Zetser ◽  
Moshe Y. Flugelman ◽  
Israel Vlodavsky ◽  
Neta Ilan
Keyword(s):  
Cell Migration ◽  
Endothelial Cell ◽  
Protein Kinase ◽  
Protein Kinase B ◽  
Endothelial Cell Migration ◽  
Akt Activation

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 Inactivation of Foxo3a and Subsequent Downregulation of PGC-1α Mediate Nitric Oxide-Induced Endothelial Cell Migration

2010 ◽  
Vol 30 (16) ◽  
pp. 4035-4044 ◽  
Author(s):  
Sara Borniquel ◽  
Nieves García-Quintáns ◽  
Inmaculada Valle ◽  
Yolanda Olmos ◽  
Brigitte Wild ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Cell Migration ◽  
Endothelial Cell ◽  
Protein Kinase ◽  
Endothelial Cell Migration ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor ◽  
Endothelial Migration ◽  
Endothelial Nitric Oxide

ABSTRACT In damaged or proliferating endothelium, production of nitric oxide (NO) from endothelial nitric oxide synthase (eNOS) is associated with elevated levels of reactive oxygen species (ROS), which are necessary for endothelial migration. We aimed to elucidate the mechanism that mediates NO induction of endothelial migration. NO downregulates expression of peroxisome proliferator-activated receptor γ coactivator 1α (PGC-1α), which positively modulates several genes involved in ROS detoxification. We tested whether NO-induced cell migration requires PGC-1α downregulation and investigated the regulatory pathway involved. PGC-1α negatively regulated NO-dependent endothelial cell migration in vitro, and inactivation of the phosphatidylinositol 3-kinase (PI3K)/protein kinase B (Akt) pathway, which is activated by NO, reduced NO-mediated downregulation of PGC-1α. Expression of constitutively active Foxo3a, a target for Akt-mediated inactivation, reduced NO-dependent PGC-1α downregulation. Foxo3a is also a direct transcriptional regulator of PGC-1α, and we found that a functional FoxO binding site in the PGC-1α promoter is also a NO response element. These results show that NO-mediated downregulation of PGC-1α is necessary for NO-induced endothelial migration and that NO/protein kinase G (PKG)-dependent downregulation of PGC-1α and the ROS detoxification system in endothelial cells are mediated by the PI3K/Akt signaling pathway and subsequent inactivation of the FoxO transcription factor Foxo3a.

scholarly journals Protein Kinase D1 Regulates VEGF-A-Induced αvβ3 Integrin Trafficking and Endothelial Cell Migration

Traffic ◽  
2010 ◽  
Vol 11 (8) ◽  
pp. 1107-1118 ◽  
Author(s):  
Laura Di Blasio ◽  
Sara Droetto ◽  
Jim Norman ◽  
Federico Bussolino ◽  
Luca Primo
Keyword(s):  
Cell Migration ◽  
Endothelial Cell ◽  
Protein Kinase ◽  
Endothelial Cell Migration ◽  
Αvβ3 Integrin ◽  
Protein Kinase D1

scholarly journals Multiple Roles of Protein Kinase A in Arachidonic Acid–Mediated Ca2+ Entry and Tumor-Derived Human Endothelial Cell Migration

2010 ◽  
Vol 8 (11) ◽  
pp. 1466-1476 ◽  
Author(s):  
Alessandra Fiorio Pla ◽  
Tullio Genova ◽  
Emanuela Pupo ◽  
Cristiana Tomatis ◽  
Armando Genazzani ◽  
...  
Keyword(s):  
Arachidonic Acid ◽  
Cell Migration ◽  
Endothelial Cell ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Multiple Roles ◽  
Endothelial Cell Migration ◽  
Human Endothelial Cell ◽  
Kinase A

Involvement of Akt1/protein kinase Bα in tumor conditioned medium-induced endothelial cell migration and survival in vitro

2009 ◽  
Vol 135 (11) ◽  
pp. 1543-1550 ◽  
Author(s):  
Ming Li Tu ◽  
Han Qin Wang ◽  
Long Ju Chen ◽  
Jin Chang Lu ◽  
Fei Jiang ◽  
...  
Keyword(s):  
Cell Migration ◽  
Endothelial Cell ◽  
Protein Kinase ◽  
Conditioned Medium ◽  
Endothelial Cell Migration
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