Dynein–dynactin complex mediates protein kinase A-dependent clustering of Weibel–Palade bodies in endothelial cells

2006 ◽  
Vol 45 (3) ◽  
pp. e151
Author(s):  
A. Kragt ◽  
R. Bierings ◽  
M.G. Rondaij ◽  
K.A. Gijzen ◽  
E. Sellink ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Dynactin Complex ◽  
Kinase A

scholarly journals Dynein–Dynactin Complex Mediates Protein Kinase A–Dependent Clustering of Weibel-Palade Bodies in Endothelial Cells

2006 ◽  
Vol 26 (1) ◽  
pp. 49-55 ◽  
Author(s):  
Mariska G. Rondaij ◽  
Ruben Bierings ◽  
Astrid Kragt ◽  
Karina A. Gijzen ◽  
Erica Sellink ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Dynactin Complex ◽  
Kinase A

scholarly journals Characterization of a Novel Chemokine-Containing Storage Granule in Endothelial Cells: Evidence for Preferential Exocytosis Mediated by Protein Kinase A and Diacylglycerol

2005 ◽  
Vol 175 (8) ◽  
pp. 5358-5369 ◽  
Author(s):  
Inger Øynebråten ◽  
Nicolas Barois ◽  
Kathrine Hagelsteen ◽  
Finn-Eirik Johansen ◽  
Oddmund Bakke ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Storage Granule ◽  
Kinase A

scholarly journals Matrix-Specific Protein Kinase A Signaling Regulates p21-Activated Kinase Activation by Flow in Endothelial Cells

2010 ◽  
Vol 106 (8) ◽  
pp. 1394-1403 ◽  
Author(s):  
Steven Daniel Funk ◽  
Arif Yurdagul ◽  
Jonette M. Green ◽  
Krishna A. Jhaveri ◽  
Martin Alexander Schwartz ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Specific Protein ◽  
Kinase Activation ◽  
P21 Activated Kinase ◽  
Kinase A ◽  
Specific Protein Kinase

scholarly journals Integrin Cross-talk in Endothelial Cells Is Regulated by Protein Kinase A and Protein Phosphatase 1

2008 ◽  
Vol 283 (46) ◽  
pp. 31849-31860 ◽  
Author(s):  
Annette M. Gonzalez ◽  
Jessica Claiborne ◽  
Jonathan C. R. Jones
Keyword(s):  
Endothelial Cells ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Cross Talk ◽  
Protein Phosphatase ◽  
Protein Phosphatase 1 ◽  
Kinase A

scholarly journals Protein kinase A negatively regulates VEGF-induced AMPK activation by phosphorylating CaMKK2 at serine 495

2020 ◽  
Vol 477 (17) ◽  
pp. 3453-3469 ◽  
Author(s):  
Katrin Spengler ◽  
Darya Zibrova ◽  
Angela Woods ◽  
Christopher G. Langendorf ◽  
John W. Scott ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Ampk Activation ◽  
Dependent Protein ◽  
And Function ◽  
Amp Activated Protein Kinase ◽  
Camp Elevation ◽  
Kinase A ◽  
In Cells

Activation of AMP-activated protein kinase (AMPK) in endothelial cells by vascular endothelial growth factor (VEGF) via the Ca2+/calmodulin-dependent protein kinase kinase 2 (CaMKK2) represents a pro-angiogenic pathway, whose regulation and function is incompletely understood. This study investigates whether the VEGF/AMPK pathway is regulated by cAMP-mediated signalling. We show that cAMP elevation in endothelial cells by forskolin, an activator of the adenylate cyclase, and/or 3-isobutyl-1-methylxanthine (IBMX), an inhibitor of phosphodiesterases, triggers protein kinase A (PKA)-mediated phosphorylation of CaMKK2 (serine residues S495, S511) and AMPK (S487). Phosphorylation of CaMKK2 by PKA led to an inhibition of its activity as measured in CaMKK2 immunoprecipitates of forskolin/IBMX-treated cells. This inhibition was linked to phosphorylation of S495, since it was not seen in cells expressing a non-phosphorylatable CaMKK2 S495C mutant. Phosphorylation of S511 alone in these cells was not able to inhibit CaMKK2 activity. Moreover, phosphorylation of AMPK at S487 was not sufficient to inhibit VEGF-induced AMPK activation in cells, in which PKA-mediated CaMKK2 inhibition was prevented by expression of the CaMKK2 S495C mutant. cAMP elevation in endothelial cells reduced basal and VEGF-induced acetyl-CoA carboxylase (ACC) phosphorylation at S79 even if AMPK was not inhibited. Together, this study reveals a novel regulatory mechanism of VEGF-induced AMPK activation by cAMP/PKA, which may explain, in part, inhibitory effects of PKA on angiogenic sprouting and play a role in balancing pro- and anti-angiogenic mechanisms in order to ensure functional angiogenesis.

Activation of the Adenylyl Cyclase/Cyclic AMP/Protein Kinase A Pathway in Endothelial Cells Exposed to Cyclic Strain

1997 ◽  
Vol 231 (1) ◽  
pp. 184-189 ◽  
Author(s):  
C.Richard Cohen ◽  
Ira Mills ◽  
Wei Du ◽  
Khurram Kamal ◽  
Bauer E. Sumpio
Keyword(s):  
Endothelial Cells ◽  
Protein Kinase ◽  
Cyclic Amp ◽  
Protein Kinase A ◽  
Adenylyl Cyclase ◽  
Cyclic Strain ◽  
Kinase A

Regulation of endothelial cell integrin function and angiogenesis by COX-2, cAMP and Protein Kinase A

2003 ◽  
Vol 90 (10) ◽  
pp. 577-585 ◽  
Author(s):  
Olivier Dormond ◽  
Curzio Rüegg
Keyword(s):  
Endothelial Cells ◽  
Cell Migration ◽  
Endothelial Cell ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Tumor Angiogenesis ◽  
Endothelial Cell Migration ◽  
Cox 2 ◽  
Cox 2 Inhibitors ◽  
Kinase A

SummaryAngiogenesis, the development of new blood vessels from preexisting vessels, is a key step in tumor growth, invasion and metastasis formation. Inhibition of tumor angiogenesis is considered as an attractive approach to suppress cancer progression and spreading. Adhesion receptors of the integrin family promote tumor angiogenesis by mediating cell migration, proliferation and survival of angiogenic endothelial cells. Integrins up regulated and highly expressed on neovascular endothelial cells, such as αVβ3 and α5β1, have been considered as relevant targets for anti-angiogenic therapies. Small molecular integrin antagonists or blocking antibodies suppress angiogenesis and tumor progression in many animal models, and some of them are currently being tested in cancer clinical trials as anti-angiogenic agents. COX-2 inhibitors exert anti-cancer effects, at least in part, by inhibiting tumor angiogenesis. We have recently shown that COX-2 inhibitors suppress endothelial cell migration and angiogenesis by preventing αVβ3-mediated and cAMP/PKA-dependent activation of the small GTPases Rac and Cdc42. Here we will review the evidence for the involvement of vascular integrins in mediating angiogenesis and the role of COX-2 metabolites in modulating the cAMP/Protein Kinase A pathway and αVβ3-dependent Rac activation in endothelial cells.The pulication was partially financed by Serono Foundation for the Advancement of Medical Sience.Part of this paper was originally presented at the 2nd International Workshop on New Therapeutic Targets in Vascular Biology from February 6–9, 2003 in Geneva, Switzerland.

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