scholarly journals Pre-exposure to adenosine, acting via A2Areceptors on endothelial cells, alters the protein kinase A dependence of adenosine-induced dilation in skeletal muscle resistance arterioles

2014 ◽  
Vol 592 (12) ◽  
pp. 2575-2590 ◽  
Author(s):  
Nir Maimon ◽  
Patricia A. Titus ◽  
Ingrid H. Sarelius
Keyword(s):  
Skeletal Muscle ◽  
Endothelial Cells ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
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 Stress-induced increase in skeletal muscle force requires protein kinase A phosphorylation of the ryanodine receptor

2012 ◽  
Vol 590 (24) ◽  
pp. 6381-6387 ◽  
Author(s):  
Daniel C. Andersson ◽  
Matthew J. Betzenhauser ◽  
Steven Reiken ◽  
Alisa Umanskaya ◽  
Takayuki Shiomi ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Ryanodine Receptor ◽  
Muscle Force ◽  
Kinase A

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.

scholarly journals Protein kinase A–dependent modulation of Ca2+ sensitivity in cardiac and fast skeletal muscles after reconstitution with cardiac troponin

2009 ◽  
Vol 133 (6) ◽  
pp. 571-581 ◽  
Author(s):  
Douchi Matsuba ◽  
Takako Terui ◽  
Jin O-Uchi ◽  
Hiroyuki Tanaka ◽  
Takao Ojima ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Cardiac Muscle ◽  
Protein Kinase A ◽  
Striated Muscle ◽  
Physiological Mechanism ◽  
Adrenergic Stimulation ◽  
Fast Skeletal Muscle ◽  
Psoas Muscles ◽  
Kinase A

Protein kinase A (PKA)-dependent phosphorylation of troponin (Tn)I represents a major physiological mechanism during β-adrenergic stimulation in myocardium for the reduction of myofibrillar Ca2+ sensitivity via weakening of the interaction with TnC. By taking advantage of thin filament reconstitution, we directly investigated whether or not PKA-dependent phosphorylation of cardiac TnI (cTnI) decreases Ca2+ sensitivity in different types of muscle: cardiac (porcine ventricular) and fast skeletal (rabbit psoas) muscles. PKA enhanced phosphorylation of cTnI at Ser23/24 in skinned cardiac muscle and decreased Ca2+ sensitivity, of which the effects were confirmed after reconstitution with the cardiac Tn complex (cTn) or the hybrid Tn complex (designated as PCRF; fast skeletal TnT with cTnI and cTnC). Reconstitution of cardiac muscle with the fast skeletal Tn complex (sTn) not only increased Ca2+ sensitivity, but also abolished the Ca2+-desensitizing effect of PKA, supporting the view that the phosphorylation of cTnI, but not that of other myofibrillar proteins, such as myosin-binding protein C, primarily underlies the PKA-induced Ca2+ desensitization in cardiac muscle. Reconstitution of fast skeletal muscle with cTn decreased Ca2+ sensitivity, and PKA further decreased Ca2+ sensitivity, which was almost completely restored to the original level upon subsequent reconstitution with sTn. The essentially same result was obtained when fast skeletal muscle was reconstituted with PCRF. It is therefore suggested that the PKA-dependent phosphorylation or dephosphorylation of cTnI universally modulates Ca2+ sensitivity associated with cTnC in the striated muscle sarcomere, independent of the TnT isoform.

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
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