Noradrenaline reduces the ATP-stimulated phosphorylation of p38 MAP kinase via β-adrenergic receptors–cAMP–protein kinase A-dependent mechanism in cultured rat spinal microglia

2009 ◽  
Vol 55 (4) ◽  
pp. 226-234 ◽  
Author(s):  
Norimitsu Morioka ◽  
Hirokazu Tanabe ◽  
Atsuko Inoue ◽  
Toshihiro Dohi ◽  
Yoshihiro Nakata
Keyword(s):  
Protein Kinase ◽  
Map Kinase ◽  
Protein Kinase A ◽  
Adrenergic Receptors ◽  
P38 Map Kinase ◽  
Β Adrenergic Receptors ◽  
Kinase A ◽  
Dependent Mechanism

scholarly journals Reconstitution of β-adrenergic regulation of CaV1.2: Rad-dependent and Rad-independent protein kinase A mechanisms

2021 ◽  
Vol 118 (21) ◽  
pp. e2100021118
Author(s):  
Moshe Katz ◽  
Suraj Subramaniam ◽  
Orna Chomsky-Hecht ◽  
Vladimir Tsemakhovich ◽  
Veit Flockerzi ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Adrenergic Receptors ◽  
Calcium Influx ◽  
Inhibitory Protein ◽  
Reconstituted System ◽  
Distinct Features ◽  
Β Adrenergic Receptors ◽  
Independent Protein ◽  
Kinase A

L-type voltage-gated CaV1.2 channels crucially regulate cardiac muscle contraction. Activation of β-adrenergic receptors (β-AR) augments contraction via protein kinase A (PKA)–induced increase of calcium influx through CaV1.2 channels. To date, the full β-AR cascade has never been heterologously reconstituted. A recent study identified Rad, a CaV1.2 inhibitory protein, as essential for PKA regulation of CaV1.2. We corroborated this finding and reconstituted the complete pathway with agonist activation of β1-AR or β2-AR in Xenopus oocytes. We found, and distinguished between, two distinct pathways of PKA modulation of CaV1.2: Rad dependent (∼80% of total) and Rad independent. The reconstituted system reproduces the known features of β-AR regulation in cardiomyocytes and reveals several aspects: the differential regulation of posttranslationally modified CaV1.2 variants and the distinct features of β1-AR versus β2-AR activity. This system allows for the addressing of central unresolved issues in the β-AR–CaV1.2 cascade and will facilitate the development of therapies for catecholamine-induced cardiac pathologies.

scholarly journals Reciprocal Regulation of Aquaporin-2 Abundance and Degradation by Protein Kinase A and p38-MAP Kinase

2010 ◽  
Vol 21 (10) ◽  
pp. 1645-1656 ◽  
Author(s):  
Pavel I. Nedvetsky ◽  
Vedrana Tabor ◽  
Grazia Tamma ◽  
Sven Beulshausen ◽  
Philipp Skroblin ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Map Kinase ◽  
Protein Kinase A ◽  
P38 Map Kinase ◽  
Reciprocal Regulation ◽  
Aquaporin 2 ◽  
Kinase A

B-Raf-dependent regulation of the MEK-1/mitogen-activated protein kinase pathway in PC12 cells and regulation by cyclic AMP

1994 ◽  
Vol 14 (10) ◽  
pp. 6522-6530
Author(s):  
R R Vaillancourt ◽  
A M Gardner ◽  
G L Johnson
Keyword(s):  
Growth Factor ◽  
Protein Kinase ◽  
Map Kinase ◽  
Protein Kinase A ◽  
Pc12 Cells ◽  
Kinase Activation ◽  
Mitogen Activated Protein ◽  
Epidermal Growth ◽  
Camp Levels ◽  
Kinase A

Growth factor receptor tyrosine kinase regulation of the sequential phosphorylation reactions leading to mitogen-activated protein (MAP) kinase activation in PC12 cells has been investigated. In response to epidermal growth factor, nerve growth factor, and platelet-derived growth factor, B-Raf and Raf-1 are activated, phosphorylate recombinant kinase-inactive MEK-1, and activate wild-type MEK-1. MEK-1 is the dual-specificity protein kinase that selectively phosphorylates MAP kinase on tyrosine and threonine, resulting in MAP kinase activation. B-Raf and Raf-1 are growth factor-regulated Raf family members which regulate MEK-1 and MAP kinase activity in PC12 cells. Protein kinase A activation in response to elevated cyclic AMP (cAMP) levels inhibited B-Raf and Raf-1 stimulation in response to growth factors. Ras.GTP loading in response to epidermal growth factor, nerve growth factor, or platelet-derived growth factor was unaffected by protein kinase A activation. Even though elevated cAMP levels inhibited Raf activation, the growth factor activation of MEK-1 and MAP kinase was unaffected in PC12 cells. The results demonstrate that tyrosine kinase receptor activation of MEK-1 and MAP kinase in PC12 cells is regulated by B-Raf and Raf-1, whose activation is inhibited by protein kinase A, and MEK activators, whose activation is independent of cAMP regulation.

A cyclic AMP protein kinase A-dependent mechanism by which rotavirus impairs the expression and enzyme activity of brush border-associated sucrase-isomaltase in differentiated intestinal Caco-2 cells

2004 ◽  
Vol 6 (8) ◽  
pp. 719-731 ◽  
Author(s):  
Sandra Martin-Latil ◽  
Jacqueline Cotte-Laffitte ◽  
Isabelle Beau ◽  
Anne-Marie Quéro ◽  
Monique Géniteau-Legendre ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Protein Kinase ◽  
Cyclic Amp ◽  
Protein Kinase A ◽  
Brush Border ◽  
Kinase A ◽  
Dependent Mechanism

Cytokines induce protein kinase A-mediated signalling by a redox-dependent mechanism in rat renal mesangial cells

2015 ◽  
Vol 93 (3) ◽  
pp. 362-369 ◽  
Author(s):  
Karl-Friedrich Beck ◽  
Johannes Euler ◽  
Florian Eisel ◽  
Martina Beck ◽  
Yvette Köhler ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Mesangial Cells ◽  
Kinase A ◽  
Dependent Mechanism
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