scholarly journals p38 Mitogen-Activated Protein Kinase Contributes to Adenosine A1 Receptor-Mediated Synaptic Depression in Area CA1 of the Rat Hippocampus

2006 ◽  
Vol 26 (48) ◽  
pp. 12427-12438 ◽  
Author(s):  
T. B. Brust ◽  
F. S. Cayabyab ◽  
N. Zhou ◽  
B. A. MacVicar
Keyword(s):  
Protein Kinase ◽  
Synaptic Depression ◽  
Adenosine A1 Receptor ◽  
Rat Hippocampus ◽  
Mitogen Activated Protein Kinase ◽  
Area Ca1 ◽  
Adenosine A1 ◽  
Mitogen Activated Protein ◽  
A1 Receptor

C-Jun N-terminal kinase regulates adenosine A1 receptor-mediated synaptic depression in the rat hippocampus

2007 ◽  
Vol 53 (8) ◽  
pp. 906-917 ◽  
Author(s):  
Tyson B. Brust ◽  
Francisco S. Cayabyab ◽  
Brian A. MacVicar
Keyword(s):  
Synaptic Depression ◽  
Adenosine A1 Receptor ◽  
Rat Hippocampus ◽  
Adenosine A1 ◽  
A1 Receptor

scholarly journals The Signaling Pathways Involved in the Anticonvulsive Effects of the Adenosine A1 Receptor

2020 ◽  
Vol 22 (1) ◽  
pp. 320
Author(s):  
Jeroen Spanoghe ◽  
Lars E. Larsen ◽  
Erine Craey ◽  
Simona Manzella ◽  
Annelies Van Dycke ◽  
...  
Keyword(s):  
Signaling Pathways ◽  
G Protein ◽  
Receptor Activation ◽  
Adenosine A1 Receptor ◽  
Mitogen Activated Protein Kinase ◽  
Neuronal Inhibition ◽  
Adenosine A1 ◽  
Mitogen Activated Protein ◽  
A1 Receptor ◽  
G Protein Coupled

Adenosine acts as an endogenous anticonvulsant and seizure terminator in the brain. Many of its anticonvulsive effects are mediated through the activation of the adenosine A1 receptor, a G protein-coupled receptor with a wide array of targets. Activating A1 receptors is an effective approach to suppress seizures. This review gives an overview of the neuronal targets of the adenosine A1 receptor focusing in particular on signaling pathways resulting in neuronal inhibition. These include direct interactions of G protein subunits, the adenyl cyclase pathway and the phospholipase C pathway, which all mediate neuronal hyperpolarization and suppression of synaptic transmission. Additionally, the contribution of the guanyl cyclase and mitogen-activated protein kinase cascades to the seizure-suppressing effects of A1 receptor activation are discussed. This review ends with the cautionary note that chronic activation of the A1 receptor might have detrimental effects, which will need to be avoided when pursuing A1 receptor-based epilepsy therapies.

Phosphorylation and Activation of Mitogen-Activated Protein Kinase by Kainic Acid-Induced Seizure in Rat Hippocampus

1994 ◽  
Vol 202 (2) ◽  
pp. 1163-1168 ◽  
Author(s):  
Y.S. Kim ◽  
K.S. Hong ◽  
Y.S. Seong ◽  
J.B. Park ◽  
S. Kuroda ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Kainic Acid ◽  
Rat Hippocampus ◽  
Mitogen Activated Protein Kinase ◽  
Mitogen Activated Protein

scholarly journals Differential Activation of Mitogen-Activated Protein Kinase Pathways after Traumatic Brain Injury in the Rat Hippocampus

2002 ◽  
Vol 22 (3) ◽  
pp. 327-334 ◽  
Author(s):  
Naoki Otani ◽  
Hiroshi Nawashiro ◽  
Shinji Fukui ◽  
Namiko Nomura ◽  
Akiko Yano ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Traumatic Brain Injury ◽  
Brain Injury ◽  
Protein Kinase ◽  
Pyramidal Cell ◽  
Pyramidal Neurons ◽  
Rat Hippocampus ◽  
Mitogen Activated Protein Kinase ◽  
Mitogen Activated Protein ◽  
Cell Layers

Mitogen-activated protein kinases, which play a crucial role in signal transduction, are activated by phosphorylation in response to a variety of mitogenic signals. In the present study, the authors used Western blot analysis and immunohistochemistry to show that phosphorylated extracellular signal-regulated protein kinase (p-ERK) and c-Jun NH(2)-terminal kinase (p-JNK), but not p38 mitogen-activated protein kinase, significantly increased in both the neurons and astrocytes after traumatic brain injury in the rat hippocampus. Different immunoreactivities of p-ERK and p-JNK were observed in the pyramidal cell layers and dentate hilar cells immediately after traumatic brain injury. Immunoreactivity for p-JNK was uniformly induced but was only transiently induced throughout all pyramidal cell layers. However, strong immunoreactivity for p-ERK was observed in the dentate hilar cells and the damaged CA3 neurons, along with the appearance of pyknotic morphologic changes. In addition, immunoreactivity for p-ERK was seen in astrocytes surrounding dentate and CA3 pyramidal neurons 6 hours after traumatic brain injury. These findings suggest that ERK and JNK but not p38 cascades may be closely involved in signal transduction in the rat hippocampus after traumatic brain injury.

Upregulated renal adenosine A1 receptors augment PKC and glucose transport but inhibit proliferation

1996 ◽  
Vol 270 (2) ◽  
pp. F263-F274 ◽  
Author(s):  
R. Coulson ◽  
P. S. Proch ◽  
R. A. Olsson ◽  
C. E. Chalfant ◽  
D. R. Cooper
Keyword(s):  
Cell Proliferation ◽  
Protein Kinase ◽  
Glucose Uptake ◽  
Glucose Transport ◽  
Adenosine Receptor ◽  
Adenosine A1 Receptor ◽  
Receptor Antagonists ◽  
Caffeine Treatment ◽  
Adenosine A1 ◽  
A1 Receptor

Adenosine A1 receptor densities were increased in cultured LLC-PK1 and OK cells by chronic treatment with the adenosine receptor antagonists 1,3,7-trimethylxanthine (caffeine, 1 mM) and 1,3-dimethyl-8-cyclopentylxanthine [cyclopentyltheophylline (CPT), < or = 0.4 mM], respectively. The A1 receptor number per cell was increased twofold by 10-day treatments with 1 mM caffeine or 0.1 mM CPT, and the sodium-coupled glucose uptake was augmented twofold by 1 mM caffeine and sevenfold by 0.1 microM CPT (higher doses of CPT were progressively less stimulatory). Glucose uptake was blocked by acute (2-h) treatment with CPT, adenosine deaminase, or calphostin C. Caffeine (1 mM) or CPT (> or = 0.1 mM) inhibited cell proliferation for the first 10 days, then cell growth assumed a normal proliferative rate despite continued presence of antagonist. Cytosolic protein kinase C (PKC) beta-isoform immunoactivity and PKC-beta II mRNA were elevated at least twofold during 10 days of 0.1 mM CPT or 1 mM caffeine treatment. The sustained elevation in sodium-glucose symport and PKC activity observed with adenosine receptor antagonists was similar to acute (2-h) effects of the adenosine A1 agonist R(-)-N6-phenylisopropyladenosine (R-PIA, 0.1-1 microM). Moreover, cell proliferation was increased by adenosine (0.1 microM R-PIA), whereas Na-K-adenosinetriphosphatase activity was unaltered with chronic antagonist or acute adenosine treatments. Caffeine treatment may have some non-adenosine A1 receptor-mediated actions, because it slightly (30%) augmented protein kinase A activity. It is concluded that chronic exposure of proximal tubule cells to caffeine or CPT augments PKC and sodium-glucose transport but retards cell proliferation mainly via adenosine A1 receptor-mediated mechanisms.

Sign in / Sign up

Export Citation Format

Share Document