Effects of protein kinase A and G inhibitors on hippocampal cholinergic markers expressions in rolipram- and sildenafil-induced spatial memory improvement

2012 ◽  
Vol 101 (3) ◽  
pp. 311-319 ◽  
Author(s):  
Ali Hosseini-Sharifabad ◽  
Mohammad Hossein Ghahremani ◽  
Omid Sabzevari ◽  
Naser Naghdi ◽  
Mohammad Abdollahi ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Spatial Memory ◽  
Protein Kinase A ◽  
Memory Improvement ◽  
Cholinergic Markers ◽  
Kinase A

Hippocampal levels of phosphorylated protein kinase a (phosphor-S96) are linked to spatial memory enhancement by SGS742

Hippocampus ◽  
2009 ◽  
Vol 19 (1) ◽  
pp. 90-98 ◽  
Author(s):  
Berta Sunyer ◽  
Ki-Shuk Shim ◽  
Gunyong An ◽  
Harald Höger ◽  
Gert Lubec
Keyword(s):  
Protein Kinase ◽  
Spatial Memory ◽  
Protein Kinase A ◽  
Memory Enhancement ◽  
Phosphorylated Protein ◽  
Kinase A

scholarly journals NF-κB Regulates Spatial Memory Formation and Synaptic Plasticity through Protein Kinase A/CREB Signaling

2006 ◽  
Vol 26 (8) ◽  
pp. 2936-2946 ◽  
Author(s):  
Barbara Kaltschmidt ◽  
Delphine Ndiaye ◽  
Martin Korte ◽  
Stéphanie Pothion ◽  
Laurence Arbibe ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Spatial Memory ◽  
Protein Kinase A ◽  
De Novo ◽  
Memory Formation ◽  
Synaptic Activity ◽  
Gene Profiling ◽  
Long Term Memory ◽  
Critical Function ◽  
Kinase A

ABSTRACT Synaptic activity-dependent de novo gene transcription is crucial for long-lasting neuronal plasticity and long-term memory. In a forebrain neuronal conditional NF-κB-deficient mouse model, we demonstrate here that the transcription factor NF-κB regulates spatial memory formation, synaptic transmission, and plasticity. Gene profiling experiments and analysis of regulatory regions identified the α catalytic subunit of protein kinase A (PKA), an essential memory regulator, as a new NF-κB target gene. Consequently, NF-κB inhibition led to a decrease in forskolin-induced CREB phosphorylation. Collectively, these results disclose a novel hierarchical transcriptional network involving NF-κB, PKA, and CREB that leads to concerted nuclear transduction of synaptic signals in neurons, accounting for the critical function of NF-κB in learning and memory.

Regulation of spontaneous and induced resumption of meiosis in mouse oocytes by different intracellular pathways

Reproduction ◽  
2000 ◽  
pp. 377-383 ◽  
Author(s):  
L Leonardsen ◽  
A Wiersma ◽  
M Baltsen ◽  
AG Byskov ◽  
CY Andersen
Keyword(s):  
Signal Transduction ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Mitogen Activated Protein Kinase ◽  
Meiotic Maturation ◽  
Mouse Oocytes ◽  
Mitogen Activated Protein ◽  
Dependent Signal ◽  
Kinase Pathway ◽  
Kinase A

The mitogen-activated protein kinase-dependent and the cAMP-protein kinase A-dependent signal transduction pathways were studied in cultured mouse oocytes during induced and spontaneous meiotic maturation. The role of the mitogen-activated protein kinase pathway was assessed using PD98059, which specifically inhibits mitogen-activated protein kinase 1 and 2 (that is, MEK1 and MEK2), which activates mitogen-activated protein kinase. The cAMP-dependent protein kinase was studied by treating oocytes with the protein kinase A inhibitor rp-cAMP. Inhibition of the mitogen-activated protein kinase pathway by PD98059 (25 micromol l(-1)) selectively inhibited the stimulatory effect on meiotic maturation by FSH and meiosis-activating sterol (that is, 4,4-dimethyl-5alpha-cholest-8,14, 24-triene-3beta-ol) in the presence of 4 mmol hypoxanthine l(-1), whereas spontaneous maturation in the absence of hypoxanthine was unaffected. This finding indicates that different signal transduction mechanisms are involved in induced and spontaneous maturation. The protein kinase A inhibitor rp-cAMP induced meiotic maturation in the presence of 4 mmol hypoxanthine l(-1), an effect that was additive to the maturation-promoting effect of FSH and meiosis-activating sterol, indicating that induced maturation also uses the cAMP-protein kinase A-dependent signal transduction pathway. In conclusion, induced and spontaneous maturation of mouse oocytes appear to use different signal transduction pathways.

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