Mitogen-Activated Protein Kinase Regulates Early Phosphorylation and Delayed Expression of Ca2+/Calmodulin-Dependent Protein Kinase II in Long-Term Potentiation

Autor: Robert D. Blitzer, Kichiemon Asoma, Panayiotis Tsokas, John H. Morrison, Emmanuel M. Landau, Ravi Iyengar, Maria Grazia Giovannini, Tony Wong
Rok vydání: 2001
Předmět:
Male
MAPK/ERK pathway
medicine.medical_specialty
Long-Term Potentiation
Stimulation
In Vitro Techniques
Biology
Hippocampus
environment and public health
Rats
Sprague-Dawley
Ca2+/calmodulin-dependent protein kinase
Internal medicine
Receptors
Adrenergic
beta
Gene expression
medicine
Animals
Humans
ARTICLE
Enzyme Inhibitors
Phosphorylation
Theta Rhythm
Growth Substances
Protein kinase A
Mitogen-Activated Protein Kinase 7
Mitogen-Activated Protein Kinase 1
Mitogen-Activated Protein Kinase 3
Pyramidal Cells
musculoskeletal
neural
and ocular physiology
General Neuroscience
Isoproterenol
Excitatory Postsynaptic Potentials
Long-term potentiation
Adrenergic beta-Agonists
Electric Stimulation
Rats
Cell biology
enzymes and coenzymes (carbohydrates)
Endocrinology
nervous system
Organ Specificity
Mitogen-activated protein kinase
Calcium-Calmodulin-Dependent Protein Kinases
biology.protein
Mitogen-Activated Protein Kinases
biological phenomena
cell phenomena
and immunity
Calcium-Calmodulin-Dependent Protein Kinase Type 2
HeLa Cells
Zdroj: The Journal of Neuroscience. 21:7053-7062
ISSN: 1529-2401
0270-6474
DOI: 10.1523/jneurosci.21-18-07053.2001
Popis: Activation of mitogen-activated protein kinase (MAPK) and Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) are required for numerous forms of neuronal plasticity, including long-term potentiation (LTP). We induced LTP in rat hippocampal area CA1 using theta-pulse stimulation (TPS) paired with beta-adrenergic receptor activation [isoproterenol (ISO)], a protocol that may be particularly relevant to normal patterns of hippocampal activity during learning. This stimulation resulted in a transient phosphorylation of p42 MAPK, and the resulting LTP was MAPK dependent. In addition, CaMKII was regulated in two, temporally distinct ways after TPS-ISO: a transient rise in the fraction of phosphorylated CaMKII and a subsequent persistent increase in CaMKII expression. The increases in MAPK and CaMKII phosphorylation were strongly colocalized in the dendrites and cell bodies of CA1 pyramidal cells, and both the transient phosphorylation and delayed expression of CaMKII were prevented by inhibiting p42/p44 MAPK. These results establish a novel bimodal regulation of CaMKII by MAPK, which may contribute to both post-translational modification and increased gene expression.
Databáze: OpenAIRE
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