Cited by 226Neuroscience and Neuropharmacology ResearchMemory and Neural MechanismsProtein Kinase Regulation and GTPase Signaling

Increased phosphorylation of Ca2++/calmodulin-dependent protein kinase II and its endogenous substrates in the induction of long-term potentiation

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Fukunaga, Kohji, Muller, Dominique, Miyamoto, Eishichi·1995·Journal of Biological Chemistry

Abstract

Induction of long-term potentiation in the CA1 region of hippocampal slices is associated with increased activity of Ca2+/calmodulin-dependent protein kinase II (CaM kinase II) (Fukunaga, K., Stoppini, L., Miyamoto, E., and Muller, D. (1993) J. Biol. Chem. 268, 7863-7867). Here we report that application of high but not low frequency stimulation to two groups of afferents in the CA1 region of 32P-labeled slices resulted in the phosphorylation of two major substrates of this enzyme, synapsin I and microtubule-associated protein 2, as well as in the autophosphorylation of CaM kinase II. Furthermore, immunoblotting analysis revealed that long term potentiation induction was associated with an increase in the amount of CaM kinase II in the same region. All these changes were prevented when high frequency stimulation was applied in the presence of the N-methyl-D-aspartate receptor antagonist, D-2-amino-5-phosphonopentanoate. These results indicate that activation of CaM kinase II is involved in the induction of synaptic potentiation in both the postsynaptic and presynaptic regions.

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  • Results based on single spine stimulations contrast earlier biochemical studies that reported persistent phosphorylation of CaMKII upon more global induction of LTP.

    “It should be noted that these results based on single spine stimulations contrast earlier biochemical studies that reported persistent phosphorylation of CaMKII upon more global induction of LTP (Fukunaga et al., 1995; Barria et al., 1997; Lisman and Zhabotinsky, 2001).”

    From Barriers in the brain: resolving dendritic spine morphology and compartmentalization (2014) · cites this paper as Fukunaga et al., 1995

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Research works printed but not linked: 8

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Authors
Fukunaga, K., Muller, D., & Miyamoto, E.
Affiliations
Kumamoto University (JP)
Corresponding author
Fukunaga, Kohji
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1995-03
Volume
270
Issue
11
Pages
6119-6124
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2082683998
Cited by
226
References
0
Citations by year
2024: 5 · 2023: 2 · 2022: 3 · 2021: 5 · 2020: 3 · 2019: 4 · 2018: 8 · 2017: 8 · 2016: 5 · 2015: 6 · 2014: 9 · 2013: 8 · 2012: 5
FWCI
4.35
Type
journal article
Language
en
Open access
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
  • Archive ouverte UNIGE (University of Geneva) (submittedVersion)
Funders
  • National Research Foundation
  • Japan Society for the Promotion of Science
Topics
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
  • Life Sciences › Neuroscience › Cognitive Neuroscience › Memory and Neural Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Keywords
calcium/calmodulin-dependent protein kinase II, long-term potentiation, synapsin I, MAP2, autophosphorylation, NMDA receptor, high-frequency stimulation, hippocampal CA1, synaptic potentiation
MeSH terms
Animals, Calmodulin, Electric Stimulation, Hippocampus, Imidazoles, Kinetics, Male, Microtubule-Associated Proteins, Phosphoproteins, Phosphorus Radioisotopes, Phosphorylation, Synapses, Synapsins, Rats, Sprague-Dawley, Long-Term Potentiation, Calcium-Calmodulin-Dependent Protein Kinases, Pyramidal Cells, Macromolecular Substances, Rats, In Vitro Techniques

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