The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
Long-term potentiation is associated with an increased activity of Ca2+/calmodulin-dependent protein kinase II.
Open accessAbstract
Among the molecular mechanisms that have been proposed to contribute to long-term potentiation in hippocampus are the activation and autophosphorylation of Ca2+/calmodulin-dependent protein kinase II (CaM kinase II). Here we report that high, but not low frequency stimulation applied to two groups of CA1 afferents resulted in a long lasting increase in the Ca(2+)-independent and total activities of the enzyme as well as an increase in the ratio of Ca(2+)-independent to total activity. The effect was obtained using two different CaM kinase II substrates, it was observed in hippocampal slices and in hippocampal organotypic cultures, and it could be blocked by preincubation of slices with the N-methyl-D-aspartate receptor antagonist D-2-amino-5-phosphonopentanoate. Treatment of slices with calyculin A, a phosphatase inhibitor, modified the activity of the enzyme, but long term potentiation could still be induced and a further increase in Ca(2+)-independent CaM kinase II activity still observed.
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Deficient Hippocampal Long-Term Potentiation in α-Calcium-Calmodulin Kinase II Mutant Mice
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Inhibition of Postsynaptic PKC or CaMKII Blocks Induction But Not Expression of LTP
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An essential role for postsynaptic calmodulin and protein kinase activity in long-term potentiation
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The molecular basis of CaMKII function in synaptic and behavioural memory
Lisman, J., Schulman, H., & Cline, H. (2002) · Nature Reviews Neuroscience · doi:10.1038/nrn753 · Cited by 1,860
Autophosphorylation at Thr 286 of the α Calcium-Calmodulin Kinase II in LTP and Learning
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Regulatory phosphorylation of AMPA-type glutamate receptors by CaM-KII during long-term potentiation
Barria, A., Muller, D., Derkach, V., Griffith, L. C., & Soderling, T. R. (1997) · Science · doi:10.1126/science.276.5321.2042 · Cited by 1,049
Self-citationThe cell biology of synaptic plasticity: AMPA receptor trafficking
Shepherd, J. D., & Huganir, R. L. (2007) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.23.090506.123516 · Cited by 978
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Metadata
- Authors
- Fukunaga, K., Stoppini, L., Miyamoto, E., & Muller, D.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1993-04
- Volume
- 268
- Issue
- 11
- Pages
- 7863-7867
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1538865085
- Cited by
- 398
- References
- 29
- FWCI
- 7.23
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Fukunaga, K., Stoppini, L., Miyamoto, E., & Muller, D. (1993). Long-term potentiation is associated with an increased activity of Ca2+/calmodulin-dependent protein kinase II. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)53037-4
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
