The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.
Glutamate-induced transient modification of the postsynaptic density
Open accessAbstract
Depolarization of rat hippocampal neurons with a high concentration of external potassium induces a thickening of postsynaptic densities (PSDs) within 1.5-3 min. After high-potassium treatment, PSDs thicken 2.1-fold in cultured neurons and 1.4-fold in hippocampal slices compared with their respective controls. Thin-section immunoelectron microscopy of hippocampal cultures indicates that at least part of the observed thickening of PSDs can be accounted for by an accumulation of Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) on their cytoplasmic faces. Indeed, PSD-associated gold label for CaMKII increases 5-fold after depolarization with potassium. The effects of high-potassium treatment on the composition and structure of the PSDs are mimicked by direct application of glutamate. In cultures, glutamate-induced thickening of PSDs and the accumulation of CaMKII on PSDs are reversed within 5 min of removal of glutamate and Ca(2+) from the extracellular medium. These results suggest that PSDs are dynamic structures whose thickness and composition are subject to rapid and transient changes during synaptic activity.
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“activation of CaMKII results in the rapid translocation of CaMKII to the PSD (137, 140, 169, 216–220).”
From Synaptic memory and CaMKII (2023) · cites this paper as [137]
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“Glutamate treatment of neuronal cultures causes CaMKII clustering at excitatory synapses (136–140).”
From Synaptic memory and CaMKII (2023) · cites this paper as [137]
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Cited by
Sorted by citations
The molecular basis of CaMKII function in synaptic and behavioural memory
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“Indeed, electron microscopic studies show that raising Ca 2+ causes a build-up of CaMKII in the PS”
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Metadata
- Authors
- Dosemeci, A., Tao-Cheng, J.-H., Vinade, L., Winters, C. A., Pozzo-Miller, L., & Reese, T. S.
- Affiliations
- Marine Biological Laboratories, Woods Hole, MA 02543; Laboratory of Neurobiology, Electron Microscopy Facility, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892; and Department of Neurobiology, University of Alabama, Birmingham, AL 35294
- National Institutes of Health (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2001-08-21
- Volume
- 98
- Issue
- 18
- Pages
- 10428-10432
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC56977
- OpenAlex
- W2131475149
- Cited by
- 184
- References
- 24
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 4 · 2023: 7 · 2022: 6 · 2021: 3 · 2020: 18 · 2019: 4 · 2018: 8 · 2017: 6 · 2016: 13 · 2015: 7 · 2014: 6 · 2013: 5 · 2012: 5
- FWCI
- 3.33
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation (9817317)
- National Institutes of Health
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Neuroscience › Cognitive Neuroscience › Memory and Neural Mechanisms
- Keywords
- postsynaptic density, glutamate, CaMKII, hippocampal neurons, depolarization, high potassium, synaptic plasticity, calcium/calmodulin-dependent protein kinase, calcium signaling
- MeSH terms
- Animals, Cells, Cultured, Hippocampus, Nerve Tissue Proteins, Neurons, Potassium, Microscopy, Immunoelectron, Calcium-Calmodulin-Dependent Protein Kinases, Glutamic Acid, Rats, Calcium-Calmodulin-Dependent Protein Kinase Type 2
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