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Different basal levels of CaMKII phosphorylated at Thr286/287 at nociceptive and low-threshold primary afferent synapses.
Department of Experimental Medical Science, Division of Neuroscience, Lund University, Lund, Sweden.ORCID iD: 0000-0003-3584-7829
Department of Experimental Medical Science, Division of Neuroscience, Lund University, Lund, Sweden.
2005 (English)In: European Journal of Neuroscience, ISSN 0953-816X, E-ISSN 1460-9568, Vol. 21, no 9, 2445-2458 p.Article in journal (Refereed) Published
Abstract [en]

Postsynaptic autophosphorylation of Ca2+/calmodulin-dependent protein kinase II (CaMKII) at Thr286/287 is crucial for the induction of long-term potentiation at many glutamatergic synapses, and has also been implicated in the persistence of synaptic potentiation. However, the availability of CaMKII phosphorylated at Thr286/287 at individual glutamatergic synapses in vivo is unclear. We used post-embedding immunogold labelling to quantitatively analyse the ultrastructural localization of CaMKII phosphorylated at Thr286/287 (pCaMKII) at synapses formed by presumed nociceptive and low-threshold mechanosensitive primary afferent nerve endings in laminae I-IV of rat spinal cord. Immunogold labelling was enriched in the postsynaptic densities of such synapses, consistent with observations in pre-embedding immunoperoxidase-stained dorsal horn. Presynaptic axoplasm also exhibited sparse immunogold labelling, in peptidergic terminals partly associated with dense core vesicles. Analysis of single or serial pCaMKII-immunolabelled sections indicated that the large majority of synapses formed either by presumed peptidergic or non-peptidergic nociceptive primary afferent terminals in laminae I-II of the spinal cord, or by presumed low-threshold mechanosensitive primary afferent terminals in laminae IIi-IV, contained pCaMKII in their postsynaptic density. However, the postsynaptic levels of pCaMKII immunolabelling at low-threshold primary afferent synapses were only approximately 50% of those at nociceptive synapses. These results suggest that constitutively autophosphorylated CaMKII in the postsynaptic density is a common characteristic of glutamatergic synapses, thus potentially contributing to maintenance of synaptic efficacy. Furthermore, pCaMKII appears to be differentially regulated between high- and low-threshold primary afferent synapses, possibly reflecting different susceptibility to synaptic plasticity between these afferent pathways.

Place, publisher, year, edition, pages
Wiley-Blackwell Publishing Inc., 2005. Vol. 21, no 9, 2445-2458 p.
National Category
Neurosciences
Identifiers
URN: urn:nbn:se:liu:diva-133056DOI: 10.1111/j.1460-9568.2005.04081.xISI: 000229284100013PubMedID: 15932602Scopus ID: 2-s2.0-20444485368OAI: oai:DiVA.org:liu-133056DiVA: diva2:1054570
Available from: 2016-12-08 Created: 2016-12-08 Last updated: 2016-12-13Bibliographically approved

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