Rapid Translocation of Cytosolic Ca<sup>2+</sup>/Calmodulin‐Dependent Protein Kinase II into Postsynaptic Density After Decapitation

Suzuki, Tatsuo; Okumura-Noji, Kuniko; Tanaka, Ryo; Tada, Toyohiro

doi:10.1046/j.1471-4159.1994.63041529.x

Cited by 113 publications

(87 citation statements)

References 25 publications

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“…Because of this, we assume that the αCaMKII in our TxP fraction represented predominantly PSD-associated kinase. The TxP fraction contained the highest relative concentration of αCaMKII, indicating that, as expected based on previous results (Kennedy et al, 1983;Petersen et al, 2003;Suzuki et al, 1994), αCaMKII is enriched at the post-synaptic density in recovered CA1-minislices from adult rats.…”

Section: Resultssupporting

confidence: 88%

“…Previous studies have demonstrated that the conditions encountered during sacrifice and hippocampal slice preparation lead to alterations in T286 phosphorylation (Lengyel et al, 2001;Ho et al, 2004), an increase in CaMKII concentration in PSD-enriched fractions (Suzuki et al, 1994), and CaMKII cluster formation (Dosemeci et al, 2000;Tao-Cheng et al, 2002). Because of this, all of the CA1-minislices used in this study were allowed to recover for at least 90 minutes following sacrifice.…”

Section: Resultsmentioning

confidence: 99%

“…The minislices were then incubated at interface in 32°C ACSF (that had been bubbled with a 95% O 2 / 5% CO 2 mix) and humidified with 95% O 2 / 5% CO 2 . Since the conditions encountered during sacrifice and minislice preparation are known to alter T286 phosphorylation (Lengyel et al, 2001;Ho et al, 2004), increase CaMKII concentration in PSD-enriched fractions (Suzuki et al, 1994), and induce CaMKII cluster formation (Dosemeci et al, 2000;Tao-Cheng et al, 2002), the minislices were recovered at interface for at least 90 minutes (Ho et al, 2004), with ACSF being replaced every 15 minutes. Similar protocols using submersion recovery techniques have been shown to restore T286 phosphorylation to what are believed to be physiological levels (Lengyel et al, 2001) and reverse the sacrifice induced clustering of the kinase .…”

Section: Ca1-minislice Preparation and Treatmentmentioning

confidence: 99%

“…Several studies have demonstrated that CaMKII is necessary for the induction of LTP (Malinow et al, 1989;Malenka et al, 1989;Silva et al, 1992;Giese et al, 1998), and that introduction of activated CaMKII is sufficient to potentiate synaptic responses in neurons (Pettit et al, 1994;Lledo et al, 1995;McGlade-McCulloh et al, 1993). CaMKII is enriched at the postsynaptic density (PSD) (Kennedy et al, 1983;Suzuki et al, 1994;Petersen et al, 2003), a protein-dense specialization at the post-synaptic membrane that is composed primarily of scaffolding proteins, ion channels, and signal transduction enzymes (Ziff, 1997). Localization of CaMKII at the PSD has been proposed to be critical for its role in LTP (Lisman et al, 2002;Barria and Malinow, 2005).…”

Section: Introductionmentioning

confidence: 99%

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αCaMKII autophosphorylation levels differ depending on subcellular localization

et al. 2007

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Calcium/calmodulin-dependent protein kinase II (CaMKII) has important roles in many processes in the central nervous system. It is enriched at the post-synaptic density (PSD), a localization which is thought to be critical for many of its proposed neuronal functions. In order to better understand the mechanisms that regulate association of CaMKII with the PSD, we compared the levels of autophosphorylation between PSD-associated kinase and kinase in other parts of the neuron. We were surprised to find that αCaMKII in a PSD-enriched fraction prepared from recovered hippocampal CA1-minislices had a relatively low level of threonine 286 (T286) phosphorylation and a relatively high level of threonine 305 (T305) phosphorylation. Furthermore, when the minislices were subjected to a treatment that mimics ischemic conditions, there was a significant translocation of αCaMKII to the PSD-enriched fraction accompanied with a dramatic reduction in T286 phosphorylation levels throughout the neuron. These findings have important implications for our understanding of the role of autophosphorylation in the localization of CaMKII.

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Section: Resultssupporting

confidence: 88%

Section: Resultsmentioning

confidence: 99%

Section: Ca1-minislice Preparation and Treatmentmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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αCaMKII autophosphorylation levels differ depending on subcellular localization

et al. 2007

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“…However, under the pathological conditions, such as cerebral ischemia, over-stimulation of the neurotransmitter receptors may cause extensive oxidation of CaMKII. Thus, a combination of oxidation with intracellular acidification under these conditions (51) could account for the severe inactivation of the kinase and accumulation of both the synaptic and non-synaptic CaMKII aggregates (11,12,40,(52)(53)(54).…”

Section: Discussionmentioning

confidence: 99%

Ischemia-elicited Oxidative Modulation of Ca2+/Calmodulin-dependent Protein Kinase II

Shetty

Huang

2008

Journal of Biological Chemistry

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Ca 2؉ /calmodulin (CaM)-dependent protein kinase II (CaMKII) plays a critical role in neuronal signal transduction and synaptic plasticity. Here, we showed that this kinase was very susceptible to oxidative modulation. Treatment of mouse brain synaptosomes with H 2 O 2 , diamide, and sodium nitroprusside caused aggregation of CaMKII through formation of disulfide and non-disulfide linkages, and partial inhibition of the kinase activity. These CaMKII aggregates were found to associate with the post synaptic density. However, treatment of purified CaMKII with these oxidants did not replicate those effects observed in the synaptosomes. Using two previously identified potential mediators of oxidants in the brain, glutathione disulfide S-monoxide (GS-DSMO) and glutathione disulfide S-dioxide (GS-DSDO), we showed that they oxidized and inhibited CaMKII in a manner partly related to those of the oxidanttreated synaptosomes as well as the ischemia-elicited oxidative stress in the acutely prepared hippocampal slices. Interestingly, the autophosphorylated and activated CaMKII was relatively refractory to GS-DSMO-and GS-DSDO-mediated aggregation. Short term ischemia (10 min) caused a depression of basal synaptic response of the hippocampal slices, and re-oxygenation (after 10 min) reversed the depression. However, oxidation of CaMKII remained at above the pre-ischemic level throughout the treatment. Oxidation of CaMKII also prevented full recovery of CaMKII autophosphorylation after re-oxygenation. Subsequently, the high frequency stimulation-mediated synaptic potentiation in the hippocampal CA1 region was significantly reduced compared with the control without ischemia. Thus, ischemia-evoked oxidation of CaMKII, probably via the action of glutathione disulfide S-oxides or their analogues, may be involved in the suppression of synaptic plasticity.Ca 2ϩ /calmodulin (CaM) 2 -dependent protein kinase II (CaMKII) is one of the major Ca 2ϩ -sensing enzymes important in transducing neuronal, hormonal, and electrical signals in brain, heart, and other tissues. In the central nervous system, CaMKII plays a pivotal role in the facilitation of synaptic plasticity, learning, and memory and in activity-dependent developmental processes (1). CaMKII holoenzyme is a dodecamer composed of two stacked hexameric rings, in which each catalytic/regulatory domain from the upper ring interacts with the equivalent catalytic/regulatory domain in the lower ring by an antiparallel coiled-coil, which resides in regulatory domains (2). Binding of Ca 2ϩ /CaM to the regulatory domain separates the dimer pair and causes the exposure of Thr-286 or Thr-287 (within ␣ or ␤ subunit) for phosphorylation by another catalytic domain in the same ring. This inter-subunit phosphorylation of Thr-286/287 converts the kinase into a high affinity binding protein for Ca 2ϩ /CaM, and the kinase becomes an activatorindependent autonomous enzyme (3). The autophosphorylation also leads to increased affinity of the kinase for several proteins near the sites of elevated Ca 2...

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Methamphetamine decreases calcium-calmodulin dependent protein kinase II activity in discrete rat brain regions

Suemaru

Akiyama

Tanabe

et al. 2000

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A Ca(2+)/calmodulin-dependent signaling cascade has been implicated in the regulation of dopaminergic neurotransmission after chronic administration of amphetamine and methamphetamine (METH). We found a decrease in Ca(2+)/calmodulin-dependent protein kinase II (CaM-kinase II) activity in five regions of the rat brain (parietal cortex; frontal cortex; hippocampus; striatum; and nucleus accumbens) after a single injection of METH. Pretreatment with the selective dopamine D1 receptor antagonist SCH 23390 prevented the acute METH-induced decrease in CaM-kinase II activity in the parietal cortex, striatum, nucleus accumbens, and substantia nigra/ventral tegmental area (SN/VTA). Pretreatment with the N-methyl-D-aspartate receptor antagonist MK-801 significantly restored the acute METH-induced decrease in CaM-kinase II activity in the parietal cortex, nucleus accumbens, and SN/VTA. Striatal CaM-kinase II activity was still significantly lower than that of the chronic saline-treated controls after a 1-week, but not a 4-week, abstinence from chronic administration of METH. A METH challenge after a 4-week abstinence period induced a more pronounced decrease in CaM-kinase II activity in rats chronically injected with METH than in rats chronically injected with saline. Western blot analysis revealed that the amount of CaM-kinase II protein was not altered after a single METH injection or after chronic METH injections, compared with saline-treated controls. However, amounts of phosphorylated (Thr(286)) CaM-kinase II in the parietal cortex, striatum and SN/VTA were significantly decreased at 3 h after an acute METH injection compared with saline-treated controls. These results suggest that dephosphorylation of CaM-kinase II may contribute to the decreased enzyme activities induced by acute METH administration, and that chronic treatment with METH leads to an enhanced capacity of METH to decrease CaM-kinase II activity after an extended withdrawal period.

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Rapid Translocation of Cytosolic Ca²⁺/Calmodulin‐Dependent Protein Kinase II into Postsynaptic Density After Decapitation

Cited by 113 publications

References 25 publications

αCaMKII autophosphorylation levels differ depending on subcellular localization

αCaMKII autophosphorylation levels differ depending on subcellular localization

Ischemia-elicited Oxidative Modulation of Ca2+/Calmodulin-dependent Protein Kinase II

Methamphetamine decreases calcium-calmodulin dependent protein kinase II activity in discrete rat brain regions

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Rapid Translocation of Cytosolic Ca2+/Calmodulin‐Dependent Protein Kinase II into Postsynaptic Density After Decapitation

Cited by 113 publications

References 25 publications

αCaMKII autophosphorylation levels differ depending on subcellular localization

αCaMKII autophosphorylation levels differ depending on subcellular localization

Ischemia-elicited Oxidative Modulation of Ca2+/Calmodulin-dependent Protein Kinase II

Methamphetamine decreases calcium-calmodulin dependent protein kinase II activity in discrete rat brain regions

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Rapid Translocation of Cytosolic Ca²⁺/Calmodulin‐Dependent Protein Kinase II into Postsynaptic Density After Decapitation