Activity of Ca<sup>2+</sup>/Calmodulin‐Dependent Protein Kinase II Following Ischemia: A Comparison Between CA1 and Dentate Gyrus in a Hippocampal Slice Model

Westgate, S. A.; Brown, Jerry R.; Aronowski, Jaroslaw; Waxham, M. Neal

doi:10.1046/j.1471-4159.1994.63062217.x

Cited by 25 publications

(7 citation statements)

References 36 publications

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“…CamKII protein and activity levels are decreased after episodes of cerebral ischemia (Churn et al, 1990;Onodera et al, 1990;Morioka et al, 1992;Yamamoto et al, 1992). These alterations are more persistent in regions that are selectively vulnerable to ischemic cell death (Westgate et al, 1994;Hu and Wieloch, 1995). Also, decreases in CamKII occur after the onset of seizure activity in a variety of animal models (Goldenring et al, 1986;Murray et al, 1995).…”

Section: Discussionmentioning

confidence: 99%

Altered mRNA expression for brain-derived neurotrophic factor and type II calcium/Calmodulin-dependent protein kinase in the hippocampus of patients with intractable temporal lobe epilepsy

et al. 2000

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Section: Discussionmentioning

confidence: 99%

Altered mRNA expression for brain-derived neurotrophic factor and type II calcium/Calmodulin-dependent protein kinase in the hippocampus of patients with intractable temporal lobe epilepsy

et al. 2000

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“…Protein levels and activity of CaMKII were observed to be re-distributed between cytosolic and membrane fractions in hippocampal tissues, and also showed overall decreases following global ischemic injury (Aronowski et al, 1992;Kolb et al, 1995;Shackelford et al, 1995). Studies also showed that time-dependent loss of synaptic responses was more intense in CA1 pyramidal cells than granule cells in hypoxia-induced hippocampal slices, and these changes were positively correlated with the levels of CaMKII activity (Westgate et al, 1994). Investigations using CaMKII subunit-deficient mouse further showed that brain tissues with loss of CaMKII activity become more susceptible to the infarction following ischemia (Murray et al, 1995).…”

Section: Introductionmentioning

confidence: 95%

Calcium-independent CaMKII activity is involved in ginsenoside Rb1-mediated neuronal recovery after hypoxic damage

Park¹,

Namgung²,

Lee³

et al. 2005

Life Sciences

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“…To induce ischemic stress, slices were incubated in a modified ACSF containing 10 mM sucrose (to replace glucose) previously saturated with 95% N 2 /5% CO 2 based on the established hippocampal slice model of ischemia (38). At timed intervals samples (4 -8 slices) were removed from the medium and immediately homogenized in 400 l of Buffer A plus 10 mM iodoacetamide.…”

Section: Preparation Of Mouse Hippocampal Slices and Induction Ofmentioning

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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Activity of Ca²⁺/Calmodulin‐Dependent Protein Kinase II Following Ischemia: A Comparison Between CA1 and Dentate Gyrus in a Hippocampal Slice Model

Cited by 25 publications

References 36 publications

Altered mRNA expression for brain-derived neurotrophic factor and type II calcium/Calmodulin-dependent protein kinase in the hippocampus of patients with intractable temporal lobe epilepsy

Altered mRNA expression for brain-derived neurotrophic factor and type II calcium/Calmodulin-dependent protein kinase in the hippocampus of patients with intractable temporal lobe epilepsy

Calcium-independent CaMKII activity is involved in ginsenoside Rb1-mediated neuronal recovery after hypoxic damage

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

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Activity of Ca2+/Calmodulin‐Dependent Protein Kinase II Following Ischemia: A Comparison Between CA1 and Dentate Gyrus in a Hippocampal Slice Model

Cited by 25 publications

References 36 publications

Altered mRNA expression for brain-derived neurotrophic factor and type II calcium/Calmodulin-dependent protein kinase in the hippocampus of patients with intractable temporal lobe epilepsy

Altered mRNA expression for brain-derived neurotrophic factor and type II calcium/Calmodulin-dependent protein kinase in the hippocampus of patients with intractable temporal lobe epilepsy

Calcium-independent CaMKII activity is involved in ginsenoside Rb1-mediated neuronal recovery after hypoxic damage

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

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Activity of Ca²⁺/Calmodulin‐Dependent Protein Kinase II Following Ischemia: A Comparison Between CA1 and Dentate Gyrus in a Hippocampal Slice Model