calmodulin/seizures

Understanding the molecular basis of altered neuronal excitability in epilepsy is a major challenge in neuroscience research. The present study suggests an inverse correlation between changes in neuronal excitability in status epilepticus and the activity of type II multifunctional

Calcium/calmodulin-dependent protein kinase type II (CamKII) is a ubiquitous brain enzyme implicated in a wide variety of neuronal processes. Understanding CamKII has become increasingly complicated with the recent identification of multiple gene transcripts coding for separate subunits. Previous

Seizure is a form of excessive neuronal excitation and seizure-induced neuronal damage has profound effects on the prognosis of epilepsy. In various seizure models, the inactivation of Ca2+/calmodulin-dependent protein kinase II (CaMKII) occurs during seizure activity preceding neuronal cell death.

We have examined the potential involvement of calcium/calmodulin-dependent protein kinases in the regulation of brain-derived neurotrophic factor mRNA in vivo following kainic acid (kainate)-induced seizure activity by in situ hybridization. KN-62, a specific inhibitor of

The effect of a brief pentylenetetrazol (PTZ) convulsive seizure on rat cerebral cortical Ca2+/calmodulin dependent protein kinase II (CaMKII) was investigated. By immunoblot, it was found that a single PTZ seizure, lasting less than a minute, caused translocation of CaMKII alpha-subunit

The ED50 value of cyanide as measured by induction of convulsions (tonic seizure) was significantly increased by 80% or 69% when trifluoperazine (TFP) or chlorpromazine (CHP), a specific calmodulin inhibitor was preinjected intracerebroventricularly (i.v.t.) at a dose of 0.09 mumol/body of mice.

Ca(2+)-calmodulin-dependent protein kinase II (CaMKII) and protein phosphatase 2B (calcineurin) play a critical role in modulation responses of nerve cells to Ca(2+)-signal. Here we asked the question, whether and how these enzymes may become affected by single seizure activity. Male epilepsy-prone

Ca2+/calmodulin-dependent protein kinase II (CaM Kinase II) activity was evaluated in a well-characterized in vitro model of epileptiform activity. Long-lasting spontaneous recurrent seizure (SRS) activity was induced in hippocampal neuronal cultures by exposure to low Mg2+ media for 3 h. Analysis

We identified a 45-kDa protein by 2D electrophoresis that was enhanced following pentylenetetrazol (PTZ)-mediated seizures. Mass-spectrography of this protein revealed the beta subunit of Ca2+/calmodulin-dependent protein kinase II (CaMKIIbeta), although no evidence for increase in bulk CaMKIIbeta

We studied levels of mRNA for the alpha- and beta-subunits of calmodulin (CaM) kinase II using the amygdaloid kindling model of epilepsy. There were significant increases in mRNA for the beta-subunit of CaM kinase II in the hippocampus 4-24 h after stage 5-kindled seizures. Moreover, this mRNA was

The anticonvulsant activity of calmodulin antagonist W-7, was investigated on convulsions induced in mice by the insecticide lindane and by the calcium channel agonist BayK-8644. We also studied the inhibitory effect of W-7 on on c-fos mRNA expression induced by both convulsants. We observed a good

The anticonvulsant activity of delta-HCH and of a calmodulin antagonist, W-7 were investigated on convulsions induced in mice by lindane (ED100 100 mg/kg), by GABAergic antagonists PTZ (ED100 60 mg/kg) and PTX(ED100 4 mg/kg), by calcium channel agonist BAY-K-8644 (ED100 5 mg/kg), by two agonists of

It was shown that increased excitability in neurons underlying epilepsies would be maintained by abnormalities in protein phosphorylation systems. This study was initiated to compare the functioning of Ca(2+)/calmodulin- and cAMP-dependent systems of protein phosphorylation in homogenates of

This study evaluated the alteration of CaMKII autophosphorylation and distribution in rat brain following a single, brief pentylenetetrazol (PTZ) seizure and during PTZ kindling. Total CaMKII alpha subunit (alpha-CaMKII) and alpha-CaMKII phosphorylated at Thr(286) were detected by immunoblot. A

Using a Western blot method it was been shown that a aontent of beta-CaMKII subunit was decreased on 40 % in hippocampus of Krushinskii-Molodkina rats (rats, genetically prone to audiogenic seizures) in comparison with normal Wistar rats. Additionally, we have investigate the temporal modifications