EN
PKC is implicated in the regulation of mitochondrial membranes integrity, however its precise function is not fully understood. We have examined association of PKCβ with mitochondria isolated from ischemia-vulnerable (CA1) and ischemia-resistant (CA2-3, DG) hippocampal regions in gerbil model of transient brain ischemia. We show that ischemia-induced translocation of PKCβ to mitochondria in (CA2-3,DG) is signifi cant, rapid and stable and, may bespeak neuroprotection. Furthermore, in an in vitro organotypic hippocampal slice culture, the specifi c PKCβ inhibitor - peptide increases detrimental effect of 100 μM NMDA. Cell death measured with propidium iodide showed 96% ± 25 vs. 63% ± 9 after NMDA alone and vs. 1.5% ± 0.5 dead neurons in unchallenged slices. We have also been looking for PKCβ mtiochondrial partners using “pull-down” method and Mass Spectrometry analysis. It revealed mitochondrial proteins: creatine kinase, ANT, α, β chains of ATP synthase, complex I protein of electron transport chain and thioredoxin, which can bind directly to PKCβ. All of these proteins are connected with energy and superoxide production. Our data suggest that PKCβ translocation to mitochondria might be connected with endogenous neuroprotection in CA2-3, DG hippocampus. PKCβ acting through abovementioned mitochondrial proteins could positively infl uence the balance in ROS production during reoxygenation after transient ischemia. Supported by Polish Mitochondrial Network MitoNet.pl.