Activation of protein kinase C-?? attenuates kainate-induced cell death of cortical neurons

Jung, Yi‐Sook; Lee, Bo Kyung; Park, Hye-Seong; Shim, Jae-Kyung; Kim, Seung Up; Lee, Soo Hwan; Baik, Eun Joo; Moon, Chang-Hyun

doi:10.1097/00001756-200505120-00017

Cited by 17 publications

(15 citation statements)

References 18 publications

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“…For instance, PKCε and PKCδ interacting peptides show encouraging results in the control of ischemic phenomena at both cardiac and neuronal levels. 19,28,29,31 Modulating the PKC isoform activation/anchoring mechanism offers an interesting additional approach for developing innovative therapeutic tools in diverse physiologic and pathologic conditions. 71,72 …”

Section: Discussionmentioning

confidence: 99%

“…29 PKCε and γ inhibition are also involved in hyperalgesia, 30 while activation of PKCδ attenuates the kainate-induced cell death of cortical neurons. 31 Additionally, PKCζ inhibition may protect from excitotoxic neuronal death 32 while ethanol withdrawal hyper-responsiveness may be sensitive to selective inhibition of PKCγ. 33 Moreover, mutational approaches point out that the PKCγ gene is associated with animal models of Parkinson's disease 34 and with cerebellar ataxia in humans.…”

Section: Pkc Isoform-specific Brain Functionsmentioning

confidence: 99%

“…Calcium dependent PKC activity (A) and translocation (B) was assayed utilizing histone as substrate as described. 38 Calcium-independent PKC activity (C) and translocation (D) was assayed utilizing (Ser 25 ) PKC [19][20][21][22][23][24][25][26][27][28][29][30][31][32][33][34][35][36] as substrate as described. 41 Translocation is reported as ratio of activity in membranes and soluble fractions after treatment with PMA 160 nM for 15 min.…”

Section: Kinase Activity Shows Strain and Substrate-dependent Changesmentioning

confidence: 99%

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Protein Kinase C Signal Transduction Regulation in Physiological and Pathological Aging

Battaini

2005

Annals of the New York Academy of Sciences

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Calcium/phospholipid-regulated protein kinase C (PKC) signalling is known to be involved in cellular functions relevant to brain health and disease, including ion channel modulation, receptor regulation, neurotransmitter release, synaptic plasticity, and survival. Brain aging is characterized by altered neuronal molecular cascades and interneuronal communication in response to various stimuli. In the last few years we have provided evidence that in rodents, despite no changes in PKC isoform levels (both calcium dependent and calcium independent), the activation/translocation process of the calcium-dependent and -independent kinases and the content of the adaptor protein RACK1 (receptor for activated C kinase-1) are deficient in physiological brain aging. Moreover, human studies have shown that PKC and its adaptor protein RACK1 are also interdependent in pathological brain aging (e.g., Alzheimer's disease); in fact, calcium-dependent PKC translocation and RACK1 levels are both deficient in an area-selective manner. These data point to the notion that, in addition to a well-described lipid environment alteration, changes in protein-protein interactions may impair the mechanisms of PKC activation in aging. It is interesting to note that interventions to counteract the age-related functional loss also restore PKC activation and the adaptor protein machinery expression. A better insight into the factors controlling PKC activation may be important not only to elucidate the molecular basis of signal transmission, but also to identify new strategies to correct or even to prevent agedependent alterations in cell-to-cell communication.

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Section: Discussionmentioning

confidence: 99%

Section: Pkc Isoform-specific Brain Functionsmentioning

confidence: 99%

Section: Kinase Activity Shows Strain and Substrate-dependent Changesmentioning

confidence: 99%

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Protein Kinase C Signal Transduction Regulation in Physiological and Pathological Aging

Battaini

2005

Annals of the New York Academy of Sciences

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“…The plasma translocation of the novel isoforms of PKC was assessed by comparing immunoblots of the cytosolic-and membrane-associated fractions obtained 5 min after the MBH DMSO, OAG, OAG ϩ Rot, and Rot treatments in vivo. It is important to point out that Rot has previously been shown to inhibit PKC-␦ translocation in neuronal cells (23). MBH wedges (ϳ8 mg) were homogenized using a handheld glass homogenizer in lysis buffer A (20 mmol/l 3-(N-morpholino) propanesulfonic acid [MOPS], 2 mmol/l EDTA, 0.32 mmol/l sucrose, 30 mmol/l sodium fluoride, 10 mmol/l sodium pyrophosphate, 2 mmol/l sodium orthovanadate, 1 mmol/l phenylmethylsulfonylfluoride, 3 mmol/l benzamidine, 5 mol/l pepstatin A, and 10 mol/l leupeptin).…”

mentioning

confidence: 99%

Hypothalamic Protein Kinase C Regulates Glucose Production

et al. 2008

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OBJECTIVE-A selective rise in hypothalamic lipid metabolism and the subsequent activation of SUR1/Kir6.2 ATP-sensitive K ϩ (K ATP ) channels inhibit hepatic glucose production. The mechanisms that link the ability of hypothalamic lipid metabolism to the activation of K ATP channels remain unknown.RESEARCH DESIGN AND METHODS-To examine whether hypothalamic protein kinase C (PKC) mediates the ability of central nervous system lipids to activate K ATP channels and regulate glucose production in normal rodents, we first activated hypothalamic PKC in the absence or presence of K ATP channel inhibition. We then inhibited hypothalamic PKC in the presence of lipids. Tracer-dilution methodology in combination with the pancreatic clamp technique was used to assess the effect of hypothalamic administrations on glucose metabolism in vivo.RESULTS-We first reported that direct activation of hypothalamic PKC via direct hypothalamic delivery of PKC activator 1-oleoyl-2-acetyl-sn-glycerol (OAG) suppressed glucose production. Coadministration of hypothalamic PKC-␦ inhibitor rottlerin with OAG prevented the ability of OAG to activate PKC-␦ and lower glucose production. Furthermore, hypothalamic dominantnegative Kir6.2 expression or the delivery of the K ATP channel blocker glibenclamide abolished the glucose production-lowering effects of OAG. Finally, inhibition of hypothalamic PKC eliminated the ability of lipids to lower glucose production.CONCLUSIONS-These studies indicate that hypothalamic PKC activation is sufficient and necessary for lowering glucose production.

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“…Literature shows that PKC d has different effects on neuronal cells [36,37]. PKC d is involved in different cellular events such as growth and differentiation [38].…”

Section: Discussionmentioning

confidence: 99%

The Trophic Effect of Ouabain on Retinal Ganglion Cell is Mediated by EGF Receptor and PKC δ Activation

et al. 2010

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It was already shown that ouabain treatment can stimulate PKC isoenzymes leading to the activation of intracellular pathways involved in cell survival, growth and proliferation. We have previously demonstrated that ouabain or PMA treatment increases retinal ganglion cell survival, an effect mediated by PKC activation. The aim of this work was to investigate the role of EGF receptors in the ouabain effect and also to study which PKC isoform is activated by treatment with ouabain and PMA. Our results show that 2.5 microM tyrphostin, 1.0 microM PP1, 4.0 microM U73122, 1.0 microM JNK inhibitor V and 2.0 microM rottlerin blocked the ouabain effect indicating an involvement of receptors for EGF, Src, PLC, JNK and PKC delta respectively. The effect of PMA was only abolished when cultures were treated with rottlerin or with the JNK inhibitor suggesting the involvement of PKC delta and JNK. These results indicate that PKC delta could be a key regulator of retinal ganglion cell survival.

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Activation of protein kinase C-?? attenuates kainate-induced cell death of cortical neurons

Cited by 17 publications

References 18 publications

Protein Kinase C Signal Transduction Regulation in Physiological and Pathological Aging

Protein Kinase C Signal Transduction Regulation in Physiological and Pathological Aging

Hypothalamic Protein Kinase C Regulates Glucose Production

The Trophic Effect of Ouabain on Retinal Ganglion Cell is Mediated by EGF Receptor and PKC δ Activation

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