PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 30609764-10 2019 Furthermore, PC-1 also blocked glutamate-induced phosphorylation of mitogen-activated protein kinases (MAPKs) including ERK1/2 and p38, but not JNK. Glutamic Acid 31-40 mitogen-activated protein kinase 3 Mus musculus 120-126 34719643-1 2021 Glutamate differentially affects the levels extracellular signal-regulated kinase (ERK)1/2 and ERK3 and the protective effect of B355252, an aryl thiophene compound, 4-chloro-N-(naphthalen-1-ylmethyl)-5-(3-(piperazin-1-yl)phenoxy)thiophene-2-sulfonamide, is associated with suppression of ERK1/2. Glutamic Acid 0-9 mitogen-activated protein kinase 3 Mus musculus 44-90 34719643-1 2021 Glutamate differentially affects the levels extracellular signal-regulated kinase (ERK)1/2 and ERK3 and the protective effect of B355252, an aryl thiophene compound, 4-chloro-N-(naphthalen-1-ylmethyl)-5-(3-(piperazin-1-yl)phenoxy)thiophene-2-sulfonamide, is associated with suppression of ERK1/2. Glutamic Acid 0-9 mitogen-activated protein kinase 3 Mus musculus 289-295 33781778-0 2021 Dopamine and glutamate receptors control social stress-induced striatal ERK1/2 activation. Glutamic Acid 13-22 mitogen-activated protein kinase 3 Mus musculus 72-78 29122481-5 2017 Glutamate markedly increased the phosphorylation of extracellular signal regulated kinase (ERK)-1/2 and p38, which are crucial in oxidative stress-mediated neuronal cell death. Glutamic Acid 0-9 mitogen-activated protein kinase 3 Mus musculus 52-99 29790746-8 2018 Immunoblot analysis revealed that compound 4 reduced the phosphorylation of MAPKs (JNK, ERK1/2, and p38) induced by glutamate. Glutamic Acid 116-125 mitogen-activated protein kinase 3 Mus musculus 88-94 23859404-8 2013 Transfection with kinase-dead 3-phosphoinositide-dependent protein kinase 1 (PDK1-KD) reduced glutamate-induced ERK1/2 phosphorylation and H2O2 generation. Glutamic Acid 94-103 mitogen-activated protein kinase 3 Mus musculus 112-118 28888848-4 2017 Although the contribution of the ERK pathway to glutamate-induced oxytosis in HT22 cells is controversial, Western blot analysis revealed that glutamate caused down-regulation of mitogen-activated protein kinase kinase kinase (c-Raf) and a resulting decrease in the phosphorylation of c-Raf, as well as of mitogen-activated protein kinase kinase1/2 (MEK1/2) and ERK1/2, downstream components of the c-Raf/MEK/ERK pathway. Glutamic Acid 143-152 mitogen-activated protein kinase 3 Mus musculus 362-368 26539627-0 2016 Glutamate levels control HT22 murine hippocampal cell death by regulating biphasic patterns of Erk1/2 activation: role of metabolic glutamate receptor 5. Glutamic Acid 0-9 mitogen-activated protein kinase 3 Mus musculus 95-101 26539627-3 2016 Extracellular signal-regulated kinase (Erk)1/2 activation by glutamate is important for both glutamate-induced cell death and survival. Glutamic Acid 61-70 mitogen-activated protein kinase 3 Mus musculus 0-46 26539627-3 2016 Extracellular signal-regulated kinase (Erk)1/2 activation by glutamate is important for both glutamate-induced cell death and survival. Glutamic Acid 93-102 mitogen-activated protein kinase 3 Mus musculus 0-46 26539627-5 2016 Glutamate and H2O2 treatment similarly induced early (<1 h) Erk1/2 phosphorylation regardless of concentration. Glutamic Acid 0-9 mitogen-activated protein kinase 3 Mus musculus 63-69 26539627-6 2016 On the other hand, persistent Erk1/2 phosphorylation (16-24 h) was observed only in the presence of excess glutamate. Glutamic Acid 107-116 mitogen-activated protein kinase 3 Mus musculus 30-36 26539627-8 2016 Our findings suggest that glutamate concentration modulates two distinct phases of Erk1/2 activation, which can explain the glutamate concentration-dependent determination of HT22 cell fate. Glutamic Acid 26-35 mitogen-activated protein kinase 3 Mus musculus 83-89 26539627-8 2016 Our findings suggest that glutamate concentration modulates two distinct phases of Erk1/2 activation, which can explain the glutamate concentration-dependent determination of HT22 cell fate. Glutamic Acid 124-133 mitogen-activated protein kinase 3 Mus musculus 83-89 24315869-6 2014 In addition, the phosphorylation of ERK1/2 induced by glutamate insult was clearly prevented by 3, while little changed by 4. Glutamic Acid 54-63 mitogen-activated protein kinase 3 Mus musculus 36-42 23859404-10 2013 These results suggest that activation of PI3Kgamma induces ERK1/2 phosphorylation, leading to extracellular H2O2 generation via PDK1 in oxidative glutamate toxicity. Glutamic Acid 146-155 mitogen-activated protein kinase 3 Mus musculus 59-65 24004478-14 2013 Glutamate significantly upregulated the phosphorylation of extracellular signal regulated kinase Erk1/2 (pERK1/2), while decreasing Erk3. Glutamic Acid 0-9 mitogen-activated protein kinase 3 Mus musculus 97-103 24004478-15 2013 In contrast, B355252 potently attenuated the glutamate-dependent activation of Erk1/2 and robustly increased the level of ERK3 in HT-22. Glutamic Acid 45-54 mitogen-activated protein kinase 3 Mus musculus 79-85 21838783-8 2011 We also observed a transient sequestration of P-ERK1/2 in the cytoplasm upon glutamate stimulation. Glutamic Acid 77-86 mitogen-activated protein kinase 3 Mus musculus 48-54 23307752-4 2013 Further, we found glutamate treatment increased phosphorylated ERK1/2 level, but the specific necroptosis inhibitor Necrostatin-1 (Nec-1) significantly inhibited the phosphorylation of ERK1 (P44) at 5, 10, and 15 min after glutamate treatment; the phosphorylation of ERK2 (P42) level was also markedly reduced by Nec-1 at 10 min after glutamate treatment. Glutamic Acid 18-27 mitogen-activated protein kinase 3 Mus musculus 63-69 23307752-4 2013 Further, we found glutamate treatment increased phosphorylated ERK1/2 level, but the specific necroptosis inhibitor Necrostatin-1 (Nec-1) significantly inhibited the phosphorylation of ERK1 (P44) at 5, 10, and 15 min after glutamate treatment; the phosphorylation of ERK2 (P42) level was also markedly reduced by Nec-1 at 10 min after glutamate treatment. Glutamic Acid 18-27 mitogen-activated protein kinase 3 Mus musculus 63-67 23307752-4 2013 Further, we found glutamate treatment increased phosphorylated ERK1/2 level, but the specific necroptosis inhibitor Necrostatin-1 (Nec-1) significantly inhibited the phosphorylation of ERK1 (P44) at 5, 10, and 15 min after glutamate treatment; the phosphorylation of ERK2 (P42) level was also markedly reduced by Nec-1 at 10 min after glutamate treatment. Glutamic Acid 18-27 mitogen-activated protein kinase 3 Mus musculus 191-194 23307752-4 2013 Further, we found glutamate treatment increased phosphorylated ERK1/2 level, but the specific necroptosis inhibitor Necrostatin-1 (Nec-1) significantly inhibited the phosphorylation of ERK1 (P44) at 5, 10, and 15 min after glutamate treatment; the phosphorylation of ERK2 (P42) level was also markedly reduced by Nec-1 at 10 min after glutamate treatment. Glutamic Acid 223-232 mitogen-activated protein kinase 3 Mus musculus 191-194 23307752-4 2013 Further, we found glutamate treatment increased phosphorylated ERK1/2 level, but the specific necroptosis inhibitor Necrostatin-1 (Nec-1) significantly inhibited the phosphorylation of ERK1 (P44) at 5, 10, and 15 min after glutamate treatment; the phosphorylation of ERK2 (P42) level was also markedly reduced by Nec-1 at 10 min after glutamate treatment. Glutamic Acid 223-232 mitogen-activated protein kinase 3 Mus musculus 191-194 21463649-2 2012 It also abolishes glutamate-mediated, Ca(2+)-dependent ERK(1/2) phosphorylation in the astrocytes. Glutamic Acid 18-27 mitogen-activated protein kinase 3 Mus musculus 55-62 19665009-5 2009 Activation of ERK1/2, a hallmark of glutamate-induced cytotoxicity, was also decreased by autophagy inhibition. Glutamic Acid 36-45 mitogen-activated protein kinase 3 Mus musculus 14-20 21320410-8 2011 Enhanced GluK2 editing by fluoxetine abolished glutamate-mediated increases in intra cellular Ca(2+) and ERK(1/2) phosphorylation. Glutamic Acid 47-56 mitogen-activated protein kinase 3 Mus musculus 105-112 20816674-8 2010 These results suggest that glutamate triggers the Nox-dependent generation of extracellular H2O2 via ERK1/2 activation, which contributes to oxidative glutamate toxicity. Glutamic Acid 27-36 mitogen-activated protein kinase 3 Mus musculus 101-107 20816674-8 2010 These results suggest that glutamate triggers the Nox-dependent generation of extracellular H2O2 via ERK1/2 activation, which contributes to oxidative glutamate toxicity. Glutamic Acid 151-160 mitogen-activated protein kinase 3 Mus musculus 101-107 17050165-2 2006 HT22 cells resistant to glutamate displayed increased phosphorylation of cAMP-response-element binding (CREB) and decreased ERK1/2 suggestive of differences in signal transmission. Glutamic Acid 24-33 mitogen-activated protein kinase 3 Mus musculus 124-130 18080754-1 2008 We previously showed that cultured mouse cerebellar granule cells during incubation in glutamine-replete medium respond to 45 mM [K(+)](e) after 20 and 60 min incubation with extracellular-signal regulated kinase 1 and 2 (ERK(1/2)) phosphorylation which is mainly, but probably not exclusively, secondary to glutamate release and transactivation of epidermal growth factor (EGF) receptors. Glutamic Acid 308-317 mitogen-activated protein kinase 3 Mus musculus 175-220 18080754-3 2008 Addition of 50 microM glutamate to the cells caused ERK(1/2) phosphorylation already after 5 min most of which was sensitive to PKC inhibition although a minor part was PKC inhibition-resistant. Glutamic Acid 22-31 mitogen-activated protein kinase 3 Mus musculus 52-59 17544586-2 2007 This effect can be mimicked by 5 min of exposure to 50 microM glutamate, suggesting that ERK1/2 phosphorylation in response to the depolarization is brought about by the resulting glutamate release. Glutamic Acid 62-71 mitogen-activated protein kinase 3 Mus musculus 89-95 17544586-2 2007 This effect can be mimicked by 5 min of exposure to 50 microM glutamate, suggesting that ERK1/2 phosphorylation in response to the depolarization is brought about by the resulting glutamate release. Glutamic Acid 180-189 mitogen-activated protein kinase 3 Mus musculus 89-95 19446794-2 2009 In the striatum, ERK1/2 kinases are co-activated by glutamate and dopamine D1/5 receptors, but the mechanisms providing such signaling integration are still unknown. Glutamic Acid 52-61 mitogen-activated protein kinase 3 Mus musculus 17-23 19446794-6 2009 RESULTS: Phosphorylation of ERK1/2 in response to glutamate, dopamine D1 agonist, or both stimuli simultaneously is impaired in Ras-GRF1-deficient striatal cells and organotypic slices of the striatonigral MSN compartment. Glutamic Acid 50-59 mitogen-activated protein kinase 3 Mus musculus 28-34 15579467-3 2005 We have demonstrated previously that this glutamate-induced oxidative toxicity requires activation of the mitogen-activated protein kinase member ERK1/2, but the mechanisms by which this activation takes place in oxidatively stressed neurons are still not fully known. Glutamic Acid 42-51 mitogen-activated protein kinase 3 Mus musculus 146-152 16537649-3 2006 We suggest that, during glutamate-induced oxidative stress, protein kinase C (PKC) delta becomes activated and induces sustained activation of extracellular signal-regulated kinase 1/2 (ERK1/2) through a mechanism that involves degradation of MKP-1. Glutamic Acid 24-33 mitogen-activated protein kinase 3 Mus musculus 143-184 16537649-3 2006 We suggest that, during glutamate-induced oxidative stress, protein kinase C (PKC) delta becomes activated and induces sustained activation of extracellular signal-regulated kinase 1/2 (ERK1/2) through a mechanism that involves degradation of MKP-1. Glutamic Acid 24-33 mitogen-activated protein kinase 3 Mus musculus 186-192 16537649-4 2006 Glutamate-induced activation of ERK1/2 was blocked by inhibition of PKCdelta, confirming that ERK1/2 is regulated by PKCdelta. Glutamic Acid 0-9 mitogen-activated protein kinase 3 Mus musculus 32-38 16537649-4 2006 Glutamate-induced activation of ERK1/2 was blocked by inhibition of PKCdelta, confirming that ERK1/2 is regulated by PKCdelta. Glutamic Acid 0-9 mitogen-activated protein kinase 3 Mus musculus 94-100 16537649-5 2006 Prolonged exposure to glutamate caused reduction in the protein level of MKP-1, which correlated with the sustained activation of ERK1/2. Glutamic Acid 22-31 mitogen-activated protein kinase 3 Mus musculus 130-136 16537649-9 2006 Taken together, these results demonstrate that activation of PKCdelta triggers degradation of MKP-1 through the ubiquitin-proteasome pathway, thereby contributing to persistent activation of ERK1/2 under glutamate-induced oxidative toxicity. Glutamic Acid 204-213 mitogen-activated protein kinase 3 Mus musculus 191-197 16621802-2 2006 Previous results with pharmacological agents implicated the extracellular signal-regulated kinases-1/2 (ERK1/2) in glutamate toxicity in HT22 cells and immature embryonic rat cortical neurons. Glutamic Acid 115-124 mitogen-activated protein kinase 3 Mus musculus 60-102 16621802-2 2006 Previous results with pharmacological agents implicated the extracellular signal-regulated kinases-1/2 (ERK1/2) in glutamate toxicity in HT22 cells and immature embryonic rat cortical neurons. Glutamic Acid 115-124 mitogen-activated protein kinase 3 Mus musculus 104-110 16621802-3 2006 In this report, we definitively establish a role for ERK1/2 in oxidative toxicity using dominant negative MEK1 expression in transiently transfected HT22 cells to block glutamate-induced cell death. Glutamic Acid 169-178 mitogen-activated protein kinase 3 Mus musculus 53-59 16621802-5 2006 Activation of ERK1/2 in HT22 cells has a distinct kinetic profile with an initial peak occurring between 30 min and 1 h of glutamate treatment and a second peak typically emerging after 6 h. We demonstrate here that the initial phase of ERK1/2 induction is because of activation of metabotropic glutamate receptor type I (mGluRI). Glutamic Acid 123-132 mitogen-activated protein kinase 3 Mus musculus 14-20 16621802-5 2006 Activation of ERK1/2 in HT22 cells has a distinct kinetic profile with an initial peak occurring between 30 min and 1 h of glutamate treatment and a second peak typically emerging after 6 h. We demonstrate here that the initial phase of ERK1/2 induction is because of activation of metabotropic glutamate receptor type I (mGluRI). Glutamic Acid 123-132 mitogen-activated protein kinase 3 Mus musculus 237-243 16621802-6 2006 ERK1/2 activation by mGluRI contributes to an HT22 cell adaptive response to oxidative stress as glutamate-induced toxicity is enhanced upon pharmacological inhibition of mGluRI. Glutamic Acid 97-106 mitogen-activated protein kinase 3 Mus musculus 0-6 16621802-7 2006 The protective effect of ERK1/2 activation at early times after glutamate treatment is mediated by a restoration of glutathione (GSH) levels that are reduced because of depletion of intracellular cysteine pools. Glutamic Acid 64-73 mitogen-activated protein kinase 3 Mus musculus 25-31 16621802-8 2006 Thus, ERK1/2 appears to play dual roles in HT22 cells acting as part of a cellular adaptive response during the initial phases of glutamate-induced oxidative stress and contributing to toxicity during later stages of stress. Glutamic Acid 130-139 mitogen-activated protein kinase 3 Mus musculus 6-12 11726647-4 2002 Furthermore, activated ERK-1/2 is retained within the nucleus in glutamate- and MG132-treated HT22 cells. Glutamic Acid 65-74 mitogen-activated protein kinase 3 Mus musculus 23-30 11726647-5 2002 Although previous studies suggested that ERK-1/2 activation was downstream of many cell death-inducing signals in HT22 cells, we show here that cycloheximide, the Z-vad caspase inhibitor, and a nonlethal heat shock protect against glutamate- and MG132-induced toxicity without diminishing ERK-1/2 activation. Glutamic Acid 231-240 mitogen-activated protein kinase 3 Mus musculus 41-48