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"Alternatively, the brain derived neurotrophic factor (BDNF)-induced activation of the neurotrophic receptor tyrosine kinase 2 (TrkB) can trigger the initiation of the MEK and ERK signaling pathway, also driving protein translation via multiple mechanisms including activation of mTORC1."
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"TCN-201 infusion into the prelimbic cortex inhibited the BDNF-mediated increase in pERK and pGluN2A whereas Ro-25-6981 infusion into the prelimbic cortex blocked BDNF-induced elevation of pERK and pGluN2B, indicating that both GluN2A- and GluN2B-containing NMDA receptors underlie BDNF-induced ERK activation."
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"Experimental studies have revealed that dexmedetomidine can increase BDNF expression by directly acting on the α2A receptor and then modulating the ERK1/2 pathway, and BDNF can in turn promote the expression of Bcl-2 and BCL-XL by activating the PI3K/Akt signaling pathway and MAPK pathway and thus suppressing the p38 and c-Jun N-terminal kinase (JNK) pathways, which eventually leads to a decrease in neuronal apoptosis (Bell et al., 2014; Li Z.C."
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"P021 treatment during early development prevented cognitive impairment and increased expressions of pCREB and BDNF that activated downstream various signaling cascades such as PLC and PKC, MEK and ERK and PI3K and Akt, and ameliorated synaptic protein deficit in 4-month-old 3xTg-AD mice."
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"In a remarkable model recently discovered by Park et al. [ xref ], the dopamine D1 receptor agonist or brain-derived neurotrophic factor (BDNF) activated ERK1/2, leading to inducible and reversible phosphorylation of mGluR5 at S1126 in striatal neurons as detected by a phospho- and site-specific antibody ( xref )."
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"BDNF normally activates ERK and Akt in motor neurons thus it is somewhat surprising that inhibition of spinal MEK (the kinase that activates ERK) abolishes pLTF (Hoffman and Mitchell, unpublished), whereas inhibition of spinal PI3 kinase (which leads to Akt activation) does not (Hoffman and Mitchell, unpublished)."
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"Recently, the D1 receptor agonist or brain-derived neurotrophic factor activated ERK1/2 and induced U0126-sensitive mGluR5-S1126, although not mGluR5-T1123, phosphorylation in striatal neurons, which facilitated Pin1-mGluR5 interactions and thereby potentiated mGluR5 activity in triggering NMDA receptor-mediated currents [ xref ]."
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"Differential kinetics of ERK1/2 activation has also been reported; however, a continuous exposure to BDNF over 2-6 h was required for a persistent phosphorylation of ERK1/2 for cortical neurons in culture XREF_BIBR, XREF_BIBR, while BDNF elicited a rapid and transient activation of ERK1/2 in hippocampal slices XREF_BIBR."
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"Indeed, immunoblotting analysis revealed that, similar to retrolinkin knockdown, shRNA mediated knockdown of WAVE1 impaired acute activation of ERK in neurons treated with BDNF, whereas neither prolonged activation of ERK nor the kinetics of Akt activation was affected (XREF_FIG)."
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"Accumulating evidence shows that microglia in the spinal cord plays a key role in the origin of chronic pain by releasing pro-inflammatory cytokines, such as tumor necrosis factor α (TNF-α), interleukin-1β (IL-1β), and brain-derived neurotrophic factor (BDNF).4 In astrocytes, IL-1β treatment activated ERK and released MMP-2."
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"However, the underlying mechanism seems to be complicated, as BDNF can activate multiple signaling pathways (PI3K and AKT, MEK and ERK, PLCgamma-PKC and PLCgamma-CaMKII, etc.) to regulate certain transcription factors (CREB and NF-kappaB, etc.) by inducing TrkB receptor phosphorylation [XREF_BIBR], but the exact functional mechanism needs to be revealed in the future."
| PMC
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"The canonical ERK pathway (XREF_FIG) is initiated by brain derived neurotrophic factor (BDNF) binding to a receptor tyrosine kinase (TrkB) [XREF_BIBR], which, through several intermediary molecules, recruits a guanosine exchange factor (GEF) that activates a monomeric GTP binding protein called Ras [XREF_BIBR]."
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"To verify that ERK activation relies on pTrk early endocytic trafficking, we analyzed endosomal membrane fractions prepared from BDNF-stimulated cortical neurons and found that most pERK1/2 signals were detected in the early endosomal fractions 30 min after BDNF addition and that knockdown of retrolinkin or endophilin A1 caused a decrease in pERK1/2 levels in the early but not late endosomal fractions ( xref ), indicating that both retrolinkin and endophilin A1 are required for BDNF-induced ERK activation on early endosomes."
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"Targeting BDNF receptor tropomyosin receptor kinase B (TRK-B) with siRNA knockdown substantially downregulated the activated (phosphorylated) form of serine/threonine specific protein kinase (AKT) and extracellular signal regulated kinase (ERK), classical survival and proliferation mediators."
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"In a remarkable model recently discovered by Park et al. [XREF_BIBR], the dopamine D1 receptor agonist or brain derived neurotrophic factor (BDNF) activated ERK1/2, leading to inducible and reversible phosphorylation of mGluR5 at S1126 in striatal neurons as detected by a phospho- and site specific antibody (XREF_FIG)."
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"XREF_BIBR, XREF_BIBR These findings together with our published data showing lack of BDNF mediated activation of ERK1/2 in mutant huntingtin cells (XREF_FIG and Gines et al. 3) suggest that mutant huntingtin induces neuronal cell death not only by altering p75 NTR and TrkB expression but also their downstream signaling."
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"BDNF-induced activation of ERK but not PI3K signaling pathway was interfered with the Al(malt)₃ pretreatment, resulting in the subsequent reduction of BDNF-induced phosphorylation of 4EBP1, p70S6K, and eIF4E. Reduced phospho-4EBP1 and phospho-eIF4E hindered the initiation step of translation, which may lead to a reduction in BDNF-induced Arc expression."
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"To verify that ERK activation relies on pTrk early endocytic trafficking, we analyzed endosomal membrane fractions prepared from BDNF stimulated cortical neurons and found that most pERK1/2 signals were detected in the early endosomal fractions 30 min after BDNF addition and that knockdown of retrolinkin or endophilin A1 caused a decrease in pERK1/2 levels in the early but not late endosomal fractions (XREF_FIG), indicating that both retrolinkin and endophilin A1 are required for BDNF induced ERK activation on early endosomes."
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"Taken together, the results of XREF_FIG - XREF_FIG indicate that classical BDNF activated PI3K and Akt, Mek and Erk, and calcium-calmodulin pathways are not required for BDNF 's enhancement of BMP7 induced Smad phosphorylation and suggest that CK2 activity is required for this synergistic trophic factor effect."
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"The working model of pLTF suggests that IH leads to serotonin release near phrenic motor neurons, activating 5-HT 2 receptors and increasing brain derived neurotrophic factor (BDNF) synthesis; BDNF subsequently activates its high affinity receptor, TrkB, and leads to ERK MAP kinase activation."
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"To examine if CGRP contributes to ERK1/2 activation, we incubated spinal cord slices in vitro with CGRP and found that CGRP could not activate ERK1/2 after up to 90 min of stimulation; however, parallel studies showed that ERK1/2 was activated by BDNF within 30 min of incubation in these spinal slices (Qiao et al., 2008)."
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"In contrast, the magnitude of BDNF stimulated extracellular signal regulated kinase (ERK) activation was found to be much greater than that of IGF-1-stimulated ERK, such that the difference in magnitude stimulated by BDNF in the presence and absence of IGF-1 did not reach statistical significance."
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"The extracellular signal regulated kinase (ERK) 1/2, a downstream target of BDNF, is activated by the binding of BDNF to tyrosine kinase receptor-B (Trk-B) via the Ras dependent cascade, including phosphorylation (p) of transcription factors such as cAMP response element binding protein (CREB) [XREF_BIBR]."
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"By using an in vitro maturation model, we found that neurons at DIV (day in vitro) 7, around a period when functional synapses start to form and GABAergic inhibition emerges, displayed the most dynamic activation of extracellular signal-regulated kinase 1/2 (ERK1/2) and CREB by exogenous BDNF."
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"To examine if CGRP contributes to ERK1/2 activation, we incubated spinal cord slices in vitro with CGRP and found that CGRP could not activate ERK1/2 after up to 90 min of stimulation; however, parallel studies showed that ERK1/2 was activated by BDNF within 30 min of incubation in these spinal slices ( xref )."
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"A single BDNF injection into the PFC activates the ERK signaling pathway, changes the phosphorylation of NMDA receptors in the PL by activating Src family kinases (Barry & McGinty 2017) and produces enduring inhibition through normalizing cocaine-mediated extracellular glutamate spillover in the NAcc (Berglind et al. 2009)."
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"Pretreatment of cells with a pharmacological Trk inhibitor K252a led to suppression of BDNF- or GSB-106-induced activation of Erk1/2 and Akt (Fig. xref D), thus suggesting that the pro-survival signaling evoked by GSB-106 in serum withdrawn SH-SY5Y cells requires TrkB activation."
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"Because glutamatergic neuronal activity enhances the duration of BDNF induced ERK activity in cortical cultures, we investigated whether NMDA receptor activity mediates BDNF induced suppression of cocaine seeking and elevation of ERK phosphorylation in a short access SA-reinstatement model."
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"TCN-201 infusion into the prelimbic cortex inhibited the BDNF mediated increase in pERK and pGluN2A whereas Ro-25-6981 infusion into the prelimbic cortex blocked BDNF induced elevation of pERK and pGluN2B, indicating that both GluN2A- and GluN2B containing NMDA receptors underlie BDNF induced ERK activation."
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"In order to determine whether activation of these pathways are important for BDNF protection, the activation of PI-3K and Akt or ERK pathways by BDNF was blocked pharmacologically with a PI-3K inhibitor (LY294002, 30 muM), an Akt inhibitor (TCN, 10 muM), or an ERK inhibitor (PD98059, 30 muM)."