Activation of the neuroprotective ERK signaling pathway by fructose-1,6-bisphosphate during hypoxia involves intracellular Ca2+ and phospholipase C

Neuroprotection by fructose-1,6-bisphosphate involves ROS alterations via p38 MAPK/ERK

“…Increased ROS levels during oxidative stress leads to cell death; thus, it is important to regulate ROS levels and protect CNS tissues from oxidative stress [25]. FBP has been shown to protect neurons against cell death following oxidative stress [13,41]. Here, we examined the neuroprotective effect of FBP against NMDA-induced cortical neuronal death in terms of ROS and the intracellular signalings, p38 MAPK, and ERK.…”

“…In organotypic slice model, FBP activated pERK expression in hippocampal neurons [13], and the author expected the survival effect of FBP were acted through ERK signaling. However, in our culture scheme with pure cortical neurons, the treatment of NMDA activated the p-ERK expression, and FBP down-regulated the p38 MAPK/ERK signaling.…”

“…The protective role of FBP has been attributed to reduction of ATP loss [3,21] or regulation of glucose metabolism [24]. In organotypic slice cultures subjected to hypoxic conditions, FBP initiated a series of neuroprotective signals including PLC activation and increased activity of the ERK signaling pathway [13,28]. FBP has also been shown to suppress superoxide (O 2À ) and H 2 O 2 production by activated neutrophils [31,35], inhibit NO-dependent GAPDH in the intestinal epithelium [34], and preserve glutathione in cortical neurons during oxidative stress [41].…”

“…The ERK1/2 can play an important role in the neuronal death caused by oxidative stress, not in oxidative-independent neuronal death [30,33,19]. The overactivation of p38MAPK/ERK can promote neuronal death and the inhibition of p38MAPK/ERK lead to cell survival [26,38], although p38MAPK/ERK activation has been reported to protect certain populations of neurons against specific insults [8,13,20].…”

Social Buffering Prevents Stress-Induced Decreases in Dendritic Length, Branching in Dentate Granule Cells and Hippocampus-Related Memory Performance

“…BDNF induction has been known to play a critical role in mediating morphological and synaptic plasticity in DG granule cells [12][13][14]. Moreover, BDNF is found to induce these morphological and synaptic changes likely via phosphorylation of local extracellular signalregulated kinases (ERK) and ERK-dependent cAMP response element binding protein (CREB) phosphorylation [15][16][17]. Thus, the present study was designed to assess whether the present stressor regimen may cause changes in local ERK and CREB expression and phosphorylation in DG.…”