Suppression of synaptic plasticity by fullerenol in rat hippocampus in vitro

Abstract

Fullerenol, a water-soluble fullerene derivative, has attracted much attention due to its bioactive properties, including the antioxidative properties and free radical scavenging ability. Due to its superior nature, fullerenol represents a promising diagnostic, therapeutic, and protective agent. Therefore, elucidation of the possible side effects of fullerenol is important in determining its potential role. In the present study, we investigated the acute effects of 5 μM fullerenol on synaptic plasticity in hippocampal brain slices of rats. Incubation with fullerenol for 20 minutes significantly decreased the peak of paired-pulse facilitation and long-term potentiation, indicating that fullerenol suppresses the short- and long-term synaptic plasticity of region I of hippocampus. We found that fullerenol depressed the activity and the expression of nitric oxide (NO) synthase in hippocampus. In view of the important role of NO in synaptic plasticity, the inhibition of fullerenol on NO synthase may contribute to the suppression of synaptic plasticity. These findings may facilitate the evaluation of the side effects of fullerenol.

Long-term maintenance of synaptic plasticity by Fullerenol Ameliorates lead-induced-impaired learning and memory in vivo

“…A recent article has shown that fullerenols have neuroprotective activities, including promoting restoration of dopamine levels, reducing oxidative stress, preventing death of neurons and alleviating aggregation of alpha-synuclein [ 34 ]. But our previous study of fullerenol on synaptic plasticity in hippocampal brain slices of rats indicates that high-level fullerenols depress the activity and the expression of nitric oxide synthase in hippocampus [ 35 ]. The role of fullerenols in the nervous system is controversial.…”

Integrative Proteomics–Metabolomics Strategy for Pathological Mechanism of Vascular Depression Mouse Model

“…CaMKII, an enzyme primarily in the brain, belonging to the calcium-activated serine/threonine protein kinase family, is a key protein downstream of the NMDA receptor signaling pathway, and a core protein in the calcium ion signaling pathway is also involved in the synthesis and release of glutamate, the regulation of ion channels, and the regulation of synaptic retractions . Moreover, CaMKII has a long-lasting enzymatic activity for LTP regulation and is therefore considered to be a molecular switch . The presence of the Ca signaling pathway is an integral part of the normal function of synaptic maintenance in the hippocampus.…”

“…55 Moreover, CaMKII has a long-lasting enzymatic activity for LTP regulation and is therefore considered to be a molecular switch. 56 The presence of the Ca signaling pathway is an integral part of the normal function of synaptic maintenance in the hippocampus. The transfer of neurotransmitter to the postsynaptic membrane is accompanied by the influx of Ca2+ into the membrane through NMDAR, which in turn causes the activation of CaMKIIA 57 and the whole signaling pathway.…”

Effect of Hypoxic Injury in Mood Disorder

“…Some studies show that NO affects the hippocampal synaptic plasticity, including LTD and LTP, and consequently learning and memory [ 49 – 54 ]. Also, NO serves as a retrograde messenger and acts directly on the presynaptic neurons to produce LTP [ 48 , 55 – 57 ] and then suppresses the synaptic plasticity [ 58 ]. Other studies have shown that some drugs could protect the hippocampal neurons by inhibiting the NOS activity and expression in the hippocampus [ 58 – 60 ].…”

“…Also, NO serves as a retrograde messenger and acts directly on the presynaptic neurons to produce LTP [ 48 , 55 – 57 ] and then suppresses the synaptic plasticity [ 58 ]. Other studies have shown that some drugs could protect the hippocampal neurons by inhibiting the NOS activity and expression in the hippocampus [ 58 – 60 ]. The ER stress induced by chronic IH resulted in apoptosis and fine structural changes in the synapses in the hippocampal CA1 region [ 61 ], which might inhibit the transfer of Schaffer collaterals from CA3 to CA1 neurons [ 62 ].…”