This work reported the lanthanide ion(Gd^(3+))doped tungsten trioxide(Gd-WO_(3))nanocrystal for remarkable promoted photocatalytic degradation of organic pollutants and simultaneous in-situ H_(2)O_(2)production.With d...This work reported the lanthanide ion(Gd^(3+))doped tungsten trioxide(Gd-WO_(3))nanocrystal for remarkable promoted photocatalytic degradation of organic pollutants and simultaneous in-situ H_(2)O_(2)production.With doped lanthanide ion(Gd^(3+)),Gd-WO_(3)showed a much broad and enhanced solar light absorption,which not only promoted the photocatalytic degradation efficiency of organic compounds,but also provided a suitable bandgap for direct reduction of oxygen to H_(2)O_(2).Additionally,the isolated Gd^(3+)on WO_(3)surface can efficiently weaken the*OOH binding energy,increasing the activity and selectivity of direct reduction of oxygen to H_(2)O_(2),with a rate of 0.58 mmol L^(-1)g^(-1)h^(-1).The in-situ generated H_(2)O_(2)can be subsequently converted to·OH based on Fenton reaction,further contributed to the overall removal of organic pollutants.Our results demonstrate a cascade photocatalytic oxidation-Fenton reaction which can efficiently utilize photo-generated electrons and holes for organic pollutants treatment.展开更多
Accumulating evidence indicates that the synaptic activation of N-methyl-o-aspartate receptors （NMDARs） has a neuroprotective effect on neurons. Our previous study demonstrated that APPL1 （adaptor protein containin...Accumulating evidence indicates that the synaptic activation of N-methyl-o-aspartate receptors （NMDARs） has a neuroprotective effect on neurons. Our previous study demonstrated that APPL1 （adaptor protein containing pleckstrin homology domain, phosphotyrosine- binding domain, and leucine zipper motif） mediates the synaptic activity-dependent activation of PI3K-Akt signaling via coupling this pathway with NMDAR-PSD95 （postsynaptic density protein 95） complexes. However, the molecular mechanism underlying this process is still unknown. In the present study, we investigated the inter- action of APPL1 with PSD95 using co-immunocyto- chemical staining and western blotting. We found that the PDZ2 domain of PSD95 is a binding partner of APPL1. Furthermore, we identified serine 707 of APPL1, a pre- dicted phosphorylation site within the PDZ-binding motif at the C-terminus, as critical for the binding of APPL1 to PSD95, as well as for activation of the Akt signaling pathway during synaptic activity. This suggests that serine 707 of APPL1 is a potential phosphorylation site and may be involved in regulating the neuroprotective Akt signaling pathway that depends on synaptic NMDAR activity.展开更多
Local signaling events at synapses or axon terminals are communicated to the nucleus to elicit transcriptional responses,and thereby translate information about the external environment into internal neuronal represen...Local signaling events at synapses or axon terminals are communicated to the nucleus to elicit transcriptional responses,and thereby translate information about the external environment into internal neuronal representations.This retrograde signaling is critical to dendritic growth,synapse development,and neuronal plasticity.Here,we demonstrate that neuronal activity induces retrograde translocation and nuclear accumulation of endosomal adaptor APPL1.Disrupting the interaction of APPL1 with Importin ocl abolishes nuclear accumulation of APPL1,which in turn decreases the levels of histone acetylation.We further demonstrate that retrograde translocation of APPL1 is required for the regulation of gene transcription and then maintenance of hippocampal late-phase long-term potentiation.Thus,these results illustrate an APPLl-mediated pathway that contributes to the modulation of synaptic plasticity via coupling neuronal activity with chromatin remodeling.展开更多
基金supported by Natural Science Foundation of Zhejiang Province(No.LR21B07002)National Natural Science Foundation of China(Nos.22176170,21976152)the Open Research Program of Key Laboratory of 3D Micro/Nano Fabrication and Characterization of Zhejiang Province,Westlake University。
文摘This work reported the lanthanide ion(Gd^(3+))doped tungsten trioxide(Gd-WO_(3))nanocrystal for remarkable promoted photocatalytic degradation of organic pollutants and simultaneous in-situ H_(2)O_(2)production.With doped lanthanide ion(Gd^(3+)),Gd-WO_(3)showed a much broad and enhanced solar light absorption,which not only promoted the photocatalytic degradation efficiency of organic compounds,but also provided a suitable bandgap for direct reduction of oxygen to H_(2)O_(2).Additionally,the isolated Gd^(3+)on WO_(3)surface can efficiently weaken the*OOH binding energy,increasing the activity and selectivity of direct reduction of oxygen to H_(2)O_(2),with a rate of 0.58 mmol L^(-1)g^(-1)h^(-1).The in-situ generated H_(2)O_(2)can be subsequently converted to·OH based on Fenton reaction,further contributed to the overall removal of organic pollutants.Our results demonstrate a cascade photocatalytic oxidation-Fenton reaction which can efficiently utilize photo-generated electrons and holes for organic pollutants treatment.
基金supported by grants from the National Natural Science Foundation of China(91232303,81221003,and 81561168)
文摘Accumulating evidence indicates that the synaptic activation of N-methyl-o-aspartate receptors （NMDARs） has a neuroprotective effect on neurons. Our previous study demonstrated that APPL1 （adaptor protein containing pleckstrin homology domain, phosphotyrosine- binding domain, and leucine zipper motif） mediates the synaptic activity-dependent activation of PI3K-Akt signaling via coupling this pathway with NMDAR-PSD95 （postsynaptic density protein 95） complexes. However, the molecular mechanism underlying this process is still unknown. In the present study, we investigated the inter- action of APPL1 with PSD95 using co-immunocyto- chemical staining and western blotting. We found that the PDZ2 domain of PSD95 is a binding partner of APPL1. Furthermore, we identified serine 707 of APPL1, a pre- dicted phosphorylation site within the PDZ-binding motif at the C-terminus, as critical for the binding of APPL1 to PSD95, as well as for activation of the Akt signaling pathway during synaptic activity. This suggests that serine 707 of APPL1 is a potential phosphorylation site and may be involved in regulating the neuroprotective Akt signaling pathway that depends on synaptic NMDAR activity.
基金This work was supported by the National Natural Science Foundation of China(81671049 and 91732102 to S.Q.31900722 to Y.W.)+4 种基金Natural Science Foundation of Zhejiang Province for Distinguished Young Scholars(LR16C090001 to S.Q.)Non-profit Central Research Institute Fund of Chinese Academy of Medical Sciences(2018PT31041)Fundamental Research Funds for the Central Universities of China(2019XZZX001-01-1A to S.Q.)the Chinese Ministry of Education Project 111 Program(B13026 to S.Q.)Key Realm R&D Program of Guangdong Province(2019B030335001).
文摘Local signaling events at synapses or axon terminals are communicated to the nucleus to elicit transcriptional responses,and thereby translate information about the external environment into internal neuronal representations.This retrograde signaling is critical to dendritic growth,synapse development,and neuronal plasticity.Here,we demonstrate that neuronal activity induces retrograde translocation and nuclear accumulation of endosomal adaptor APPL1.Disrupting the interaction of APPL1 with Importin ocl abolishes nuclear accumulation of APPL1,which in turn decreases the levels of histone acetylation.We further demonstrate that retrograde translocation of APPL1 is required for the regulation of gene transcription and then maintenance of hippocampal late-phase long-term potentiation.Thus,these results illustrate an APPLl-mediated pathway that contributes to the modulation of synaptic plasticity via coupling neuronal activity with chromatin remodeling.
