Na^(+)/K^(+)-ATPase is a transmembrane protein that has important roles in the maintenance of electrochemical gradients across cell membranes by transporting three Na^(+)out of and two K^(+)into cells.Additionally,Na^...Na^(+)/K^(+)-ATPase is a transmembrane protein that has important roles in the maintenance of electrochemical gradients across cell membranes by transporting three Na^(+)out of and two K^(+)into cells.Additionally,Na^(+)/K^(+)-ATPase participates in Ca^(2+)-signaling transduction and neurotransmitter release by coordinating the ion concentration gradient across the cell membrane.Na^(+)/K^(+)-ATPase works synergistically with multiple ion channels in the cell membrane to form a dynamic network of ion homeostatic regulation and affects cellular communication by regulating chemical signals and the ion balance among different types of cells.Therefo re,it is not surprising that Na^(+)/K^(+)-ATPase dysfunction has emerged as a risk factor for a variety of neurological diseases.However,published studies have so far only elucidated the important roles of Na^(+)/K^(+)-ATPase dysfunction in disease development,and we are lacking detailed mechanisms to clarify how Na^(+)/K^(+)-ATPase affects cell function.Our recent studies revealed that membrane loss of Na^(+)/K^(+)-ATPase is a key mechanism in many neurological disorders,particularly stroke and Parkinson's disease.Stabilization of plasma membrane Na^(+)/K^(+)-ATPase with an antibody is a novel strategy to treat these diseases.For this reason,Na^(+)/K^(+)-ATPase acts not only as a simple ion pump but also as a sensor/regulator or cytoprotective protein,participating in signal transduction such as neuronal autophagy and apoptosis,and glial cell migration.Thus,the present review attempts to summarize the novel biological functions of Na^(+)/K^(+)-ATPase and Na^(+)/K^(+)-ATPase-related pathogenesis.The potential for novel strategies to treat Na^(+)/K^(+)-ATPase-related brain diseases will also be discussed.展开更多
The low-valence cations Na^(+)and Sr^(2+)were selected as the co-dopants to increase the vacancies concentration in the Y_(2.982)Ce_(0.018)Al_(2)Ga_(3)O_(12)phosphor.The successful incorporation of Na^(+)and Sr^(2+)wa...The low-valence cations Na^(+)and Sr^(2+)were selected as the co-dopants to increase the vacancies concentration in the Y_(2.982)Ce_(0.018)Al_(2)Ga_(3)O_(12)phosphor.The successful incorporation of Na^(+)and Sr^(2+)was confirmed by the X-Ray Difiraction(XRD)results.All the samples show 5d-4f green persistent luminescence of Ce^(3+)after 450 nm excitation.The decay curves demonstrate that the persistent luminescence is efiectively enhanced with Na+and Sr2+doping.The thermoluminescence glow curves also show not only does the trap concentration increase,but also the distribution of trap depths is broadened.In addition,the air-and H_(2)/Ar-annealing treatments were conducted on every as-made sample.The experimental results prove that the increased traps after the Na^(+)/Sr^(2+)doping are mainly attributed to the oxygen vacancies,and the traps have a continuous and broad distribution of trap depths.We hope this work could give new inspiration for designing a high-performance persistent phosphor.展开更多
基金supported by the National Natural Science Foundation of China,No.82173800 (to JB)Shenzhen Science and Technology Program,No.KQTD20200820113040070 (to JB)。
文摘Na^(+)/K^(+)-ATPase is a transmembrane protein that has important roles in the maintenance of electrochemical gradients across cell membranes by transporting three Na^(+)out of and two K^(+)into cells.Additionally,Na^(+)/K^(+)-ATPase participates in Ca^(2+)-signaling transduction and neurotransmitter release by coordinating the ion concentration gradient across the cell membrane.Na^(+)/K^(+)-ATPase works synergistically with multiple ion channels in the cell membrane to form a dynamic network of ion homeostatic regulation and affects cellular communication by regulating chemical signals and the ion balance among different types of cells.Therefo re,it is not surprising that Na^(+)/K^(+)-ATPase dysfunction has emerged as a risk factor for a variety of neurological diseases.However,published studies have so far only elucidated the important roles of Na^(+)/K^(+)-ATPase dysfunction in disease development,and we are lacking detailed mechanisms to clarify how Na^(+)/K^(+)-ATPase affects cell function.Our recent studies revealed that membrane loss of Na^(+)/K^(+)-ATPase is a key mechanism in many neurological disorders,particularly stroke and Parkinson's disease.Stabilization of plasma membrane Na^(+)/K^(+)-ATPase with an antibody is a novel strategy to treat these diseases.For this reason,Na^(+)/K^(+)-ATPase acts not only as a simple ion pump but also as a sensor/regulator or cytoprotective protein,participating in signal transduction such as neuronal autophagy and apoptosis,and glial cell migration.Thus,the present review attempts to summarize the novel biological functions of Na^(+)/K^(+)-ATPase and Na^(+)/K^(+)-ATPase-related pathogenesis.The potential for novel strategies to treat Na^(+)/K^(+)-ATPase-related brain diseases will also be discussed.
文摘The low-valence cations Na^(+)and Sr^(2+)were selected as the co-dopants to increase the vacancies concentration in the Y_(2.982)Ce_(0.018)Al_(2)Ga_(3)O_(12)phosphor.The successful incorporation of Na^(+)and Sr^(2+)was confirmed by the X-Ray Difiraction(XRD)results.All the samples show 5d-4f green persistent luminescence of Ce^(3+)after 450 nm excitation.The decay curves demonstrate that the persistent luminescence is efiectively enhanced with Na+and Sr2+doping.The thermoluminescence glow curves also show not only does the trap concentration increase,but also the distribution of trap depths is broadened.In addition,the air-and H_(2)/Ar-annealing treatments were conducted on every as-made sample.The experimental results prove that the increased traps after the Na^(+)/Sr^(2+)doping are mainly attributed to the oxygen vacancies,and the traps have a continuous and broad distribution of trap depths.We hope this work could give new inspiration for designing a high-performance persistent phosphor.
