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Tau protein function: The mechanical exploration of axonal transport disorder caused by persistent pressure in dorsal root ganglia
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Zeitschriftentitel: | Molecular Genetics & Genomic Medicine |
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In: | Molecular Genetics & Genomic Medicine, 7, 2019, 4 |
Format: | E-Article |
Sprache: | Englisch |
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Wiley
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author_facet |
Zhang, Lei Fu, Jun Cheng, Xin‐Hua Tang, Li Zhang, Lei Fu, Jun Cheng, Xin‐Hua Tang, Li |
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author |
Zhang, Lei Fu, Jun Cheng, Xin‐Hua Tang, Li |
spellingShingle |
Zhang, Lei Fu, Jun Cheng, Xin‐Hua Tang, Li Molecular Genetics & Genomic Medicine Tau protein function: The mechanical exploration of axonal transport disorder caused by persistent pressure in dorsal root ganglia Genetics (clinical) Genetics Molecular Biology |
author_sort |
zhang, lei |
spelling |
Zhang, Lei Fu, Jun Cheng, Xin‐Hua Tang, Li 2324-9269 2324-9269 Wiley Genetics (clinical) Genetics Molecular Biology http://dx.doi.org/10.1002/mgg3.580 <jats:title>Abstract</jats:title><jats:sec><jats:title>Objective</jats:title><jats:p>We analyzed the function of Tau protein to explore the underlying mechanism of axonal transport disorder caused by persistent pressure in the dorsal root ganglia (<jats:styled-content style="fixed-case">DRG</jats:styled-content>).</jats:p></jats:sec><jats:sec><jats:title>Methods</jats:title><jats:p>Wistar rats were divided into the sham operated group, the control group and the experimental group. The Wistar rat model of continuous compression of <jats:styled-content style="fixed-case">DRG</jats:styled-content> was used for further investigation. <jats:styled-content style="fixed-case">DRG</jats:styled-content> neurons were extracted and cultured, and the protein content was detected using bicinchoninic acid method. Western blotting and immunofluorescence assays were performed to detect the protein content. Intraperitoneal injection of lithium chloride was performed for interaction with Tau. The results were then analyzed statistically.</jats:p></jats:sec><jats:sec><jats:title>Results</jats:title><jats:p>After 2 weeks of sustained pressure, the expression level of Tau<jats:sub>396</jats:sub> increased by 33%, while Tau<jats:sub>404</jats:sub> increased by 25% in the <jats:styled-content style="fixed-case">DRG</jats:styled-content> of the experimental group (<jats:italic>p</jats:italic> < 0.05). The expression level of <jats:styled-content style="fixed-case">PSD</jats:styled-content>‐95 in the <jats:styled-content style="fixed-case">DRG</jats:styled-content> decreased by 15% (<jats:italic>p</jats:italic> < 0.05), while the expression of <jats:styled-content style="fixed-case">vG</jats:styled-content>luT1, <jats:styled-content style="fixed-case">vG</jats:styled-content>luT3 and <jats:styled-content style="fixed-case">vA</jats:styled-content>chT decreased significantly in the <jats:styled-content style="fixed-case">DRG</jats:styled-content> of the experimental group (<jats:italic>p</jats:italic> < 0.05). There was no significant difference in the expression of <jats:styled-content style="fixed-case">vG</jats:styled-content>luT2 and <jats:styled-content style="fixed-case">vGAT</jats:styled-content> among the three groups (<jats:italic>p</jats:italic> > 0.05). After intervention with lithium chloride, the expression of phosphorylated Tau at the above sites decreased in varying degrees compared with the model group. The expression level of Tau<jats:sub>404</jats:sub> was reduced by 55%, and that of Tau<jats:sub>199</jats:sub> by 60% in the <jats:styled-content style="fixed-case">DRG</jats:styled-content> of the experimental group.</jats:p></jats:sec><jats:sec><jats:title>Conclusion</jats:title><jats:p>Chronic compression of <jats:styled-content style="fixed-case">DRG</jats:styled-content> and hypoxia caused phosphorylation of Tau in axons and inhibition of <jats:styled-content style="fixed-case">PSD</jats:styled-content>‐95, and the function of the synaptic glutamic acid vesicle is defective in the synapse. This process is crucial in the development and progression of axonal transport dysfunction induced by chronic <jats:styled-content style="fixed-case">DRG</jats:styled-content> compression, and phosphorylation of Tau plays a substantial role in this process.</jats:p></jats:sec> Tau protein function: The mechanical exploration of axonal transport disorder caused by persistent pressure in dorsal root ganglia Molecular Genetics & Genomic Medicine |
doi_str_mv |
10.1002/mgg3.580 |
facet_avail |
Online Free |
finc_class_facet |
Biologie |
format |
ElectronicArticle |
fullrecord |
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id |
ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTAwMi9tZ2czLjU4MA |
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DE-Gla1 DE-Zi4 DE-15 DE-Pl11 DE-Rs1 DE-105 DE-14 DE-Ch1 DE-L229 DE-D275 DE-Bn3 DE-Brt1 DE-Zwi2 DE-D161 |
imprint |
Wiley, 2019 |
imprint_str_mv |
Wiley, 2019 |
issn |
2324-9269 |
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2324-9269 |
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English |
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Wiley (CrossRef) |
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zhang2019tauproteinfunctionthemechanicalexplorationofaxonaltransportdisordercausedbypersistentpressureindorsalrootganglia |
publishDateSort |
2019 |
publisher |
Wiley |
recordtype |
ai |
record_format |
ai |
series |
Molecular Genetics & Genomic Medicine |
source_id |
49 |
title |
Tau protein function: The mechanical exploration of axonal transport disorder caused by persistent pressure in dorsal root ganglia |
title_unstemmed |
Tau protein function: The mechanical exploration of axonal transport disorder caused by persistent pressure in dorsal root ganglia |
title_full |
Tau protein function: The mechanical exploration of axonal transport disorder caused by persistent pressure in dorsal root ganglia |
title_fullStr |
Tau protein function: The mechanical exploration of axonal transport disorder caused by persistent pressure in dorsal root ganglia |
title_full_unstemmed |
Tau protein function: The mechanical exploration of axonal transport disorder caused by persistent pressure in dorsal root ganglia |
title_short |
Tau protein function: The mechanical exploration of axonal transport disorder caused by persistent pressure in dorsal root ganglia |
title_sort |
tau protein function: the mechanical exploration of axonal transport disorder caused by persistent pressure in dorsal root ganglia |
topic |
Genetics (clinical) Genetics Molecular Biology |
url |
http://dx.doi.org/10.1002/mgg3.580 |
publishDate |
2019 |
physical |
|
description |
<jats:title>Abstract</jats:title><jats:sec><jats:title>Objective</jats:title><jats:p>We analyzed the function of Tau protein to explore the underlying mechanism of axonal transport disorder caused by persistent pressure in the dorsal root ganglia (<jats:styled-content style="fixed-case">DRG</jats:styled-content>).</jats:p></jats:sec><jats:sec><jats:title>Methods</jats:title><jats:p>Wistar rats were divided into the sham operated group, the control group and the experimental group. The Wistar rat model of continuous compression of <jats:styled-content style="fixed-case">DRG</jats:styled-content> was used for further investigation. <jats:styled-content style="fixed-case">DRG</jats:styled-content> neurons were extracted and cultured, and the protein content was detected using bicinchoninic acid method. Western blotting and immunofluorescence assays were performed to detect the protein content. Intraperitoneal injection of lithium chloride was performed for interaction with Tau. The results were then analyzed statistically.</jats:p></jats:sec><jats:sec><jats:title>Results</jats:title><jats:p>After 2 weeks of sustained pressure, the expression level of Tau<jats:sub>396</jats:sub> increased by 33%, while Tau<jats:sub>404</jats:sub> increased by 25% in the <jats:styled-content style="fixed-case">DRG</jats:styled-content> of the experimental group (<jats:italic>p</jats:italic> < 0.05). The expression level of <jats:styled-content style="fixed-case">PSD</jats:styled-content>‐95 in the <jats:styled-content style="fixed-case">DRG</jats:styled-content> decreased by 15% (<jats:italic>p</jats:italic> < 0.05), while the expression of <jats:styled-content style="fixed-case">vG</jats:styled-content>luT1, <jats:styled-content style="fixed-case">vG</jats:styled-content>luT3 and <jats:styled-content style="fixed-case">vA</jats:styled-content>chT decreased significantly in the <jats:styled-content style="fixed-case">DRG</jats:styled-content> of the experimental group (<jats:italic>p</jats:italic> < 0.05). There was no significant difference in the expression of <jats:styled-content style="fixed-case">vG</jats:styled-content>luT2 and <jats:styled-content style="fixed-case">vGAT</jats:styled-content> among the three groups (<jats:italic>p</jats:italic> > 0.05). After intervention with lithium chloride, the expression of phosphorylated Tau at the above sites decreased in varying degrees compared with the model group. The expression level of Tau<jats:sub>404</jats:sub> was reduced by 55%, and that of Tau<jats:sub>199</jats:sub> by 60% in the <jats:styled-content style="fixed-case">DRG</jats:styled-content> of the experimental group.</jats:p></jats:sec><jats:sec><jats:title>Conclusion</jats:title><jats:p>Chronic compression of <jats:styled-content style="fixed-case">DRG</jats:styled-content> and hypoxia caused phosphorylation of Tau in axons and inhibition of <jats:styled-content style="fixed-case">PSD</jats:styled-content>‐95, and the function of the synaptic glutamic acid vesicle is defective in the synapse. This process is crucial in the development and progression of axonal transport dysfunction induced by chronic <jats:styled-content style="fixed-case">DRG</jats:styled-content> compression, and phosphorylation of Tau plays a substantial role in this process.</jats:p></jats:sec> |
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author | Zhang, Lei, Fu, Jun, Cheng, Xin‐Hua, Tang, Li |
author_facet | Zhang, Lei, Fu, Jun, Cheng, Xin‐Hua, Tang, Li, Zhang, Lei, Fu, Jun, Cheng, Xin‐Hua, Tang, Li |
author_sort | zhang, lei |
container_issue | 4 |
container_start_page | 0 |
container_title | Molecular Genetics & Genomic Medicine |
container_volume | 7 |
description | <jats:title>Abstract</jats:title><jats:sec><jats:title>Objective</jats:title><jats:p>We analyzed the function of Tau protein to explore the underlying mechanism of axonal transport disorder caused by persistent pressure in the dorsal root ganglia (<jats:styled-content style="fixed-case">DRG</jats:styled-content>).</jats:p></jats:sec><jats:sec><jats:title>Methods</jats:title><jats:p>Wistar rats were divided into the sham operated group, the control group and the experimental group. The Wistar rat model of continuous compression of <jats:styled-content style="fixed-case">DRG</jats:styled-content> was used for further investigation. <jats:styled-content style="fixed-case">DRG</jats:styled-content> neurons were extracted and cultured, and the protein content was detected using bicinchoninic acid method. Western blotting and immunofluorescence assays were performed to detect the protein content. Intraperitoneal injection of lithium chloride was performed for interaction with Tau. The results were then analyzed statistically.</jats:p></jats:sec><jats:sec><jats:title>Results</jats:title><jats:p>After 2 weeks of sustained pressure, the expression level of Tau<jats:sub>396</jats:sub> increased by 33%, while Tau<jats:sub>404</jats:sub> increased by 25% in the <jats:styled-content style="fixed-case">DRG</jats:styled-content> of the experimental group (<jats:italic>p</jats:italic> < 0.05). The expression level of <jats:styled-content style="fixed-case">PSD</jats:styled-content>‐95 in the <jats:styled-content style="fixed-case">DRG</jats:styled-content> decreased by 15% (<jats:italic>p</jats:italic> < 0.05), while the expression of <jats:styled-content style="fixed-case">vG</jats:styled-content>luT1, <jats:styled-content style="fixed-case">vG</jats:styled-content>luT3 and <jats:styled-content style="fixed-case">vA</jats:styled-content>chT decreased significantly in the <jats:styled-content style="fixed-case">DRG</jats:styled-content> of the experimental group (<jats:italic>p</jats:italic> < 0.05). There was no significant difference in the expression of <jats:styled-content style="fixed-case">vG</jats:styled-content>luT2 and <jats:styled-content style="fixed-case">vGAT</jats:styled-content> among the three groups (<jats:italic>p</jats:italic> > 0.05). After intervention with lithium chloride, the expression of phosphorylated Tau at the above sites decreased in varying degrees compared with the model group. The expression level of Tau<jats:sub>404</jats:sub> was reduced by 55%, and that of Tau<jats:sub>199</jats:sub> by 60% in the <jats:styled-content style="fixed-case">DRG</jats:styled-content> of the experimental group.</jats:p></jats:sec><jats:sec><jats:title>Conclusion</jats:title><jats:p>Chronic compression of <jats:styled-content style="fixed-case">DRG</jats:styled-content> and hypoxia caused phosphorylation of Tau in axons and inhibition of <jats:styled-content style="fixed-case">PSD</jats:styled-content>‐95, and the function of the synaptic glutamic acid vesicle is defective in the synapse. This process is crucial in the development and progression of axonal transport dysfunction induced by chronic <jats:styled-content style="fixed-case">DRG</jats:styled-content> compression, and phosphorylation of Tau plays a substantial role in this process.</jats:p></jats:sec> |
doi_str_mv | 10.1002/mgg3.580 |
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id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTAwMi9tZ2czLjU4MA |
imprint | Wiley, 2019 |
imprint_str_mv | Wiley, 2019 |
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match_str | zhang2019tauproteinfunctionthemechanicalexplorationofaxonaltransportdisordercausedbypersistentpressureindorsalrootganglia |
mega_collection | Wiley (CrossRef) |
physical | |
publishDate | 2019 |
publishDateSort | 2019 |
publisher | Wiley |
record_format | ai |
recordtype | ai |
series | Molecular Genetics & Genomic Medicine |
source_id | 49 |
spelling | Zhang, Lei Fu, Jun Cheng, Xin‐Hua Tang, Li 2324-9269 2324-9269 Wiley Genetics (clinical) Genetics Molecular Biology http://dx.doi.org/10.1002/mgg3.580 <jats:title>Abstract</jats:title><jats:sec><jats:title>Objective</jats:title><jats:p>We analyzed the function of Tau protein to explore the underlying mechanism of axonal transport disorder caused by persistent pressure in the dorsal root ganglia (<jats:styled-content style="fixed-case">DRG</jats:styled-content>).</jats:p></jats:sec><jats:sec><jats:title>Methods</jats:title><jats:p>Wistar rats were divided into the sham operated group, the control group and the experimental group. The Wistar rat model of continuous compression of <jats:styled-content style="fixed-case">DRG</jats:styled-content> was used for further investigation. <jats:styled-content style="fixed-case">DRG</jats:styled-content> neurons were extracted and cultured, and the protein content was detected using bicinchoninic acid method. Western blotting and immunofluorescence assays were performed to detect the protein content. Intraperitoneal injection of lithium chloride was performed for interaction with Tau. The results were then analyzed statistically.</jats:p></jats:sec><jats:sec><jats:title>Results</jats:title><jats:p>After 2 weeks of sustained pressure, the expression level of Tau<jats:sub>396</jats:sub> increased by 33%, while Tau<jats:sub>404</jats:sub> increased by 25% in the <jats:styled-content style="fixed-case">DRG</jats:styled-content> of the experimental group (<jats:italic>p</jats:italic> < 0.05). The expression level of <jats:styled-content style="fixed-case">PSD</jats:styled-content>‐95 in the <jats:styled-content style="fixed-case">DRG</jats:styled-content> decreased by 15% (<jats:italic>p</jats:italic> < 0.05), while the expression of <jats:styled-content style="fixed-case">vG</jats:styled-content>luT1, <jats:styled-content style="fixed-case">vG</jats:styled-content>luT3 and <jats:styled-content style="fixed-case">vA</jats:styled-content>chT decreased significantly in the <jats:styled-content style="fixed-case">DRG</jats:styled-content> of the experimental group (<jats:italic>p</jats:italic> < 0.05). There was no significant difference in the expression of <jats:styled-content style="fixed-case">vG</jats:styled-content>luT2 and <jats:styled-content style="fixed-case">vGAT</jats:styled-content> among the three groups (<jats:italic>p</jats:italic> > 0.05). After intervention with lithium chloride, the expression of phosphorylated Tau at the above sites decreased in varying degrees compared with the model group. The expression level of Tau<jats:sub>404</jats:sub> was reduced by 55%, and that of Tau<jats:sub>199</jats:sub> by 60% in the <jats:styled-content style="fixed-case">DRG</jats:styled-content> of the experimental group.</jats:p></jats:sec><jats:sec><jats:title>Conclusion</jats:title><jats:p>Chronic compression of <jats:styled-content style="fixed-case">DRG</jats:styled-content> and hypoxia caused phosphorylation of Tau in axons and inhibition of <jats:styled-content style="fixed-case">PSD</jats:styled-content>‐95, and the function of the synaptic glutamic acid vesicle is defective in the synapse. This process is crucial in the development and progression of axonal transport dysfunction induced by chronic <jats:styled-content style="fixed-case">DRG</jats:styled-content> compression, and phosphorylation of Tau plays a substantial role in this process.</jats:p></jats:sec> Tau protein function: The mechanical exploration of axonal transport disorder caused by persistent pressure in dorsal root ganglia Molecular Genetics & Genomic Medicine |
spellingShingle | Zhang, Lei, Fu, Jun, Cheng, Xin‐Hua, Tang, Li, Molecular Genetics & Genomic Medicine, Tau protein function: The mechanical exploration of axonal transport disorder caused by persistent pressure in dorsal root ganglia, Genetics (clinical), Genetics, Molecular Biology |
title | Tau protein function: The mechanical exploration of axonal transport disorder caused by persistent pressure in dorsal root ganglia |
title_full | Tau protein function: The mechanical exploration of axonal transport disorder caused by persistent pressure in dorsal root ganglia |
title_fullStr | Tau protein function: The mechanical exploration of axonal transport disorder caused by persistent pressure in dorsal root ganglia |
title_full_unstemmed | Tau protein function: The mechanical exploration of axonal transport disorder caused by persistent pressure in dorsal root ganglia |
title_short | Tau protein function: The mechanical exploration of axonal transport disorder caused by persistent pressure in dorsal root ganglia |
title_sort | tau protein function: the mechanical exploration of axonal transport disorder caused by persistent pressure in dorsal root ganglia |
title_unstemmed | Tau protein function: The mechanical exploration of axonal transport disorder caused by persistent pressure in dorsal root ganglia |
topic | Genetics (clinical), Genetics, Molecular Biology |
url | http://dx.doi.org/10.1002/mgg3.580 |