The Physiological Link between Metabolic Rate Depression and Tau Phosphorylation in Mammalian

Abnormal phosphorylation and aggregation of tau protein are hallmarks of a variety of neurological disorders, including Alzheimer’s disease (AD). Increased tau phosphorylation is assumed to represent an early event in pathogenesis and a pivotal aspect for aggregation and formation of neurofibrillary...

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Main Authors: Jens T. Stieler, Torsten Bullmann, Franziska Kohl, Øivind Tøien, Martina K. Brückner, Brian M. Barnes, Thomas Arendt
Other Authors: The Pennsylvania State University CiteSeerX Archives
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Online Access:http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.292.6047
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spelling ftciteseerx:oai:CiteSeerX.psu:10.1.1.292.6047 2023-05-15T15:09:04+02:00 The Physiological Link between Metabolic Rate Depression and Tau Phosphorylation in Mammalian Jens T. Stieler Torsten Bullmann Franziska Kohl Øivind Tøien Martina K. Brückner Brian M. Barnes Thomas Arendt The Pennsylvania State University CiteSeerX Archives application/zip http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.292.6047 en eng http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.292.6047 Metadata may be used without restrictions as long as the oai identifier remains attached to it. ftp://ftp.ncbi.nlm.nih.gov/pub/pmc/14/71/PLoS_One_2011_Jan_18_6(1)_e14530.tar.gz text ftciteseerx 2016-01-07T21:38:27Z Abnormal phosphorylation and aggregation of tau protein are hallmarks of a variety of neurological disorders, including Alzheimer’s disease (AD). Increased tau phosphorylation is assumed to represent an early event in pathogenesis and a pivotal aspect for aggregation and formation of neurofibrillary tangles. However, the regulation of tau phosphorylation in vivo and the causes for its increased stage of phosphorylation in AD are still not well understood, a fact that is primarily based on the lack of adequate animal models. Recently we described the reversible formation of highly phosphorylated tau protein in hibernating European ground squirrels. Hence, mammalian hibernation represents a model system very well suited to study molecular mechanisms of both tau phosphorylation and dephosphorylation under in vivo physiological conditions. Here, we analysed the extent and kinetics of hibernation-state dependent tau phosphorylation in various brain regions of three species of hibernating mammals: arctic ground squirrels, Syrian hamsters and black bears. Overall, tau protein was highly phosphorylated in torpor states and phosphorylation levels decreased after arousal in all species. Differences between brain regions, hibernation-states and phosphosites were observed with respect to degree and kinetics of tau phosphorylation. Furthermore, we tested the phosphate net turnover of tau protein to analyse potential alterations in kinase and/or phosphatase activities during hibernation. Our results demonstrate that the hibernation-state dependent phosphorylation of tau protein is specifically regulated but involves, in addition, passive, temperature driven regulatory Text Arctic Unknown Arctic
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description Abnormal phosphorylation and aggregation of tau protein are hallmarks of a variety of neurological disorders, including Alzheimer’s disease (AD). Increased tau phosphorylation is assumed to represent an early event in pathogenesis and a pivotal aspect for aggregation and formation of neurofibrillary tangles. However, the regulation of tau phosphorylation in vivo and the causes for its increased stage of phosphorylation in AD are still not well understood, a fact that is primarily based on the lack of adequate animal models. Recently we described the reversible formation of highly phosphorylated tau protein in hibernating European ground squirrels. Hence, mammalian hibernation represents a model system very well suited to study molecular mechanisms of both tau phosphorylation and dephosphorylation under in vivo physiological conditions. Here, we analysed the extent and kinetics of hibernation-state dependent tau phosphorylation in various brain regions of three species of hibernating mammals: arctic ground squirrels, Syrian hamsters and black bears. Overall, tau protein was highly phosphorylated in torpor states and phosphorylation levels decreased after arousal in all species. Differences between brain regions, hibernation-states and phosphosites were observed with respect to degree and kinetics of tau phosphorylation. Furthermore, we tested the phosphate net turnover of tau protein to analyse potential alterations in kinase and/or phosphatase activities during hibernation. Our results demonstrate that the hibernation-state dependent phosphorylation of tau protein is specifically regulated but involves, in addition, passive, temperature driven regulatory
author2 The Pennsylvania State University CiteSeerX Archives
format Text
author Jens T. Stieler
Torsten Bullmann
Franziska Kohl
Øivind Tøien
Martina K. Brückner
Brian M. Barnes
Thomas Arendt
spellingShingle Jens T. Stieler
Torsten Bullmann
Franziska Kohl
Øivind Tøien
Martina K. Brückner
Brian M. Barnes
Thomas Arendt
The Physiological Link between Metabolic Rate Depression and Tau Phosphorylation in Mammalian
author_facet Jens T. Stieler
Torsten Bullmann
Franziska Kohl
Øivind Tøien
Martina K. Brückner
Brian M. Barnes
Thomas Arendt
author_sort Jens T. Stieler
title The Physiological Link between Metabolic Rate Depression and Tau Phosphorylation in Mammalian
title_short The Physiological Link between Metabolic Rate Depression and Tau Phosphorylation in Mammalian
title_full The Physiological Link between Metabolic Rate Depression and Tau Phosphorylation in Mammalian
title_fullStr The Physiological Link between Metabolic Rate Depression and Tau Phosphorylation in Mammalian
title_full_unstemmed The Physiological Link between Metabolic Rate Depression and Tau Phosphorylation in Mammalian
title_sort physiological link between metabolic rate depression and tau phosphorylation in mammalian
url http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.292.6047
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