Cystatin C promotes tau protein phosphorylation and causes microtubule instability by inhibiting intracellular turnover of GSK3β in neurons

In Alzheimer's disease (AD) tau protein hyperphosphorylation causes neurofibrillary tangle formation, microtubule instability and neurodegeneration. Determining the mechanism of tau hyperphosphorylation will provide a better understanding of AD pathology. Cystatin C (CysC) is a risk factor for...

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Published in:	Molecular and cellular neuroscience Vol. 89; pp. 1 - 8
Main Authors:	Duan, Jinhai, Marcellus, Kristen A., Qin, Xike, Wang, Yunling, Paudel, Hemant K.
Format:	Journal Article
Language:	English
Published:	United States Elsevier Inc 01-06-2018
Subjects:	3xTg-AD mice Alzheimer Disease - metabolism Alzheimer's disease Animals Cystatin C Cystatin C - pharmacology Glycogen Synthase Kinase 3 beta - metabolism GSK3β HEK293 Cells Humans Mice Microtubules - drug effects Microtubules - metabolism Neurons - drug effects Neurons - metabolism PC12 Cells Phosphorylation Protein Processing, Post-Translational Proteolysis Rats Tau phosphorylation tau Proteins - metabolism Tau phosphorylation Aβ GSK3β AD NFTs 3xTg-AD mice CysC Cystatin C Alzheimer's disease
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Abstract	In Alzheimer's disease (AD) tau protein hyperphosphorylation causes neurofibrillary tangle formation, microtubule instability and neurodegeneration. Determining the mechanism of tau hyperphosphorylation will provide a better understanding of AD pathology. Cystatin C (CysC) is a risk factor for late-onset AD and its level is upregulated in the brains of AD patients. The role of CysC is AD pathogenesis is not known. In this study, we found that CysC level is upregulated in 3xTg-AD mouse brain. We demonstrate that CysC does not affect cellular Aβ production. However, when overexpressed in neuron (NGF-differentiated PC12 cells), CysC inhibits turnover of GSK3β, promotes GSK3β-catalyzed tau phosphorylation at Ser396/404 and causes microtubule instability. Our data provide a novel insight into the role of CysC in AD pathogenesis. •Cystatin C is one of the risk factors for LOAD.•Cystatin C does not affect Aβ production in HEK-293 cells.•Cystatin C promotes GSK3β-catalyzed tau protein phosphorylation in neurons.•Cystatin C inhibits cellular degradation of GSK3β.
AbstractList	In Alzheimer's disease (AD) tau protein hyperphosphorylation causes neurofibrillary tangle formation, microtubule instability and neurodegeneration. Determining the mechanism of tau hyperphosphorylation will provide a better understanding of AD pathology. Cystatin C (CysC) is a risk factor for late-onset AD and its level is upregulated in the brains of AD patients. The role of CysC is AD pathogenesis is not known. In this study, we found that CysC level is upregulated in 3xTg-AD mouse brain. We demonstrate that CysC does not affect cellular Aβ production. However, when overexpressed in neuron (NGF-differentiated PC12 cells), CysC inhibits turnover of GSK3β, promotes GSK3β-catalyzed tau phosphorylation at Ser396/404 and causes microtubule instability. Our data provide a novel insight into the role of CysC in AD pathogenesis. In Alzheimer's disease (AD) tau protein hyperphosphorylation causes neurofibrillary tangle formation, microtubule instability and neurodegeneration. Determining the mechanism of tau hyperphosphorylation will provide a better understanding of AD pathology. Cystatin C (CysC) is a risk factor for late-onset AD and its level is upregulated in the brains of AD patients. The role of CysC is AD pathogenesis is not known. In this study, we found that CysC level is upregulated in 3xTg-AD mouse brain. We demonstrate that CysC does not affect cellular Aβ production. However, when overexpressed in neuron (NGF-differentiated PC12 cells), CysC inhibits turnover of GSK3β, promotes GSK3β-catalyzed tau phosphorylation at Ser and causes microtubule instability. Our data provide a novel insight into the role of CysC in AD pathogenesis. In Alzheimer's disease (AD) tau protein hyperphosphorylation causes neurofibrillary tangle formation, microtubule instability and neurodegeneration. Determining the mechanism of tau hyperphosphorylation will provide a better understanding of AD pathology. Cystatin C (CysC) is a risk factor for late-onset AD and its level is upregulated in the brains of AD patients. The role of CysC is AD pathogenesis is not known. In this study, we found that CysC level is upregulated in 3xTg-AD mouse brain. We demonstrate that CysC does not affect cellular Aβ production. However, when overexpressed in neuron (NGF-differentiated PC12 cells), CysC inhibits turnover of GSK3β, promotes GSK3β-catalyzed tau phosphorylation at Ser396/404 and causes microtubule instability. Our data provide a novel insight into the role of CysC in AD pathogenesis. •Cystatin C is one of the risk factors for LOAD.•Cystatin C does not affect Aβ production in HEK-293 cells.•Cystatin C promotes GSK3β-catalyzed tau protein phosphorylation in neurons.•Cystatin C inhibits cellular degradation of GSK3β.
Author	Wang, Yunling Paudel, Hemant K. Qin, Xike Duan, Jinhai Marcellus, Kristen A.
Author_xml	– sequence: 1 givenname: Jinhai surname: Duan fullname: Duan, Jinhai organization: Department of Neurology, Guangdong General Hospital, Guangdong Academy of Medical Sciences, Guangdong Institute of Geriatrics, Guangdong Institute of Neurosciences, Guangzhou 510080, China – sequence: 2 givenname: Kristen A. surname: Marcellus fullname: Marcellus, Kristen A. organization: Lady Davis Institute for Medical Research, Jewish General Hospital, McGill University, Montreal, Quebec H4H 1R3, Canada – sequence: 3 givenname: Xike surname: Qin fullname: Qin, Xike organization: Lady Davis Institute for Medical Research, Jewish General Hospital, McGill University, Montreal, Quebec H4H 1R3, Canada – sequence: 4 givenname: Yunling surname: Wang fullname: Wang, Yunling organization: Lady Davis Institute for Medical Research, Jewish General Hospital, McGill University, Montreal, Quebec H4H 1R3, Canada – sequence: 5 givenname: Hemant K. surname: Paudel fullname: Paudel, Hemant K. email: hemant.paudel@mcgill.ca organization: Lady Davis Institute for Medical Research, Jewish General Hospital, McGill University, Montreal, Quebec H4H 1R3, Canada
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Keywords	Tau phosphorylation Aβ GSK3β AD NFTs 3xTg-AD mice CysC Cystatin C Alzheimer's disease
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Snippet	In Alzheimer's disease (AD) tau protein hyperphosphorylation causes neurofibrillary tangle formation, microtubule instability and neurodegeneration....
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SubjectTerms	3xTg-AD mice Alzheimer Disease - metabolism Alzheimer's disease Animals Cystatin C Cystatin C - pharmacology Glycogen Synthase Kinase 3 beta - metabolism GSK3β HEK293 Cells Humans Mice Microtubules - drug effects Microtubules - metabolism Neurons - drug effects Neurons - metabolism PC12 Cells Phosphorylation Protein Processing, Post-Translational Proteolysis Rats Tau phosphorylation tau Proteins - metabolism
Title	Cystatin C promotes tau protein phosphorylation and causes microtubule instability by inhibiting intracellular turnover of GSK3β in neurons
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