NDLI: C-Reactive Protein Induces Tau Hyperphosphorylation via GSK3β Signaling Pathway in SH-SY5Y Cells

Content Provider	Springer Nature Link
Author	Guo, Haibiao Wang, Haitao Wang, Canmao Cheng, Yufang Zou, Zhengqiang Li, Yiwen Wu, Jingang Xu, Jiangping
Copyright Year	2015
Abstract	Amyloid plaques and neurofibrillary tangles are the key pathological features of Alzheimer’s disease (AD). Studies have shown that C-reactive protein (CRP) increases during inflammatory reactions and, therefore, has been associated with AD. However, there is no published report relating the impact of CRP to the regulation of tau phosphorylation. In the present study, we investigated the effects of CRP on the phosphorylation of tau protein in SH-SY5Y cells. Treatment of cells with CRP (5, 10, 20 μg/ml) resulted in neurotoxicity and apoptosis, as was observed by MTT assay and Hoechst staining, respectively. Western blot analysis showed that CRP, in a time- and concentration-dependent manner, induced the phosphorylation of tau at Ser202 and ser396 in SH-SY5Y cells. Phosphorylation of Akt (Ser473) and GSK3β (Ser9) were decreased by CRP treatment, whereas phosphorylation of ERK and p38 were not affected. Pharmacological inhibition of GSK3β reversed the effects induced by CRP, viz., cytotoxicity, apoptosis, and tau phosphorylation. Herein, we present a novel mechanism of cell death following CRP insult, which activates tau hyperphosphorylation by regulating GSK3β activity. CRP could potentially be used as an important pathological factor for the therapeutic intervention of AD.
Starting Page	519
Ending Page	527
Page Count	9
File Format	PDF
ISSN	08958696
Journal	Journal of Molecular Neuroscience
Volume Number	56
Issue Number	2
e-ISSN	15591166
Language	English
Publisher	Springer US
Publisher Date	2015-05-13
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	C-reactive protein (CRP) Neurofibrillary tangles (NFTs) Tau Alzheimer’s disease (AD) Glycogen synthase kinase 3-beta (GSK3β) Neurosciences Neurochemistry Cell Biology Proteomics Neurology
Content Type	Text
Resource Type	Article
Subject	Medicine Cellular and Molecular Neuroscience

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

S100B induces tau protein hyperphosphorylation via Dickopff-1 up-regulation and disrupts the Wnt pathway in human neural stem cells

Chronic lithium administration to FTDP-17 tau and GSK-3? overexpressing mice prevents tau hyperphosphorylation and neurofibrillary tangle formation, but pre-formed neurofibrillary tangles do not revert

Stable Mutated tau441 Transfected SH-SY5Y Cells as Screening Tool for Alzheimer’s Disease Drug Candidates

Tau: The Center of a Signaling Nexus in Alzheimer's Disease

Programmed Cell Death Protein 1 Blockade Reduces Glycogen Synthase Kinase 3β Activity and Tau Hyperphosphorylation in Alzheimer’s Disease Mouse Models

Exposure to Pyrithiamine Increases β-Amyloid Accumulation, Tau Hyperphosphorylation, and Glycogen Synthase Kinase-3 Activity in the Brain

Advances in the Pathogenesis of Alzheimer’s Disease: Focusing on Tau-Mediated Neurodegeneration

The neuron-specific isoform of glycogen synthase kinase-3β is required for axon growth

A novel glycogen synthase kinase-3 inhibitor 2-methyl-5-(3-{4-[(S )-methylsulfinyl]phenyl}-1-benzofuran-5-yl)-1,3,4-oxadiazole decreases tau phosphorylation and ameliorates cognitive deficits in a transgenic model of Alzheimer’s disease

C-Reactive Protein Induces Tau Hyperphosphorylation via GSK3β Signaling Pathway in SH-SY5Y Cells

Similar Documents

S100B induces tau protein hyperphosphorylation via Dickopff-1 up-regulation and disrupts the Wnt pathway in human neural stem cells

Chronic lithium administration to FTDP-17 tau and GSK-3? overexpressing mice prevents tau hyperphosphorylation and neurofibrillary tangle formation, but pre-formed neurofibrillary tangles do not revert

Stable Mutated tau441 Transfected SH-SY5Y Cells as Screening Tool for Alzheimer’s Disease Drug Candidates

Tau: The Center of a Signaling Nexus in Alzheimer's Disease

Programmed Cell Death Protein 1 Blockade Reduces Glycogen Synthase Kinase 3β Activity and Tau Hyperphosphorylation in Alzheimer’s Disease Mouse Models

Exposure to Pyrithiamine Increases β-Amyloid Accumulation, Tau Hyperphosphorylation, and Glycogen Synthase Kinase-3 Activity in the Brain

Advances in the Pathogenesis of Alzheimer’s Disease: Focusing on Tau-Mediated Neurodegeneration

The neuron-specific isoform of glycogen synthase kinase-3β is required for axon growth

A novel glycogen synthase kinase-3 inhibitor 2-methyl-5-(3-{4-[(S )-methylsulfinyl]phenyl}-1-benzofuran-5-yl)-1,3,4-oxadiazole decreases tau phosphorylation and ameliorates cognitive deficits in a transgenic model of Alzheimer’s disease

C-Reactive Protein Induces Tau Hyperphosphorylation via GSK3β Signaling Pathway in SH-SY5Y Cells