Thursday, November 27, 2014

Animal models of tauopathies and their implications for research/translation into the clinic

Invited Review

 

Animal models of tauopathies and their implications for research/translation into the clinic

 

Simon Dujardin, Morvane Colin* and Luc Buée DOI: 10.1111/nan.12200

 

Author Information

 

Inserm, UMR1172 Jean-Pierre Aubert research centre, Lille, France ; Université de Lille, Faculté de Médecine, Lille, France; CHRU, Memory Clinic, Lille, France

 

* Corresponding authors: Drs L. Buée & M. Colin Inserm UMR1172, ‘Alzheimer & Tauopathies’ Bâtiment Biserte, rue Polonovski 59045 Lille Cedex, France Tel: +33 320 298850, Fax: +33 220 538562 Emails: morvane.colin@inserm.fr, luc.buee@inserm.fr

 

This article has been accepted for publication and undergone full peer review but has not been through the copyediting, typesetting, pagination and proofreading process, which may lead to differences between this version and the Version of Record. Please cite this article as doi: 10.1111/nan.12200

 

Publication History Accepted manuscript online: 26 NOV 2014 10:37PM EST Manuscript Accepted: 23 NOV 2014

 

Keywords:

 

Alzheimer's disease; prion; propagation; tau protein; phosphorylation; aggregation; neurodegeneration; therapeutic approaches

 

Abstract

 

Our aims are to review animal models of tauopathies, which include a number of brain disorders with various aetiologies, including aging, genetics, infectious diseases, toxins, trauma, and other unknown factors. Tauopathies are characterised by the accumulation of filaments of the microtubule-associated tau protein. The different aetiopathogeneses and distinct molecular events involved in tau aggregation have led to the development of various animal models for these diseases.

 

In this review, rather than listing all current models, we focus on specific animal models addressing, among others, the question of tau hyperphosphorylation, tau aggregation and tau spreading. Physiological conditions, including normal aging and hibernation, may exhibit tau phosphorylation and some aspects of tauopathies. However, most of the models of tauopathies involve genetically modified animals (mostly rodents, but also fruit fly, zebrafish, and worm). Some of these models have been crucial for the development of therapeutic approaches in humans.

 

The present review shows the difficulty in pinpointing a specific mechanism that may be targeted in tauopathies but also opens up new avenues for innovative therapeutic strategies.

 


 

Monday, November 17, 2014

 

Prion-like transmission and spreading of tau pathology

 


 

Wednesday, June 19, 2013

 

Spreading of tau pathology in Alzheimer's disease by cell-to-cell transmission

 


 

Saturday, May 25, 2013

 

Brain homogenates from human tauopathies induce tau inclusions in mouse brain

 


 


 

Sunday, November 23, 2014

 

Transmission Characteristics of Variably Protease-Sensitive Prionopathy

 

* We concluded that VPSPr is transmissible; thus, it is an authentic prion disease.

 


 


 


 


 

Self-Propagative Replication of Ab Oligomers Suggests Potential Transmissibility in Alzheimer Disease

 

Received July 24, 2014; Accepted September 16, 2014; Published November 3, 2014

 


 

Singeltary comment ;

 


 

Monday, November 3, 2014

 

USA CJD TSE PRION UNIT, TEXAS, SURVEILLANCE UPDATE NOVEMBER 2014

 

National Prion Disease Pathology Surveillance Center Cases Examined1 (October 7, 2014)

 

***6 Includes 11 cases in which the diagnosis is pending, and 19 inconclusive cases;

 

***7 Includes 12 (11 from 2014) cases with type determination pending in which the diagnosis of vCJD has been excluded.

 

***The sporadic cases include 2660 cases of sporadic Creutzfeldt-Jakob disease (sCJD),

 

***50 cases of Variably Protease-Sensitive Prionopathy (VPSPr)

 

***and 21 cases of sporadic Fatal Insomnia (sFI).

 


 

 Sunday, November 23, 2014

 

Confirmed Variant Creutzfeldt-Jakob Disease (variant CJD) Case in Texas in June 2014 confirmed as USA case NOT European

 

 
 
 
TSS

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