pFTAA: a high affinity oligothiophene probe that detects filamentous tau in vivo and in cultured neurons

作     者：Jack Brelstaff Maria Grazia Spillantini Aviva M.Tolkovsky 

作者机构：Department of Clinical Neurosciences The Clifford Allbutt Building University of Cambridge 

出 版 物：《Neural Regeneration Research》 (中国神经再生研究（英文版）)

年 卷 期：2015年第10卷第11期

页      面：1746-1747页

核心收录：

学科分类：1002[医学-临床医学] 100204[医学-神经病学] 10[医学] 

基　　金：funded by grant NC/L000741/1 from the National Council of the 3Rs 

主　　题：pFTAA a high affinity oligothiophene probe that detects filamentous tau in vivo and in cultured neurons high 

摘      要：Tauopathies describe a group of neurodegenerative diseases in which the protein tau,encoded by the gene MAPT,is aberrantly misfolded,leading to tau aggregation,neural dysfunction,and cell death（Spillantini and Goedert,2013）.In Alzheimer＇s disease（AD）,tau forms the characteristic intracellular neurofibrillary tangles（NFTs）,which are thought to be the major cause of neurodegeneration（Bloom,2014）.In other tauopathies,including frontotemporal dementia with Parkinsonism linked to chromo- some 17 （FTDP-17T）, corticobasal degeneration and progressive supranuclear palsy, there are specific forms of tau aggregates and filaments without any amyloid pathology, demonstrating tau＇s po- tent disease-causing potential （Spillantini and Goedert, 2013）. Tau is a microtubule （MT） binding protein, which becomes abnormally hyperphosphorylated on several residues prior/during the process of aggregation, thereby causing loss of its MT binding activity （Mandelkow and Mandelkow, 2012）.