Abstract

Labeling Pathological Tau: An Important Quest for the Unknown.

Highlights

  • Senile plaques are formed by the accumulation of Aβ peptides derived from the proteolysis of the Amyloid Precursor Protein, while neurofibrillary tangles are ultrastructures predominantly compose of aberrantly phosphorylated tau proteins

  • Previous studies indicated that reduction of Aβ peptides and increase of phosphorylated tau peptides in the cerebrospinal fluid (CSF) serve as biomarkers to confirm the diagnosis of probable Alzheimer’s disease (AD) (Olsson et al, 2016)

  • Different studies showed that the detection of Aβ pathology precede the detection of pathological tau, it is the accumulation of tau aggregates at specific brain regions that directly correlates with executive dysfunction and cognitive impairment in AD (Arriagada et al, 1992; Jack et al, 2013)

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Summary

Introduction

The fluorescent pentameric oligothiophene pFTAA identifies filamentous tau in live neurons cultured from adult P301S tau mice by Brelstaff, J., Ossola, B., Neher, J. Neuropathological studies indicated that the level of accumulation of these pathological lesions correlate with the severity of the clinical presentation (Braak and Braak, 1991; Hyman et al, 2012). Due to the low invasiveness and promising results already obtained, most research efforts have been re-directed to develop selective molecules that facilitate the imaging of pathological proteins in living neurons and individuals.

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