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Development of a grape seed polyphenolic extract with anti‐oligomeric activity as a novel treatment in progressive supranuclear palsy and other tauopathies
Author(s) -
Pasinetti Giulio Maria,
KsiezakReding Hanna,
SantaMaria Ismael,
Wang Jun,
Ho Lap
Publication year - 2010
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2010.06875.x
Subject(s) - progressive supranuclear palsy , tauopathy , corticobasal degeneration , neuroscience , neurodegeneration , tau protein , synucleinopathies , tau pathology , intracellular , biology , chemistry , parkinson's disease , medicine , disease , biochemistry , alzheimer's disease , pathology , alpha synuclein
J. Neurochem. (2010) 114 , 1557–1568. Abstract A diverse group of neurodegenerative diseases – including progressive supranuclear palsy (PSP), corticobasal degeneration and Alzheimer’s disease among others, collectively referred to as tauopathies – are characterized by progressive, age‐dependent intracellular formations of misfolded protein aggregates that play key roles in the initiation and progression of neuropathogenesis. Recent studies from our laboratory reveal that grape seed‐derived polyphenolic extracts (GSPE) potently prevent tau fibrillization into neurotoxic aggregates and therapeutically promote the dissociation of preformed tau aggregates [J. Alzheimer’s Dis. (2009) vol. 16, pp. 433]. Based on our extensive bioavailability, bioactivity and functional preclinical studies, combined with the safety of GSPE in laboratory animals and in humans, we initiated a series of studies exploring the role of GSPE (Meganatural‐Az ® GSPE) as a potential novel botanical drug for the treatment of certain forms of tauopathies including PSP, a neurodegenerative disorder involving the accumulation and deposition of misfolded tau proteins in the brain characterized, in part, by abnormal intracellular tau inclusions in specific anatomical areas involving astrocytes, oligodendrocytes and neurons [J. Neuropathol. Exp. Neurol. (2002) vol. 61, pp. 33]. In this mini‐review article, we discuss the biochemical characterization of GSPE in our laboratory and its potential preventative and therapeutic role in model systems of abnormal tau processing pertinent to PSP and related tauopathies.