In Focus: Phosphorylated PP2A (tyrosine 307) is associated with Alzheimer neurofibrillary pathology

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Phosphorylated PP2A (tyrosine 307) is associated with Alzheimer neurofibrillary pathology

Down-regulation of protein phosphatase 2A (PP2A) is thought to play a critical role in tau hyperphosphorylation in Alzheimer's disease (AD). In vitro phosphorylation of PP2A catalytic subunit at Y307 efficiently inactivates PP2A. A specific antibody against phosphorylated (p) PP2A (Y307) (PP2Ac-Yp307) was used to investigate possible PP2A down-regulation by known pathophysiological changes asso...

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Molecular pathology of Alzheimer neurofibrillary

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Alzheimer neurofibrillary tangles contain phosphorylated and hidden neurofilament epitopes.

Three monoclonal antibodies to neurofilaments (RT97, BF10 and 147), two of which also recognised neurofibrillary tangles (RT97 and BF10), have all been shown to be specific for phosphorylated epitopes. Treatment of histological sections with alkaline phosphatase prior to immunostaining resulted in reduction of axonal neurofilament staining with all three whilst the neurofibrillary tangles stain...

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CSF phosphorylated tau protein correlates with neocortical neurofibrillary pathology in Alzheimer's disease.

Hyperphosphorylated tau protein (P-tau) in CSF is a core biomarker candidate of Alzheimer's disease. Hyperphosphorylation of tau is thought to lead to neurofibrillary changes, a neuropathological hallmark of this type of dementia. Currently, the question is unresolved whether CSF levels of P-tau reflect neurofibrillary changes within the brain of a patient with the illness. Twenty-six patients ...

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ژورنال

عنوان ژورنال: Journal of Cellular and Molecular Medicine

سال: 2007

ISSN: 1582-1838

DOI: 10.1111/j.1582-4934.2008.00249.x