path(HBP:"Corticobasal Degeneration")

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Corticobasal Degeneration

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HBP

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20190207

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Tau Modifications Sections of NESTOR

On the other side, sarkosyl extracts from the filaments of PSP [129], corticobasal degeneration (CBD; [130]), argyrophilic grain disease (AgD; [131]), and some cases of FTDP-17, contain tau protein that separates as doublets of 64 and 69 kDa and are predominantly composed of tau isoforms with 4R (class II tauopathies), whereas sarkosyl extracts from filaments of Pick’s disease are characterized by the presence of pathological tau doublets of 60 and 64 kDa and contain mainly 3R tau isoforms (class III tauopathy). PubMed:26751493

Thus, K280 acetylation is a feature found in a variety of human 4R or 3R/4R tauopathies including AD, but not 3R-tauopathies such as PiD. PubMed:21427723

Tau-nY18 did not label the classical pathological lesions of CBD or PSP but did label the neuronal lesions associated with PiD. Tau-nY29 revealed some, but not all classes of tau inclusions associated with both CBD and PSP but did label numerous Pick body inclusions in PiD. Tau-nY197 was restricted to the neuropil threads in both CBD and PSP; however, similar to Tau-nY29, extensive Pick body pathology was clearly labeled. Tau-nY394 did not detect any of the lesions associated with these disorders. PubMed:22057784

Tau-nY29 detects soluble tau and paired helical filament tau from severely affected Alzheimer's brain but fails to recognize tau from normal aged brain. This observation suggests that nitration at Tyr29 is a disease-related event that may alter the intrinsic ability of tau to self-polymerize. In Alzheimer's brain, Tau-nY29 labels the fibrillar triad of tau lesions, including neurofibrillary tangles, neuritic plaques, and, to a lesser extent, neuropil threads. Intriguingly, although Tau-nY29 stains both the neuronal and glial tau pathology of Pick disease, it detects only the neuronal pathology in corticobasal degeneration and progressive supranuclear palsy without labeling the predominant glial pathology. PubMed:17050703

Tauopathies can be classified into three groups on the basis of the tau isoforms found in the aggregates: 4R tauopathies (including PSP, CBD and AGD), 3R tauopathies (for example, PiD) and 3R+4R tauopathies (for example, AD) PubMed:26631930

On the other side, sarkosyl extracts from the filaments of PSP [129], corticobasal degeneration (CBD; [130]), argyrophilic grain disease (AgD; [131]), and some cases of FTDP-17, contain tau protein that separates as doublets of 64 and 69 kDa and are predominantly composed of tau isoforms with 4R (class II tauopathies), whereas sarkosyl extracts from filaments of Pick’s disease are characterized by the presence of pathological tau doublets of 60 and 64 kDa and contain mainly 3R tau isoforms (class III tauopathy). PubMed:26751493

Tau-nY18 did not label the classical pathological lesions of CBD or PSP but did label the neuronal lesions associated with PiD. Tau-nY29 revealed some, but not all classes of tau inclusions associated with both CBD and PSP but did label numerous Pick body inclusions in PiD. Tau-nY197 was restricted to the neuropil threads in both CBD and PSP; however, similar to Tau-nY29, extensive Pick body pathology was clearly labeled. Tau-nY394 did not detect any of the lesions associated with these disorders. PubMed:22057784

Tau-nY29 detects soluble tau and paired helical filament tau from severely affected Alzheimer's brain but fails to recognize tau from normal aged brain. This observation suggests that nitration at Tyr29 is a disease-related event that may alter the intrinsic ability of tau to self-polymerize. In Alzheimer's brain, Tau-nY29 labels the fibrillar triad of tau lesions, including neurofibrillary tangles, neuritic plaques, and, to a lesser extent, neuropil threads. Intriguingly, although Tau-nY29 stains both the neuronal and glial tau pathology of Pick disease, it detects only the neuronal pathology in corticobasal degeneration and progressive supranuclear palsy without labeling the predominant glial pathology. PubMed:17050703

Thus, K280 acetylation is a feature found in a variety of human 4R or 3R/4R tauopathies including AD, but not 3R-tauopathies such as PiD. PubMed:21427723

Tauopathies can be classified into three groups on the basis of the tau isoforms found in the aggregates: 4R tauopathies (including PSP, CBD and AGD), 3R tauopathies (for example, PiD) and 3R+4R tauopathies (for example, AD) PubMed:26631930