Neuropathologic Overlap of Progressive Supranuclear Palsy, Pickʼs Disease and Corticobasal Degeneration

Feany, Mel Β.; Mattiace, Linda A.; Dickson, Dennis W.

doi:10.1097/00005072-199601000-00006

Cited by 250 publications

(113 citation statements)

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“…Immunochemical characterization of tau variants in neurodegenerative disorders using AD2 was consistent with that performed in previous studies [1 5,[9][10][11]14,16]. A major tau triplet made of Tau 55, 64 and 69 and a minor variant at 74 kDa were found in AD ( Fig.…”

Section: Resultssupporting

confidence: 88%

“…By immunoblotting, PHF-Tau are characterized by a tau triplet Tau 55, 64, 69 and a minor electrophoretic variant at 74 kDa [9]. In PiD, aggregated tau proteins are made of a major tau doublet Tau 55, 64 and a minor variant at 69 kDa [5,10], whereas in PSP, CBD and in some cases with fronto-temporal dementia with parkinsonism linked to chromosome 17 (FTDP-17), another tau doublet Tau 64, 69 with a minor variant at 74 kDa, characterizes neuronal and glial filaments [5,11,12]. Recent data indicate that the tau electrophoretic profiles observed in neurodegenerative disorders may be related to specific tau isoforms in particular subsets of neurons [13].…”

Section: Introductionmentioning

confidence: 99%

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Phosphorylation of specific sets of tau isoforms reflects different neurofibrillary degeneration processes

et al. 1998

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Tau proteins are the basic components of filaments that accumulate within neurons during neurofibrillary degeneration, a degenerating process with disease-specific phenotypes. This specificity is likely to be sustained by both phosphorylation state and isoform content of tau aggregates that form neuronal inclusions. In the present study, characterization of tau isoforms involved in neurofibrillary degeneration in Alzbeimer's disease, Pick's disease, corticobasal degeneration and progressive supranuclear palsy was performed. Both analyses by immunoblotting using specific tau antibodies and cell transfection by tau isoform cDNAs allowed us to demonstrate the aggregation of (1) the six hyperpbosphorylated tau isoforms in Alzheimer's disease, (2) tau isoforms without exon 10-encoding sequence in Pick's disease and (3) hyperphosphorylated exon 10-tau isoforms in corticobasal degeneration and progressive supranuclear palsy. Thus, neurofibrillary degeneration phenotypes are likely to be related to the phosphorylation of different combinations of tau isoforms (with and/or without exon 10-encoding sequence) in subpopulations of neurons.

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Section: Resultssupporting

confidence: 88%

Section: Introductionmentioning

confidence: 99%

Phosphorylation of specific sets of tau isoforms reflects different neurofibrillary degeneration processes

et al. 1998

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“…36 The presence of ubiquitin immunoreactivity in the filaments in oligodendrocytes differs from tau inclusions in human tauopathies, in which ubiquitin immunoreactivity is minimal with IHC. 37 In addition, less ubiquitin immunolabeling has been detected on filaments isolated from corticobasal degeneration, a sporadic 4R tauopathy, than Alzheimer's disease. 38 The variability in ubiquitin immunoreactivity might be because of different tau isoform composition in different disorders.…”

Section: Discussionmentioning

confidence: 99%

Filamentous Tau in Oligodendrocytes and Astrocytes of Transgenic Mice Expressing the Human Tau Isoform with the P301L Mutation

Lin

Lewis

Yen

et al. 2003

The American Journal of Pathology

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We recently reported a transgenic mouse line (JNPL3) that expresses mutant (P301L) tau and develops neurofibrillary tangles composed of filamentous tau aggregates. Here we show that these mice have abnormal tau filaments not only in neurons, but also in oligodendrocytes and astrocytes. Similar results were detected in another transgenic line (JNPL2؉3؉) that expresses the longest human tau isoform with the P301L mutation. The ultrastructure of the tau filaments and immunoreactivity with tau and ubiquitin antibodies were similar in glia and neurons. Given similarities of the lesions in the mice to human neuronal and glial inclusions, these transgenic mice appear to be a valuable model to study pathogenesis of the neurodegenerative tauopathies.

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“…Filaments from familial MSTD are most similar to the twisted filaments of CBD although they have a different diameter and periodicity (27,30). By contrast, SFs from PSP are distinct from the twisted filaments of familial MSTD and the SFs from CBD, AD, and Pick disease (22,49). It remains to be established whether the tau bands of 64 and 68 kDa present in PSP and CBD comprise the same tau isoforms as the corresponding bands in familial MSTD.…”

Section: Fig 1 Temporal Cortex From a Familial Mstd Patient Showingmentioning

confidence: 97%

Familial multiple system tauopathy with presenile dementia: A disease with abundant neuronal and glial tau filaments

Spillantini¹,

Goedert

Crowther

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

324

214

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Neurofibrillary lesions made of hyperphosphorylated microtubule-associated protein tau constitute not only one of the defining neuropathological features of Alzheimer disease but also are present in a number of other neurodegenerative diseases with dementia. Here we describe a novel autosomal dominant disease named familial ''multiple system tauopathy with presenile dementia,'' which is characterized by abundant fibrillary deposits of tau protein in both neurons and glial cells. There are no detectable deposits of ␤-amyloid. The tau deposits are in the form of twisted filaments that differ in diameter and periodicity from the paired helical filaments of Alzheimer disease. They are stained by both phosphorylation-independent and -dependent anti-tau antibodies. Moreover, tau immunoreactivity coexists with heparan sulfate in affected nerve and glial cells. Tau protein extracted from filaments of familial multiple system tauopathy with presenile dementia shows a minor 72-kDa band and two major bands of 64 and 68 kDa that contain mainly hyperphosphorylated four-repeat tau isoforms of 383 and 412 amino acids.

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Neuropathologic Overlap of Progressive Supranuclear Palsy, Pickʼs Disease and Corticobasal Degeneration

Cited by 250 publications

References 0 publications

Phosphorylation of specific sets of tau isoforms reflects different neurofibrillary degeneration processes

Phosphorylation of specific sets of tau isoforms reflects different neurofibrillary degeneration processes

Filamentous Tau in Oligodendrocytes and Astrocytes of Transgenic Mice Expressing the Human Tau Isoform with the P301L Mutation

Familial multiple system tauopathy with presenile dementia: A disease with abundant neuronal and glial tau filaments

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