Immunocytochemical and ultrastructural studies of Pick's disease

Murayama, Shigeo; Mori, Hiroshi; Ihara, Yasuo; Tomonaga, Masanori

doi:10.1002/ana.410270407

Cited by 134 publications

(55 citation statements)

References 34 publications

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“…The DF2 immunoreactivity of Lewy bodies led us to search for similar DF2-positive inclusions, and we found that Lewy-like bodies in motor neurons in amyotrophic lateral sclerosis (ALS; Murayama et al 1990a) and Pick bodies in Pick's disease (Murayama et al 1990b) were strongly reactive; the latter stained also for tau, whereas the former stained neither for tau nor a-synuclein. In this regard, the entity of frontotemporal lobar degeneration (FTLD) with Ub-positive/tau-negative inclusions was described later, and TDP43 was identified as the ubiquitinated protein in both this disorder and ALS (Neuman et al 2006).…”

Section: Ubiquitination Of Other Neuropathological Inclusionsmentioning

confidence: 99%

The Ubiquitin-Proteasome System and the Autophagic-Lysosomal System in Alzheimer Disease

Ihara¹,

Morishima-Kawashima²,

Nixon³

2012

Cold Spring Harbor Perspectives in Medicine

152

126

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As neurons age, their survival depends on eliminating a growing burden of damaged, potentially toxic proteins and organelles-a capability that declines owing to aging and disease factors. Here, we review the two proteolytic systems principally responsible for protein quality control in neurons and their important contributions to Alzheimer disease pathogenesis. In the first section, the discovery of paired helical filament ubiquitination is described as a backdrop for discussing the importance of the ubiquitin-proteasome system in Alzheimer disease. In the second section, we review the prominent involvement of the lysosomal system beginning with pathological endosomal-lysosomal activation and signaling at the very earliest stages of Alzheimer disease followed by the progressive failure of autophagy. These abnormalities, which result in part from Alzheimer-related genes acting directly on these lysosomal pathways, contribute to the development of each of the Alzheimer neuropathological hallmarks and represent a promising therapeutic target.

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Section: Ubiquitination Of Other Neuropathological Inclusionsmentioning

confidence: 99%

The Ubiquitin-Proteasome System and the Autophagic-Lysosomal System in Alzheimer Disease

Ihara¹,

Morishima-Kawashima²,

Nixon³

2012

Cold Spring Harbor Perspectives in Medicine

152

126

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“…Tau-positive neurofibrillary lesions also are found in progressive supranuclear palsy (PSP) (22)(23)(24), corticobasal degeneration (CBD) (25)(26)(27)(28)(29)(30), and Pick disease (31,32). However, the morphology of tau-positive filaments in these diseases differs from that of PHFs and SFs (33).…”

mentioning

confidence: 99%

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.

319

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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“…Abnormal, fibrillary forms of tau proteins known as paired helical filaments (PHFs), accumulate in the brains of individuals affected with AD (Kidd, 1963;Grundke-Iqbal et al, 1986) and certain other neurodegenerative disorders (Trojanowski et al, 1993), including corticobasal degeneration (Feany et al, 1995), progressive supranuclear palsy (Flament et al, 1991), and Pick's disease (Murayama et al, 1990;Delacourte et al, 1996). The pathologic accumulation of PHFs could be the result of impairments in proteolytic degradation pathways in these various neurodegenerative disorders.…”

mentioning

confidence: 99%

Tau Released from Paired Helical Filaments with Formic Acid or Guanidine Is Susceptible to Calpain‐Mediated Proteolysis

Ling

Gordon‐Krajcer

Księżak-Reding

1997

Journal of Neurochemistry

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Paired helical filaments (PHFs), a characteristic neuropathologic finding in Alzheimer's disease brain, are abnormal fibrillary forms of hyperphosphorylated tau (PHF-tau), which have been shown to be highly resistant to calpain digestion. Either excessive phosphorylation or fibrillary arrangement of tau proteins in PHFs may play a role in proteolytic resistance by limiting access to calpain recognition/digestion sites. To determine the contribution of the fibrillary conformation, isolated PHFs were subjected to treatment with either formic acid or guanidine. Both procedures effectively abolished the fibrillary structure of PHF but preserved PHF-tau immunoreactivity using a panel of antibodies that recognize nonphosphorylated and phosphorylated epitopes. These treatments also significantly increased the sensitivity of PHF-tau polypeptides to calpain proteolysis as shown by significant decreases in the half-life (t 112) from the infinite with native PHF to 44 min and 4.4 min in formic acid-or guanidine-treated samples, respectively. In contrast, the sensitivity of normal fetal tau (3.4 mm) was either decreased (5.9 mm) or unaffected (3.6 mm) by similar treatment. Our results indicate that after guanidine treatment, the sensitivity of PHF to calpain resembles that of fetal tau. These results strongly suggest that the fibrillary structure of PHF-tau, rather than hyperphosphorylation, is the major factor responsible for the resistance of abnormal filaments to calpain-mediated proteolysis.

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Immunocytochemical and ultrastructural studies of Pick's disease

Cited by 134 publications

References 34 publications

The Ubiquitin-Proteasome System and the Autophagic-Lysosomal System in Alzheimer Disease

The Ubiquitin-Proteasome System and the Autophagic-Lysosomal System in Alzheimer Disease

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

Tau Released from Paired Helical Filaments with Formic Acid or Guanidine Is Susceptible to Calpain‐Mediated Proteolysis

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