Cellular co-localization of phosphorylated tau- and NACP/α-synuclein-epitopes in Lewy bodies in sporadic Parkinson's disease and in dementia with Lewy bodies

@article{Arima1999CellularCO,
  title={Cellular co-localization of phosphorylated tau- and NACP/$\alpha$-synuclein-epitopes in Lewy bodies in sporadic Parkinson's disease and in dementia with Lewy bodies},
  author={Kunimasa Arima and Shigeo Hirai and Nobuhiko Sunohara and Kazuko Aoto and Yoko Izumiyama and Kenji U{\'e}da and Kazuhiko Ikeda and Mitsuru Kawai},
  journal={Brain Research},
  year={1999},
  volume={843},
  pages={53-61}
}
The precursor of the non-Abeta-component of Alzheimer's disease (AD) amyloid (NACP, alpha-synuclein) aggregates into insoluble filaments of Lewy bodies (LBs) in Parkinson's disease (PD) and dementia with LBs (DLB). The microtubule-associated protein tau is an integral component of filaments of neurofibrillary tangles (NFTs). NFTs are occasionally found in brains of PD and DLB; however, the presence of NFTs or tau-epitopes within LB-containing neurons is rare. Double-immunofluorescence study and… Expand
Co-localization of α-synuclein and phosphorylated tau in neuronal and glial cytoplasmic inclusions in a patient with multiple system atrophy of long duration
TLDR
It is considered that the limbic system can be a major site of neurodegeneration in MSA of long duration, as some α-synuclein filaments were decorated with phosphorylated tau without formation of fibrils such as paired helical filaments. Expand
Phosphorylation of tau and α-synuclein in synaptic-enriched fractions of the frontal cortex in Alzheimer’s disease, and in Parkinson’s disease and related α-synucleinopathies
TLDR
Early tau phosphorylation at the synapses in AD is indicated before the occurrence of neurofibrillary tangles in the frontal cortex, indicating synapses are targets of abnormal tau and alpha-synucleinosphorylation in both groups of diseases. Expand
Mutant ubiquitin and p62 immunoreactivity in cases of combined multiple system atrophy and Alzheimer’s disease
TLDR
It is indicated that α-synuclein and phosphorylated tau co-occur in certain brain regions in cases of combined MSA and AD and that the proteasomal pathways differ between α- synuclein- and pTau-bearing neurons. Expand
Relationship in the formation process between neurofibrillary tangles and Lewy bodies in the hippocampus of dementia with Lewy bodies brains
TLDR
It is suggested that NFT and LB are first formed in the CA2 and the CA3-4 related to degeneration of the nonperforating route of the perforant pathway, respectively, and subsequently in the subiculum-pre-CA1 chiefly related to disintegration of thePerforant route. Expand
Tau in the Pathophysiology of Parkinson’s Disease
TLDR
The structure and function of Tau are discussed and a summary of the current evidence supporting Tau’s involvement as either an active or passive element in the pathophysiology of PD is provided, which may provide novel targets for the early diagnosis and treatment of PD. Expand
α-Synuclein-positive structures in cases with sporadic Alzheimer’s disease: morphology and its relationship to tau aggregation
TLDR
The suggestion that cases with AD pathology can be classified into two groups according to the existence or absence of alpha-synuclein aggregation is supported. Expand
Microtubule-associated Protein 1B Is a Component of Cortical Lewy Bodies and Binds α-Synuclein Filaments*
TLDR
Microtubule-associated protein 1B (MAP-1B) may be involved in the pathogenesis of Lewy bodies via its interaction with monomeric and fibrillar α-synuclein. Expand
Amyloid-Beta Peptides Trigger Aggregation of Alpha-Synuclein In Vitro
TLDR
Observations imply a cross-talk of the amyloid peptides α-synuclein and Aβ species in neurodegeneration, which might be responsible for the co-occurrence of Lewy bodies and plaques in many dementia cases. Expand
α‐Synuclein‐positive structures in association with diffuse neurofibrillary tangles with calcification
TLDR
The findings suggest that the accumulation pattern of α− Synuclein is a pathological feature of DNTC, and that DNTC is associated with accumulation of both tau and α−synuclein. Expand
Tau and α-Synuclein Pathology in Amygdala of Parkinsonism-Dementia Complex Patients of Guam
TLDR
The amygdala may be selectively vulnerable to developing both tau and α-synuclein pathology or tau pathology may predispose it to synuclein aggregation, thereby implicating the aggregation of these molecules in the severe neurodegeneration frequently observed in this location. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 29 REFERENCES
Immunoelectron-microscopic demonstration of NACP/α-synuclein-epitopes on the filamentous component of Lewy bodies in Parkinson's disease and in dementia with Lewy bodies
TLDR
The present study indicates that the entire molecule of NACP is involved in the neuronal filament-aggregating processes of LB disorders. Expand
Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies.
TLDR
Western blot analyses of highly purified LBs from DLB brains showed that full-length as well as partially truncated and insoluble aggregates of alpha-synuclein are deposited in LBs, which strongly implicate alpha- Synuclein in the formation of LBs and the selective degeneration of neurons in sporadic PD and DLB. Expand
Abnormal accumulation of NACP/alpha-synuclein in neurodegenerative disorders.
TLDR
The view that NACP specifically accumulates in diseases related to Lewy bodies such as Lewy body variant of Alzheimer's disease, diffuseLewy body disease, and Parkinson's disease is supported and suggests a role for this synaptic protein in the pathogenesis of neurodegeneration. Expand
NACP, a presynaptic protein, immunoreactivity in Lewy bodies in Parkinson's disease
TLDR
Findings suggest that alteration of NACP metabolism is involved in the pathogenesis of PD, particularly in Lewy body formation, leading to neurodegeneration. Expand
Lewy bodies contain altered alpha-synuclein in brains of many familial Alzheimer's disease patients with mutations in presenilin and amyloid precursor protein genes.
TLDR
It is suggested that insoluble alpha-synuclein aggregates into filaments that form LBs in many FAD patients, and it is speculated that these inclusions may compromise the function and/or viability of affected neurons in the FAD brain. Expand
α-Synuclein in filamentous inclusions of Lewy bodies from Parkinson’s disease and dementia with Lewy bodies
Lewy bodies and Lewy neurites are the defining neuropathological characteristics of Parkinson’s disease and dementia with Lewy bodies. They are made of abnormal filamentous assemblies of unknownExpand
Senile dementia of Lewy body type and Alzheimer type are biochemically distinct in terms of paired helical filaments and hyperphosphorylated tau protein.
TLDR
These findings provide molecular support for the neuropathological and clinical separation of SDLT as a form of dementia that is distinct from AD. Expand
NACP/α-synuclein immunoreactivity in fibrillary components of neuronal and oligodendroglial cytoplasmic inclusions in the pontine nuclei in multiple system atrophy
TLDR
It is demonstrated that NACP is associated with cytoplasmic inclusions of MSA, and a role of NACP in abnormal filament aggregation in neuronal degeneration is suggested. Expand
The precursor protein of non-Aβ component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system
TLDR
NACP sequence showed 95% identity with that of rat synuclein 1, a synaptic/nuclear protein previously identified in rat brain, and good homology with Torpedo syn DNA from the electric organ synapse and bovine phosphoneuroprotein 14 (PNP-14), a brain-specific protein present in synapses, suggesting that synaptic aberration observed in senile plaques might be involved in amyloidogenesis in Alzheimer's disease. Expand
Accumulation of cyclin-dependent kinase 5 (cdk5) in neurons with early stages of Alzheimer's disease neurofibrillary degeneration
TLDR
Findings suggest that this kinase might be involved in the formation of NFTs at a relatively early stage in the neocortex. Expand
...
1
2
3
...