Developmental stages of cortical Lewy bodies and their relation to axonal transport blockage in brains of patients with dementia with Lewy bodies

Katsuse, Omi; Iseki, Eizo; Marui, Wami; Kosaka, Kenji

doi:10.1016/s0022-510x(03)00037-6

Cited by 84 publications

(66 citation statements)

References 32 publications

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“…43 Some pathophysiologic studies have reported morphologic changes associated with DLB. The lack of postmortem evidence of wallerian degeneration in the DLB brain 44 and the presence of widespread spongiform changes and gliosis affecting long projection fibers are a part of DLB pathophysiology. 45 Zaja-Milatovic et al 46,47 reported evidence of spinodendritic degeneration of gamma-aminobutyric acidsergic medium spiny neurons in specific regions of the caudate nucleus.…”

Section: Discussionmentioning

confidence: 99%

Differential Diagnosis of Dementia with Lewy Bodies and Alzheimer Disease Using Combined MR Imaging and Brain Perfusion Single-Photon Emission Tomography

Goto¹,

Ishii²,

Uemura³

et al. 2010

AJNR Am J Neuroradiol

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Section: Discussionmentioning

confidence: 99%

Differential Diagnosis of Dementia with Lewy Bodies and Alzheimer Disease Using Combined MR Imaging and Brain Perfusion Single-Photon Emission Tomography

Goto¹,

Ishii²,

Uemura³

et al. 2010

AJNR Am J Neuroradiol

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“…Redox-active iron Vesicular monoamine transporter 2 (VMAT2) LC3, GABARAP and GATE-16 (autophagosomal proteins) [646] Histone deacetylase 6 (aggresome-related protein) [647] were identified [595], whereas another study identified 1263 proteins in SN [653]. final degradation by astroglial processes [640].…”

Section: Formation and Development Of As/lewy Pathologymentioning

confidence: 99%

The role of α-synuclein in neurodegeneration — An update

Jellinger¹

2012

Translational Neuroscience

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Genetic, neuropathological and biochemical evidence implicates α-synuclein, a 140 amino acid presynaptic neuronal protein, in the pathogenesis of Parkinson's disease and other neurodegenerative disorders. The aggregated protein inclusions mainly containing aberrant α-synuclein are widely accepted as morphological hallmarks of α-synucleinopathies, but their composition and location vary between disorders along with neuronal networks affected. α-Synuclein exists physiologically in both soluble and membran-bound states, in unstructured and α-helical conformations, respectively, while posttranslational modifications due to proteostatic deficits are involved in β-pleated aggregation resulting in formation of typical inclusions. The physiological function of α-synuclein and its role linked to neurodegeneration, however, are incompletely understood. Soluble oligomeric, not fully fibrillar α-synuclein is thought to be neurotoxic, main targets might be the synapse, axons and glia. The effects of aberrant α-synuclein include alterations of calcium homeostasis, mitochondrial dysfunction, oxidative and nitric injuries, cytoskeletal effects, and neuroinflammation. Proteasomal dysfunction might be a common mechanism in the pathogenesis of neuronal degeneration in α-synucleinopathies. However, how α-synuclein induces neurodegeneration remains elusive as its physiological function. Genome wide association studies demonstrated the important role for genetic variants of the SNCA gene encoding α-synuclein in the etiology of Parkinson's disease, possibly through effects on oxidation, mitochondria, autophagy, and lysosomal function. The neuropathology of synucleinopathies and the role of α-synuclein as a potential biomarker are briefly summarized. Although animal models provided new insights into the pathogenesis of Parkinson disease and multiple system atrophy, most of them do not adequately reproduce the cardinal features of these disorders. Emerging evidence, in addition to synergistic interactions of α-synuclein with various pathogenic proteins, suggests that prionlike induction and seeding of α-synuclein could lead to the spread of the pathology and disease progression. Intervention in the early aggregation pathway, aberrant cellular effects, or secretion of α-synuclein might be targets for neuroprotection and disease-modifying therapy.

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“…13 Some authors have suggested that impairment of axonal transport causes accumulation of axonally transported substances followed by cortical Lewy body formation. 14,15 In other words, alterations…”

mentioning

confidence: 99%

Different Functional and Microstructural Changes Depending on Duration of Mild Cognitive Impairment in Parkinson Disease

Shin

Lee³

et al. 2015

American Journal of Neuroradiology

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BACKGROUND AND PURPOSE:The higher cortical burden of Lewy body and Alzheimer disease-type pathology has been reported to be associated with a faster onset of cognitive impairment of Parkinson disease. So far, there has been a few studies only about the changes of gray matter volume depending on duration of cognitive impairment in Parkinson disease. Therefore, our aim was to evaluate the different patterns of structural and functional changes in Parkinson disease with mild cognitive impairment according to the duration of parkinsonism before mild cognitive impairment.

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Developmental stages of cortical Lewy bodies and their relation to axonal transport blockage in brains of patients with dementia with Lewy bodies

Cited by 84 publications

References 32 publications

Differential Diagnosis of Dementia with Lewy Bodies and Alzheimer Disease Using Combined MR Imaging and Brain Perfusion Single-Photon Emission Tomography

Differential Diagnosis of Dementia with Lewy Bodies and Alzheimer Disease Using Combined MR Imaging and Brain Perfusion Single-Photon Emission Tomography

The role of α-synuclein in neurodegeneration — An update

Different Functional and Microstructural Changes Depending on Duration of Mild Cognitive Impairment in Parkinson Disease

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