Significant association of cadaveric dura mater grafting with subpial Aβ deposition and meningeal amyloid angiopathy

Hamaguchi, Tetsuya; Taniguchi, Yu; Sakai, Kenji; Kitamoto, Tetsuyuki; Takao, Masaki; Murayama, Shigeo; Iwasaki, Yasushi; Yoshida, Mari; Shimizu, Hiroshi; Kakita, Akiyoshi; Takahashi, Hitoshi; Suzuki, Hiroyoshi; Naiki, Hironobu; Sanjo, Nobuo; Mizusawa, Hidehiro; Yamada, Masahito

doi:10.1007/s00401-016-1588-3

Cited by 62 publications

(53 citation statements)

References 6 publications

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“…A fourth study has been recently reported from Japan 29 . They did not find a higher frequency in iatrogenic CJD as compared to sporadic CJD; however, their study included elderly patients (up to 81 years).…”

Section: Introductionmentioning

confidence: 91%

“…The youngest iatrogenic CJD cases did show more Aβ than the youngest sporadic CJD cases. The study demonstrated significant association of cadaveric dura mater grafting with subpial Aβ deposition and meningeal amyloid angiopathy using the anti-Aβ antibody 4G8 29 . They discussed the possibility that Aβ pathology propagated from the superficial portions of the brain in the patients with iatrogenic CJD 29 .…”

Section: Introductionmentioning

confidence: 99%

“…The study demonstrated significant association of cadaveric dura mater grafting with subpial Aβ deposition and meningeal amyloid angiopathy using the anti-Aβ antibody 4G8 29 . They discussed the possibility that Aβ pathology propagated from the superficial portions of the brain in the patients with iatrogenic CJD 29 . The immunohistochemical studies were performed only on sections of the frontal, parietal, temporal, and occipital lobes and it was not clear how the Aβ deposits related to the site of the surgical intervention.…”

Section: Introductionmentioning

confidence: 99%

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Can Creutzfeldt-Jakob disease unravel the mysteries of Alzheimer?

Kovács

2016

Prion

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Recent studies on iatrogenic Creutzfeldt-Jakob disease (CJD) raised concerns that one of the hallmark lesions of Alzheimer disease (AD), amyloid-β (Aβ), may be transmitted from human-to-human. The neuropathology of AD-related lesions is complex. Therefore, many aspects need to be considered in deciding on this issue. Observations of recent studies can be summarized as follows: 1) The frequency of iatrogenic CJD cases with parencyhmal and vascular Aβ deposits is statistically higher than expected; 2) The morphology and distribution of Aβ deposition may show distinct features; 3) The pituitary and the dura mater themselves may serve as potential sources of Aβ seeds; 4) Cadaveric dura mater from 2 examined cases shows Aβ deposition; and 5) There is a lack of evidence that the clinical phenotype of AD appears following the application of cadaveric pituitary hormone or dura mater transplantation. These studies support the notion that neurodegenerative diseases have common features regarding propagation of disease-associated proteins as seeds. However, until further evidence emerges, prions of transmissible spongiform encephalopathies are the only neurodegenerative disease-related proteins proven to propagate clinicopathological phenotypes.

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Section: Introductionmentioning

confidence: 91%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Can Creutzfeldt-Jakob disease unravel the mysteries of Alzheimer?

Kovács

2016

Prion

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“…L'étude des lots d'hormone produits à l'époque à l'aide de différentes approches serait, si elle s'avérait possible, essentielle au débat. distribution des lésions chez les patients décédés de MCJ iatrogène après greffe de dure-mère est particulière : répartition des plaques selon un axe perpendiculaire à la surface piale dans une étude autrichienne , fréquence plus élevée des dépôts sous-piaux dans une étude japonaise (Hamaguchi et al, 2016 (Eisele et al, 2010). Il serait, à ce stade, prématuré de conclure à une transmission de la MA puisque la pathologie observée chez ces patients n'associe pas une pathologie tau aux lésions bêta amyloïdes et qu'il n'est pas possible de prédire le devenir clinique de ces patients.…”

Section: Protéinopathies Non-prion Chez Les Patients Décédés De Maladunclassified

Transmission interhumaine des protéinopathies du système nerveux central : les données disponibles en 2016

Haı̈k¹

2017

bavf

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Bien des maladies neurodégénératives, qu’elles soient d’origine génétique ou sporadique, s’accompagnent de la formation d’agrégats d’une ou plusieurs protéines spécifiques qui forment des inclusions intracellulaires (neuronales ou gliales, cytoplasmiques ou nucléaires) ou des dépôts extra-cellulaires (volontiers sous la forme de plaques amyloïdes). Les recherches menées ces 10 dernières années ont apporté des arguments neuropathologiques et expérimentaux en faveur d’une propagation à la manière des prions de ces structures protéiques, suggérant que certaines maladies conformationelles comme les maladies d’Alzheimer et de Parkinson puissent être transmissibles. Cette question de l’infectiosité potentielle des maladies neurodégénératives chez l’homme, qui a, au-delà de leur nosologie, des conséquences en santé publique et sur la gestion du risque en laboratoire, est discutée à la lumière des données les plus récentes.

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“…Increasing evidence from experimental studies has indicated that misfolded aggregated proteins in these diseases have prion-like properties: They propagate through neuronal networks or other pathways in the CNS of individuals and also cause interindividual transmission of these diseases. In human studies, neurodegeneration seems to progress along the neuronal networks by propagation of protein aggregates in the CNS, although evidence for human-to-human transmission is still limited (4,5).…”

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confidence: 99%

The sulfation code for propagation of neurodegeneration

Yamada

Hamaguchi

2018

Journal of Biological Chemistry

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Edited by Paul E. Fraser Prion-like propagation of protein aggregates is thought to be an essential feature in many neurodegenerative diseases, but the mechanisms underlying transcellular transfer of protein aggregates remain unclear. Stopschinski et al. now demonstrate that the cellular uptake of tau, A␤, and ␣-synuclein aggregates mediated by heparan sulfate proteoglycans (HSPGs) varies with distinct glycosaminoglycan chain length and sulfation patterns. The results help us to understand how different protein aggregates propagate, leading to distinct neurodegenerative pathologies.Prion diseases are a group of fatal transmissible neurodegenerative diseases characterized by the accumulation of an abnormal form of prion protein (PrP Sc ) in the central nervous system (CNS).2 Prion diseases are transmissible interindividually, crossing even species barriers, and propagate intraindividually. Similar to prion diseases, many neurodegenerative diseases are also characterized by the accumulation of abnormal proteins in the CNS including ␤-amyloid protein (A␤) and tau in Alzheimer's disease (AD), tau in non-AD tauopathies, ␣-synuclein in Lewy body diseases such as Parkinson's disease and dementia with Lewy bodies, and transactive response DNAbinding protein 43 kDa (TDP-43) in frontotemporal dementia and amyotrophic lateral sclerosis (1-3). Increasing evidence from experimental studies has indicated that misfolded aggregated proteins in these diseases have prion-like properties: They propagate through neuronal networks or other pathways in the CNS of individuals and also cause interindividual transmission of these diseases. In human studies, neurodegeneration seems to progress along the neuronal networks by propagation of protein aggregates in the CNS, although evidence for human-to-human transmission is still limited (4, 5).For intercellular propagation of intracellular protein aggregates, release of aggregates from donor cells and uptake of aggregates by recipient cells are essential steps, followed by intracellular seeding in the recipient cells. In transcellular transfer of protein aggregates, multiple mechanisms have been proposed: 1) extracellular vesicles like exosomes and ectosomes reaching the cytoplasm of recipient cells by fusion, 2) free protein aggregates exocytosed from donor cells taken up by recipient cells with receptor-or nonreceptor-mediated endocytosis/macropinocytosis, and 3) transfer through nanotubes, although it remains unclear which is the main mechanism for transcellular transfer of certain protein aggregates in certain areas of the CNS.Diamond and colleagues (6) have focused on heparan sulfate proteoglycans (HSPGs) on the cell surface as receptors for uptake of protein aggregates such as A␤, tau, and ␣-synuclein. They previously observed that cellular uptake and consequent intracellular seeding of tau and ␣-synuclein fibrils require HSPGs, similar to results from another study (7). Inhibition of the interaction with HSPGs blocked transcellular aggregate propagation, indicating that the interact...

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Significant association of cadaveric dura mater grafting with subpial Aβ deposition and meningeal amyloid angiopathy

Cited by 62 publications

References 6 publications

Can Creutzfeldt-Jakob disease unravel the mysteries of Alzheimer?

Can Creutzfeldt-Jakob disease unravel the mysteries of Alzheimer?

Transmission interhumaine des protéinopathies du système nerveux central : les données disponibles en 2016

The sulfation code for propagation of neurodegeneration

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