Read by QxMD icon Read

alzheimer's disease prion diseases

Yicai Xiao, Gaofeng Li, Yujie Chen, Yuchun Zuo, Kauthar Rashid, Tibiao He, Hua Feng, John H Zhang, Fei Liu
Iatrogenic brain injury inevitably occurs in neurosurgical operations, leading to brain edema, ischemia, intracranial hematoma, and other postoperative complications, eventually worsening neurological outcomes of patients. If apoptotic cells are not rapidly eliminated by phagocytic engulfment, they may communicate with surrounding cells to undergo secondary necrosis and releasing toxic signals. Recent studies have shown that milk fat globule-epidermal growth factor-8 (MFGE8), which promotes phagocytosis and inhibits inflammation, is an endogenous protective factor in response to brain infarction, Alzheimer's disease, subarachnoid hemorrhage, and prion disease...
2018: Frontiers in Neurology
José A Del Río, Isidre Ferrer, Rosalina Gavín
Several studies have indicated that certain misfolded amyloids composed of tau, β-amyloid or α-synuclein can be transferred from cell to cell, suggesting the contribution of mechanisms reminiscent of those by which infective prions spread through the brain. This process of a 'prion-like' spreading between cells is also relevant as a novel putative therapeutic target that could block the spreading of proteinaceous aggregates throughout the brain which may underlie the progressive nature of neurodegenerative diseases...
March 9, 2018: Progress in Neurobiology
Lisa Seipold, Hermann Altmeppen, Tomas Koudelka, Andreas Tholey, Petr Kasparek, Radislav Sedlacek, Michaela Schweizer, Julia Bär, Marina Mikhaylova, Markus Glatzel, Paul Saftig
A disintegrin and metalloproteinase 10 (ADAM10) plays a major role in the ectodomain shedding of important surface molecules with physiological and pathological relevance including the amyloid precursor protein (APP), the cellular prion protein, and different cadherins. Despite its therapeutic potential, there is still a considerable lack of knowledge how this protease is regulated. We have previously identified tetraspanin15 (Tspan15) as a member of the TspanC8 family to specifically associate with ADAM10...
March 8, 2018: Cellular and Molecular Life Sciences: CMLS
Michael Burwinkel, Manuel Lutzenberger, Frank L Heppner, Walter Schulz-Schaeffer, Michael Baier
Seeding and spread of beta-amyloid (Aβ) pathologies have been considered to be based on prion-like mechanisms. However, limited transmissibility of Aβ seeding activity upon peripheral exposure would represent a key difference to prions, not only in terms of pathogenesis but also in terms of potential transmission of disease. We partially characterized the seeded Aβ amyloidosis after intracerebral injection of various brain homogenates in APP/PS1 mice. One particularly seed-laden homogenate was selected to investigate the development of Aβ pathologies after intravenous exposure...
March 5, 2018: Acta Neuropathologica Communications
Ricardo A S Lima-Filho, Mauricio M Oliveira
No abstract text is available yet for this article.
February 28, 2018: Journal of Neuroscience: the Official Journal of the Society for Neuroscience
Robert M Culik, Ashok Sekhar, Jayashree Nagesh, Harmeen Deol, Jessica A O Rumfeldt, Elizabeth M Meiering, Lewis E Kay
Amyotrophic lateral sclerosis (ALS) is a devastating fatal syndrome characterized by very rapid degeneration of motor neurons. A leading hypothesis is that ALS is caused by toxic protein misfolding and aggregation, as also occurs in many other neurodegenerative disorders, such as prion, Alzheimer's, Parkinson's, and Huntington's diseases. A prominent cause of familial ALS is mutations in the protein superoxide dismutase (SOD1), which promote the formation of misfolded SOD1 conformers that are prone to aberrant interactions both with each other and with other cellular components...
March 13, 2018: Proceedings of the National Academy of Sciences of the United States of America
Nicholas J Haley, Jürgen A Richt, Kristen A Davenport, Davin M Henderson, Edward A Hoover, Matteo Manca, Byron Caughey, Douglas Marthaler, Jason Bartz, Sabine Gilch
Amplification assays for transmissible spongiform encephalopathies have been in development for close to 15 years, with critical implications for the postmortem and antemortem diagnosis of human and animal prion diseases. Little has been published regarding the structured development, implementation and interpretation of experiments making use of protein misfolding cyclic amplification (PMCA) and real time quaking-induced conversion (RT-QuIC), and our goal with this Perspectives manuscript is to offer a framework which might allow for more efficient expansion of pilot studies into diagnostic trials in both human and animal subjects...
February 22, 2018: Prion
Liping Sun, Yong Zhong, Jie Gui, Xianwu Wang, Xiaorong Zhuang, Jian Weng
Background: Alzheimer's disease (AD) is a neurodegenerative disorder characterized by progressive cognitive and memory impairment. It is the most common neurological disease that causes dementia. Soluble amyloid-beta oligomers (AβO) in blood or cerebrospinal fluid (CSF) are the pathogenic biomarker correlated with AD. Methods: A simple electrochemical biosensor using graphene oxide/gold nanoparticles (GNPs) hydrogel electrode was developed in this study. Thiolated cellular prion protein (PrPC ) peptide probe was immobilized on GNPs of the hydrogel electrode to construct an AβO biosensor...
2018: International Journal of Nanomedicine
Erica Corda, Xiaotang Du, Su Yeon Shim, Antonia N Klein, Jessica Siltberg-Liberles, Sabine Gilch
Prion diseases are infectious and fatal neurodegenerative diseases affecting humans and animals. Transmission is possible within and between species with zoonotic potential. Currently, no prophylaxis or treatment exists. Prions are composed of the misfolded isoform PrPSc of the cellular prion protein PrPC . Expression of PrPC is a prerequisite for prion infection, and conformational conversion of PrPC is induced upon its direct interaction with PrPSc . Inhibition of this interaction can abrogate prion propagation, and we have previously established peptide aptamers (PAs) binding to PrPC as new anti-prion compounds...
February 19, 2018: Molecular Neurobiology
Brent Race, Katie Williams, Andrew G Hughson, Casper Jansen, Piero Parchi, Annemieke J M Rozemuller, Bruce Chesebro
Human familial prion diseases are associated with mutations at 34 different prion protein (PrP) amino acid residues. However, it is unclear whether infectious prions are found in all cases. Mutant PrP itself may be neurotoxic, or alternatively, PrP mutation might predispose to spontaneous formation of infectious PrP isoforms. Previous reports demonstrated transmission to animal models by human brain tissue expressing 7 different PrP mutations, but 3 other mutations were not transmissible. In the present work, we tested transmission using brain homogenates from patients expressing 3 untested PrP mutants: G131V, Y226X, and Q227X...
February 20, 2018: Acta Neuropathologica Communications
Daniel Markx, Cornelia Loos, Stephanie Claus, Christian Haupt, Christian Mawrin, Marcus Fändrich
Intracerebral injection of brain extracts from Alzheimer's disease (AD) patients into appropriate mouse models was previously found to drastically accelerate the deposition of Aβ amyloid in the recipient animals indicating a prion-like activity. In this study we show that this prion-like activity can be also identified by using a cell culture model of Aβ plaque formation. Analysis of biochemical fractions of AD brain extract indicate that the seeding-activity correlated with the presence of Aβ peptide and Aβ-derived aggregates...
February 16, 2018: Biochemical and Biophysical Research Communications
Felix Carbonell, Yasser Iturria-Medina, Alan C Evans
Protein misfolding refers to a process where proteins become structurally abnormal and lose their specific 3-dimensional spatial configuration. The histopathological presence of misfolded protein (MP) aggregates has been associated as the primary evidence of multiple neurological diseases, including Prion diseases, Alzheimer's disease, Parkinson's disease, and Creutzfeldt-Jacob disease. However, the exact mechanisms of MP aggregation and propagation, as well as their impact in the long-term patient's clinical condition are still not well understood...
2018: Frontiers in Neurology
Zane Jaunmuktane, Annelies Quaegebeur, Ricardo Taipa, Miguel Viana-Baptista, Raquel Barbosa, Carolin Koriath, Raf Sciot, Simon Mead, Sebastian Brandner
Amyloid-β (Aβ) is a peptide deposited in the brain parenchyma in Alzheimer's disease and in cerebral blood vessels, causing cerebral amyloid angiopathy (CAA). Aβ pathology is transmissible experimentally in animals and through medical procedures in humans, such as contaminated growth hormone or dura mater transplantation in the context of iatrogenic prion disease. Here, we present four patients who underwent neurosurgical procedures during childhood or teenage years and presented with intracerebral haemorrhage approximately three decades later, caused by severe CAA...
February 15, 2018: Acta Neuropathologica
Juan Carlos Polanco, Chuanzhou Li, Nela Durisic, Robert Sullivan, Jürgen Götz
In Alzheimer disease and related disorders, the microtubule-associated protein tau aggregates and forms cytoplasmic lesions that impair neuronal physiology at many levels. In addition to affecting the host neuron, tau aggregates also spread to neighboring, recipient cells where the misfolded tau aggregates, in a manner similar to prions, actively corrupt the proper folding of soluble tau, and thereby impair cellular functions. One vehicle for the transmission of tau aggregates are secretory nanovesicles known as exosomes...
February 15, 2018: Acta Neuropathologica Communications
Brian K Yoo, Yiling Xiao, Dan McElheny, Yoshitaka Ishii
Cross-seeding of misfolded amyloid proteins is believed to induce cross-species infection of prion diseases. In sporadic Alzheimer's disease (AD), misfolding of 42-residue β-amyloid (Aβ) is widely considered to trigger amyloid plaque deposition. Despite increasing evidence that misfolded Aβ mimics prions, interactions of misfolded 42-residue Aβ42 with more abundant 40-residue Aβ40 in AD are elusive. This study presents in-vitro evidence that a heterozygous E22G pathogenic ("Arctic") mutation of Aβ40 can enhance misfolding of Aβ via cross-seeding from wild-type (WT) Aβ42 fibril...
February 9, 2018: Journal of the American Chemical Society
Tomas T Olsson, Oxana Klementieva, Gunnar K Gouras
Alzheimer's disease (AD) brain tissue can act as a seed to accelerate aggregation of amyloid-β (Aβ) into plaques in AD transgenic mice. Aβ seeds have been hypothesized to accelerate plaque formation in a prion-like manner of templated seeding and intercellular propagation. However, the structure(s) and location(s) of the Aβ seeds remain unknown. Moreover, in contrast to tau and α-synuclein, an in vitro system with prion-like Aβ has not been reported. Here we treat human APP expressing N2a cells with AD transgenic mouse brain extracts to induce inclusions of Aβ in a subset of cells...
January 29, 2018: Neurobiology of Disease
A Harrison Brody, Stephen M Strittmatter
Alzheimer's disease (AD) represents an impending global health crisis, yet the complexity of AD pathophysiology has so far precluded the development of any interventions to successfully slow or halt AD progression. It is clear that accumulation of Amyloid-beta (Aβ) peptide triggers progressive synapse loss to cause AD symptoms. Once initiated by Aβ, disease progression is complicated and accelerated by inflammation and by tau pathology. The recognition that Aβ peptide assumes multiple distinct states and that soluble oligomeric species (Aβo) are critical for synaptic damage is central to molecular understanding of AD...
2018: Advances in Pharmacology
Silvia Vanni, Marco Zattoni, Fabio Moda, Giorgio Giaccone, Fabrizio Tagliavini, Stéphane Haïk, Jean-Philippe Deslys, Gianluigi Zanusso, James W Ironside, Margarita Carmona, Isidre Ferrer, Gabor G Kovacs, Giuseppe Legname
Background: Hemoglobin is the major protein found in erythrocytes, where it acts as an oxygen carrier molecule. In recent years, its expression has been reported also in neurons and glial cells, although its role in brain tissue remains still unknown. Altered hemoglobin expression has been associated with various neurodegenerative disorders. Here, we investigated hemoglobin mRNA levels in brains of patients affected by variant, iatrogenic, and sporadic forms of Creutzfeldt-Jakob disease (vCJD, iCJD, sCJD, respectively) and in different genetic forms of prion diseases (gPrD) in comparison to Alzheimer's disease (AD) subjects and age-matched controls...
2018: Frontiers in Neuroscience
Inga Zerr, Matthias Schmitz, André Karch, Anna Villar-Piqué, Eirini Kanata, Ewa Golanska, Daniela Díaz-Lucena, Aikaterini Karsanidou, Peter Hermann, Tobias Knipper, Stefan Goebel, Daniela Varges, Theodoros Sklaviadis, Beata Sikorska, Pawel P Liberski, Isabel Santana, Isidro Ferrer, Henrik Zetterberg, Kaj Blennow, Olga Calero, Miguel Calero, Anna Ladogana, Raquel Sánchez-Valle, Inês Baldeiras, Franc Llorens
INTRODUCTION: Neurofilament light (NFL) levels in the cerebrospinal fluid are increased in several neurodegenerative dementias. However, their diagnostic accuracy in the differential diagnostic context is unknown. METHODS: Cerebrospinal fluid NFL levels were quantified in nonprimarily neurodegenerative neurological and psychiatric diseases (n = 122), mild cognitive impairment (n = 48), Alzheimer's disease (n = 108), dementia with Lewy bodies/Parkinson's disease dementia (n = 53), vascular dementia (n = 46), frontotemporal dementia (n = 41), sporadic Creutzfeldt-Jakob disease (sCJD, n = 132), and genetic prion diseases (n = 182)...
January 29, 2018: Alzheimer's & Dementia: the Journal of the Alzheimer's Association
Masahiro Kawahara, Ken-Ichiro Tanaka, Midori Kato-Negishi
Zinc (Zn) is abundantly present in the brain, and accumulates in the synaptic vesicles. Synaptic Zn is released with neuronal excitation, and plays essential roles in learning and memory. Increasing evidence suggests that the disruption of Zn homeostasis is involved in various neurodegenerative diseases including Alzheimer's disease, a vascular type of dementia, and prion diseases. Our and other numerous studies suggest that carnosine (β-alanyl histidine) is protective against these neurodegenerative diseases...
January 29, 2018: Nutrients
Fetch more papers »
Fetching more papers... Fetching...
Read by QxMD. Sign in or create an account to discover new knowledge that matter to you.
Remove bar
Read by QxMD icon Read

Search Tips

Use Boolean operators: AND/OR

diabetic AND foot
diabetes OR diabetic

Exclude a word using the 'minus' sign

Virchow -triad

Use Parentheses

water AND (cup OR glass)

Add an asterisk (*) at end of a word to include word stems

Neuro* will search for Neurology, Neuroscientist, Neurological, and so on

Use quotes to search for an exact phrase

"primary prevention of cancer"
(heart or cardiac or cardio*) AND arrest -"American Heart Association"