keyword
MENU ▼
Read by QxMD icon Read
search

alzheimer's disease prion diseases

keyword
https://www.readbyqxmd.com/read/28811866/preliminary-data-on-the-interaction-between-some-biometals-and-oxidative-stress-status-in-mild-cognitive-impairment-and-alzheimer-s-disease-patients
#1
Ioana-Miruna Balmuș, Stefan-Adrian Strungaru, Alin Ciobica, Mircea-Nicusor Nicoara, Romeo Dobrin, Gabriel Plavan, Cristinel Ștefănescu
Increased interest regarding the biometal mechanisms of action and the pathways in which they have regulatory roles was lately observed. Particularly, it was shown that biometal homeostasis dysregulation may lead to neurodegeneration including Alzheimer's disease, Parkinson disease, or prion protein disease, since important molecular signaling mechanisms in brain functions implicate both oxidative stress and redox active biometals. Oxidative stress could be a result of a breakdown in metal-ion homeostasis which leads to abnormal metal protein chelation...
2017: Oxidative Medicine and Cellular Longevity
https://www.readbyqxmd.com/read/28811267/app-a%C3%AE-structural-diversity-and-alzheimer-s-disease-pathogenesis
#2
REVIEW
Alex E Roher, Tyler A Kokjohn, Steven G Clarke, Michael R Sierks, Chera L Maarouf, Geidy E Serrano, Marwan S Sabbagh, Thomas G Beach
The amyloid cascade hypothesis of Alzheimer's disease (AD) proposes amyloid- β (Aβ) is a chief pathological element of dementia. AD therapies have targeted monomeric and oligomeric Aβ 1-40 and 1-42 peptides. However, alternative APP proteolytic processing produces a complex roster of Aβ species. In addition, Aβ peptides are subject to extensive posttranslational modification (PTM). We propose that amplified production of some APP/Aβ species, perhaps exacerbated by differential gene expression and reduced peptide degradation, creates a diverse spectrum of modified species which disrupt brain homeostasis and accelerate AD neurodegeneration...
August 12, 2017: Neurochemistry International
https://www.readbyqxmd.com/read/28797122/cross-seeding-of-prions-by-aggregated-%C3%AE-synuclein-leads-to-transmissible-spongiform-encephalopathy
#3
Elizaveta Katorcha, Natallia Makarava, Young Jin Lee, Iris Lindberg, Mervyn J Monteiro, Gabor G Kovacs, Ilia V Baskakov
Aggregation of misfolded proteins or peptides is a common feature of neurodegenerative diseases including Alzheimer's, Parkinson's, Huntington's, prion and other diseases. Recent years have witnessed a growing number of reports of overlap in neuropathological features that were once thought to be unique to only one neurodegenerative disorder. However, the origin for the overlap remains unclear. One possibility is that diseases with mixed brain pathologies might arise from cross-seeding of one amyloidogenic protein by aggregated states of unrelated proteins...
August 10, 2017: PLoS Pathogens
https://www.readbyqxmd.com/read/28783058/evolution-of-diagnostic-tests-for-chronic-wasting-disease-a-naturally-occurring-prion-disease-of-cervids
#4
REVIEW
Nicholas J Haley, Jürgen A Richt
Since chronic wasting disease (CWD) was first identified nearly 50 years ago in a captive mule deer herd in the Rocky Mountains of the United States, it has slowly spread across North America through the natural and anthropogenic movement of cervids and their carcasses. As the endemic areas have expanded, so has the need for rapid, sensitive, and cost effective diagnostic tests-especially those which take advantage of samples collected antemortem. Over the past two decades, strategies have evolved from the recognition of microscopic spongiform pathology and associated immunohistochemical staining of the misfolded prion protein to enzyme-linked immunoassays capable of detecting the abnormal prion conformer in postmortem samples...
August 5, 2017: Pathogens
https://www.readbyqxmd.com/read/28768713/a-meta-analysis-and-review-examining-a-possible-role-for-oxidative-stress-and-singlet-oxygen-in-diverse-diseases
#5
REVIEW
Athinoula L Petrou, Athina Terzidaki
From kinetic data (k, T) we calculated the thermodynamic parameters for various processes (nucleation, elongation, fibrillization, etc.) of proteinaceous diseases that are related to the β-amyloid protein (Alzheimer's), to tau protein (Alzheimer's, Pick's), to α-synuclein (Parkinson's), prion, amylin (type II diabetes), and to α-crystallin (cataract). Our calculations led to ΔG(≠) values that vary in the range 92.8-127 kJ mol(-1) at 310 K. A value of ∼10-30 kJ mol(-1) is the activation energy for the diffusion of reactants, depending on the reaction and the medium...
August 2, 2017: Biochemical Journal
https://www.readbyqxmd.com/read/28762306/emerging-targets-and-latest-proteomics-based-therapeutic-approaches-in-neurodegenerative-diseases
#6
Munazza Tamkeen Fatima, Zeyaul Islam, Ejaj Ahmad, Parveen Salahuddin
Protein homeostasis (proteostasis) is achieved by the interplay among various components and pathways inside a cell. Dysfunction in proteostasis leads to protein misfolding and aggregation which is ubiquitously associated with many neurodegenerative disorders, although the exact role of these aggregate in the pathogenesis remains unknown. Many neurodegenerative diseases, including Alzheimer's disease, Parkinson's disease, Huntington's disease, amyotrophic lateral sclerosis, and others are characterized by the conversion of specific proteins aggregates into protein inclusions and/or plaques in degenerating brains...
July 31, 2017: Current Protein & Peptide Science
https://www.readbyqxmd.com/read/28760925/the-cholesterol-ester-cycle-regulates-signalling-complexes-and-synapse-damage-caused-by-amyloid-%C3%AE
#7
Ewan West, Craig Osborne, Clive Bate
Cholesterol is required for the formation and function of some signalling platforms. In synaptosomes amyloid-β (Aβ) oligomers, the causative agent in Alzheimer's disease, bind to cellular prion proteins (PrP(C)) resulting in increased cholesterol concentrations, translocation of cytoplasmic phospholipase A2 (cPLA2) to lipid rafts and activation of cPLA2 The formation of Aβ:PrP(C) complexes was controlled by the cholesterol ester cycle. Aβ activated cholesterol ester hydrolases which released cholesterol from stores of cholesterol esters and stabilised Aβ:PrP(C) complexes resulting in activated cPLA2 Conversely, cholesterol esterification reduced cholesterol concentrations causing the dispersal of Aβ:PrP(C) complexes...
July 31, 2017: Journal of Cell Science
https://www.readbyqxmd.com/read/28758631/statins-are-ineffective-at-reducing-neuroinflammation-or-prolonging-survival-in-scrapie-infected-mice
#8
James A Carroll, Brent Race, Katie Phillips, James F Striebel, Bruce Chesebro
Neuroinflammation is a prominent component of several neurodegenerative diseases, including multiple sclerosis, Alzheimer's disease, Parkinson's disease, tauopathies, amyotrophic lateral sclerosis and prion diseases. In such conditions, the ability to decrease neuroinflammation by drug therapy may influence disease progression. Statins have been used to treat hyperlipidemia as well as reduce neuroinflammation and oxidative stress in various tissues. In previous studies, treatment of scrapie-infected mice with the type 1 statins, simvastatin or pravastatin, showed a small beneficial effect on survival time...
July 31, 2017: Journal of General Virology
https://www.readbyqxmd.com/read/28729427/sialylated-glycosylphosphatidylinositols-suppress-the-production-of-toxic-amyloid-%C3%AE-oligomers
#9
William Nolan, Harriet McHale-Owen, Clive Bate
The production of amyloid-β (Aβ) is a key factor driving pathogenesis in Alzheimer's disease (AD). Increasing concentrations of soluble Aβ oligomers within the brain lead to synapse degeneration and the progressive dementia characteristic of AD. Since Aβ exists in both disease-relevant (toxic) and non-toxic forms, the factors that affected the release of toxic Aβ were studied in a cell model. 7PA2 cells expressing the human amyloid precursor protein released Aβ oligomers that caused synapse damage when incubated with cultured neurons...
July 20, 2017: Biochemical Journal
https://www.readbyqxmd.com/read/28724527/the-spread-of-prion-like-proteins-by-lysosomes-and-tunneling-nanotubes-implications-for-neurodegenerative-diseases
#10
REVIEW
Guiliana Soraya Victoria, Chiara Zurzolo
Progression of pathology in neurodegenerative diseases is hypothesized to be a non-cell-autonomous process that may be mediated by the productive spreading of prion-like protein aggregates from a "donor cell" that is the source of misfolded aggregates to an "acceptor cell" in which misfolding is propagated by conversion of the normal protein. Although the proteins involved in the various diseases are unrelated, common pathways appear to be used for their intercellular propagation and spreading. Here, we summarize recent evidence of the molecular mechanisms relevant for the intercellular trafficking of protein aggregates involved in prion, Alzheimer's, Huntington's, and Parkinson's diseases...
July 19, 2017: Journal of Cell Biology
https://www.readbyqxmd.com/read/28710283/amorphous-protein-aggregates-stimulate-plasminogen-activation-leading-to-release-of-cytotoxic-fragments-that-are-clients-for-extracellular-chaperones
#11
Patrick Constantinescu, Rebecca A Brown, Amy R Wyatt, Marie Ranson, Mark R Wilson
The misfolding of proteins and their accumulation in extracellular tissue compartments as insoluble amyloid or amorphous protein aggregates is a hallmark feature of many debilitating protein deposition diseases such as Alzheimers disease, prion diseases and type II diabetes. The plasminogen activation system (PAS) is best known as an extracellular fibrinolytic system, but was previously reported to also be capable of degrading amyloid fibrils. Here we show that amorphous protein aggregates interact with tPA and plasminogen, via an exposed lysine dependent mechanism, to efficiently generate plasmin...
July 14, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28709995/the-contribution-of-biophysical-and-structural-studies-of-protein-self-assembly-to-the-design-of-therapeutic-strategies-for-amyloid-diseases
#12
Nunilo Cremades, Christopher M Dobson
Many neurodegenerative disorders, including Alzheimer's, Parkinson's and the prion diseases, are characterized by a conformational conversion of normally soluble proteins or peptides into pathological species, by a process of misfolding and self-assembly that leads ultimately to the formation of amyloid fibrils. Recent studies support the idea that multiple intermediate species with a wide variety of degrees of neuronal toxicity are generated during such processes. The development of a high level of knowledge of the nature and structure of the pathogenic amyloid species would significantly enhance efforts to underline the molecular origins of these disorders and also to develop both accurate diagnoses and effective therapeutic interventions for these types of conditions...
July 12, 2017: Neurobiology of Disease
https://www.readbyqxmd.com/read/28709498/targeting-fyn-kinase-in-alzheimer-s-disease
#13
REVIEW
Haakon B Nygaard
The past decade has brought tremendous progress in unraveling the pathophysiology of Alzheimer's disease (AD). While increasingly sophisticated immunotherapy targeting soluble and aggregated brain amyloid-beta (Aβ) continues to dominate clinical research in AD, a deeper understanding of Aβ physiology has led to the recognition of distinct neuronal signaling pathways linking Aβ to synaptotoxicity and neurodegeneration and to new targets for therapeutic intervention. Identifying specific signaling pathways involving Aβ has allowed for the development of more precise therapeutic interventions targeting the most relevant molecular mechanisms leading to AD...
June 13, 2017: Biological Psychiatry
https://www.readbyqxmd.com/read/28708131/a-clinicopathological-approach-to-the-diagnosis-of-dementia
#14
REVIEW
Fanny M Elahi, Bruce L Miller
The most definitive classification systems for dementia are based on the underlying pathology which, in turn, is categorized largely according to the observed accumulation of abnormal protein aggregates in neurons and glia. These aggregates perturb molecular processes, cellular functions and, ultimately, cell survival, with ensuing disruption of large-scale neural networks subserving cognitive, behavioural and sensorimotor functions. The functional domains affected and the evolution of deficits in these domains over time serve as footprints that the clinician can trace back with various levels of certainty to the underlying neuropathology...
August 2017: Nature Reviews. Neurology
https://www.readbyqxmd.com/read/28707657/-transmission-of-pathogenic-protein-aggregates-in-alzheimer-s-disease
#15
A L Schwarzman, S V Sarantseva
Deposits of amyloid peptide Aβ and intracellular aggregates of hyperphosphorylated tau protein in the brain of patients are major neuropathological features of Alzheimer's disease (AD). For a long time, the possibility of horizontal transmission of Aβ aggregates from cell to cell and from person to person remained hypothetical, since there was no experimental evidence. However, in 1993, the formation of senile plaques was confirmed in the brains of animals after intracerebral injections of AD patient brain homogenates or homogenates of the brain of transgenic mice enriched with Aβ aggregates...
May 2017: Molekuliarnaia Biologiia
https://www.readbyqxmd.com/read/28702523/implications-of-peptide-assemblies-in-amyloid-diseases
#16
REVIEW
Pu Chun Ke, Marc-Antonie Sani, Feng Ding, Aleksandr Kakinen, Ibrahim Javed, Frances Separovic, Thomas P Davis, Raffaele Mezzenga
Neurodegenerative disorders and type 2 diabetes are global epidemics compromising the quality of life of millions worldwide, with profound social and economic implications. Despite the significant differences in pathology - much of which are poorly understood - these diseases are commonly characterized by the presence of cross-β amyloid fibrils as well as the loss of neuronal or pancreatic β-cells. In this review, we document research progress on the molecular and mesoscopic self-assembly of amyloid-beta, alpha synuclein, human islet amyloid polypeptide and prions, the peptides and proteins associated with Alzheimer's, Parkinson's, type 2 diabetes and prion diseases...
July 12, 2017: Chemical Society Reviews
https://www.readbyqxmd.com/read/28683325/silent-allosteric-modulation-of-mglur5-maintains-glutamate-signaling-while-rescuing-alzheimer-s-mouse-phenotypes
#17
Laura T Haas, Santiago V Salazar, Levi M Smith, Helen R Zhao, Timothy O Cox, Charlotte S Herber, Andrew P Degnan, Anand Balakrishnan, John E Macor, Charles F Albright, Stephen M Strittmatter
Metabotropic glutamate receptor 5 (mGluR5) has been implicated in Alzheimer's disease (AD) pathology. We sought to understand whether mGluR5's role in AD requires glutamate signaling. We used a potent mGluR5 silent allosteric modulator (SAM, BMS-984923) to separate its well-known physiological role in glutamate signaling from a pathological role in mediating amyloid-β oligomer (Aβo) action. Binding of the SAM to mGluR5 does not change glutamate signaling but strongly reduces mGluR5 interaction with cellular prion protein (PrP(C)) bound to Aβo...
July 5, 2017: Cell Reports
https://www.readbyqxmd.com/read/28671123/prion-protein-interactome-identifying-novel-targets-in-slowly-and-rapidly-progressive-forms-of-alzheimer-s-disease
#18
Saima Zafar, Mohsin Shafiq, Neelam Younas, Matthias Schmitz, Isidre Ferrer, Inga Zerr
Rapidly progressive Alzheimer's disease (rpAD) is a variant of AD distinguished by a rapid decline in cognition and short disease duration from onset to death. While attempts to identify rpAD based on biomarker profile classifications have been initiated, the mechanisms which contribute to the rapid decline and prion mimicking heterogeneity in clinical signs are still largely unknown. In this study, we characterized prion protein (PrP) expression, localization, and interactome in rpAD, slow progressive AD, and in non-dementia controls...
2017: Journal of Alzheimer's Disease: JAD
https://www.readbyqxmd.com/read/28670273/types-and-strains-their-essential-role-in-understanding-protein-aggregation-in-neurodegenerative-diseases
#19
REVIEW
Wiebke M Wemheuer, Arne Wrede, Walter J Schulz-Schaeffer
Protein misfolding and aggregation is a key event in diseases like Alzheimer's disease (AD) or Parkinson's disease (PD) and is associated with neurodegeneration. Factors that initiate protein misfolding and the role of protein aggregation in the pathophysiology of disease pose major challenges to the neuroscientific community. Interestingly, although the accumulation of the same misfolded protein, e.g., α-synuclein is detectable in all idiopathic PD patients, the disease spectrum covers a variety of different clinical presentations and disease courses...
2017: Frontiers in Aging Neuroscience
https://www.readbyqxmd.com/read/28657440/a%C3%AE-seeds-and-prions-how-close-the-fit
#20
Jay Rasmussen, Mathias Jucker, Lary C Walker
The prion paradigm is increasingly invoked to explain the molecular pathogenesis of neurodegenerative diseases involving the misfolding and aggregation of proteins other than the prion protein (PrP). Extensive evidence from in vitro and in vivo studies indicates that misfolded and aggregated Aβ peptide, which is the probable molecular trigger for Alzheimer's disease, manifests all of the key characteristics of canonical mammalian prions. These features include a β-sheet rich architecture, tendency to polymerize into amyloid, templated corruption of like protein molecules, ability to form structurally and functionally variant strains, systematic spread by neuronal transport, and resistance to inactivation by heat and formaldehyde...
July 4, 2017: Prion
keyword
keyword
80368
1
2
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"