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alzheimer's disease prion diseases

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https://www.readbyqxmd.com/read/29349578/in-situ-tissue-labeling-of-cerebral-amyloid-using-hiv-related-tat-peptide
#1
E Maderna, L Colombo, A Cagnotto, G Di Fede, A Indaco, F Tagliavini, M Salmona, G Giaccone
Delivering peptide-based drugs to the brain is a major challenge because of the existence of the blood-brain barrier (BBB). To overcome this problem, cell-penetrating peptides derived from proteins that are able to cross biological membranes have been used as cell-permeable and brain-penetrant compounds. An example is the transactivator of transcription protein transduction domain (Tat) of the human immunodeficiency virus. The basic domain of Tat is formed of arginine and lysine amino acid residues. Tat has been used as brain-penetrant carrier also in therapies for Alzheimer disease (AD), the most common form of dementia characterized by extracellular cerebral deposits of amyloid made up of Aβ peptide...
January 19, 2018: Molecular Neurobiology
https://www.readbyqxmd.com/read/29331212/prion-protein-as-a-toxic-acceptor-of-amyloid-%C3%AE-oligomers
#2
REVIEW
Silvia A Purro, Andrew J Nicoll, John Collinge
The initial report that cellular prion protein (PrPC) mediates toxicity of amyloid-β species linked to Alzheimer's disease was initially treated with scepticism, but growing evidence supports this claim. That there is a high-affinity interaction is now clear, and its molecular basis is being unraveled, while recent studies have identified possible downstream toxic mechanisms. Determination of the clinical significance of such interactions between PrPC and disease-associated amyloid-β species will require experimental medicine studies in humans...
February 15, 2018: Biological Psychiatry
https://www.readbyqxmd.com/read/29330303/mammalian-amyloidogenic-proteins-promote-prion-nucleation-in-yeast
#3
Pavithra Chandramowlishwaran, Meng Sun, Kristin L Casey, Andrey V Romanyuk, Anastasiya V Grizel, Julia V Sopova, Aleksandr A Rubel, Carmen Nussbaum-Krammer, Ina M Vorberg, Yury O Chernoff
Fibrous cross-β aggregates (amyloids) and their transmissible forms (prions) cause diseases in mammals (including humans) and control heritable traits in yeast. Initial nucleation of a yeast prion by transiently overproduced prion-forming protein or its (typically, QN-rich) prion domain is efficient only in the presence of another aggregated (in most cases, QN-rich) protein. Here, we demonstrate that a fusion of the prion domain of yeast protein Sup35 to some non-QN-rich mammalian proteins, associated with amyloid diseases, promotes nucleation of Sup35 prions in the absence of preexisting aggregates...
January 12, 2018: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/29311311/structural-heterogeneity-and-intersubject-variability-of-a%C3%AE-in-familial-and-sporadic-alzheimer-s-disease
#4
Carlo Condello, Thomas Lemmin, Jan Stöhr, Mimi Nick, Yibing Wu, Alison M Maxwell, Joel C Watts, Christoffer D Caro, Abby Oehler, C Dirk Keene, Thomas D Bird, Sjoerd G van Duinen, Lars Lannfelt, Martin Ingelsson, Caroline Graff, Kurt Giles, William F DeGrado, Stanley B Prusiner
Point mutations in the amyloid-β (Aβ) coding region produce a combination of mutant and WT Aβ isoforms that yield unique clinicopathologies in familial Alzheimer's disease (fAD) and cerebral amyloid angiopathy (fCAA) patients. Here, we report a method to investigate the structural variability of amyloid deposits found in fAD, fCAA, and sporadic AD (sAD). Using this approach, we demonstrate that mutant Aβ determines WT Aβ conformation through prion template-directed misfolding. Using principal component analysis of multiple structure-sensitive fluorescent amyloid-binding dyes, we assessed the conformational variability of Aβ deposits in fAD, fCAA, and sAD patients...
January 8, 2018: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/29310723/iatrogenic-creutzfeldt-jakob-disease-with-amyloid-%C3%AE-pathology-an-international-study
#5
Ignazio Cali, Mark L Cohen, Stéphane Haїk, Piero Parchi, Giorgio Giaccone, Steven J Collins, Diane Kofskey, Han Wang, Catriona A McLean, Jean-Philippe Brandel, Nicolas Privat, Véronique Sazdovitch, Charles Duyckaerts, Tetsuyuki Kitamoto, Ermias D Belay, Ryan A Maddox, Fabrizio Tagliavini, Maurizio Pocchiari, Ellen Leschek, Brian S Appleby, Jiri G Safar, Lawrence B Schonberger, Pierluigi Gambetti
The presence of pathology related to the deposition of amyloid-β (Aβ) has been recently reported in iatrogenic Creutzfeldt-Jakob disease (iCJD) acquired from inoculation of growth hormone (GH) extracted from human cadaveric pituitary gland or use of cadaveric dura mater (DM) grafts.To investigate this phenomenon further, a cohort of 27 iCJD cases - 21 with adequate number of histopathological sections - originating from Australia, France, Italy, and the Unites States, were examined by immunohistochemistry, amyloid staining, and Western blot analysis of the scrapie prion protein (PrPSc), and compared with age-group matched cases of sporadic CJD (sCJD), Alzheimer disease (AD) or free of neurodegenerative diseases (non-ND)...
January 8, 2018: Acta Neuropathologica Communications
https://www.readbyqxmd.com/read/29303785/mechanisms-of-disordered-neurodegenerative-function-concepts-and-facts-about-the-different-roles-of-the-protein-kinase-rna-like-endoplasmic-reticulum-kinase-perk
#6
Yasmeen M Taalab, Nour Ibrahim, Ahmed Maher, Mubashir Hassan, Wael Mohamed, Ahmed A Moustafa, Mohamed Salama, Dina Johar, Larry Bernstein
Neurodegenerative diseases, such as Alzheimer's disease, Huntington's disease, Parkinson's disease, prion disease, and amyotrophic lateral sclerosis, are a dissimilar group of disorders that share a hallmark feature of accumulation of abnormal intraneuronal or extraneuronal misfolded/unfolded protein and are classified as protein misfolding disorders. Cellular and endoplasmic reticulum (ER) stress activates multiple signaling cascades of the unfolded protein response (UPR). Consequently, translational and transcriptional alterations in target gene expression occur in response directed toward restoring the ER capacity of proteostasis and reestablishing the cellular homeostasis...
January 5, 2018: Reviews in the Neurosciences
https://www.readbyqxmd.com/read/29277556/microrna-16-targets-mrna-involved-in-neurite-extension-and-branching-in-hippocampal-neurons-during-presymptomatic-prion-disease
#7
Kristyn Burak, Lise Lamoureux, Amrit Boese, Anna Majer, Reuben Saba, Yulian Niu, Kathy Frost, Stephanie A Booth
The mechanisms that lead to neuronal death in neurodegenerative diseases are poorly understood. Prion diseases, like many more common disorders such as Alzheimer's and Parkinson's diseases, are characterized by the progressive accumulation of misfolded disease-specific proteins. The earliest changes observed in brain tissue include a reduction in synaptic number and retraction of dendritic spines, followed by reduced length and branching of neurites. These pathologies are observable during presymptomatic stages of disease and are accompanied by altered expression of transcripts that include miRNAs...
December 22, 2017: Neurobiology of Disease
https://www.readbyqxmd.com/read/29260852/targeting-the-prion-like-aggregation-of-mutant-p53-to-combat-cancer
#8
Jerson L Silva, Elio A Cino, Iaci N Soares, Vitor F Ferreira, Guilherme A P de Oliveira
Prion-like behavior of several amyloidogenic proteins has been demonstrated in recent years. Despite having functional roles in some cases, irregular aggregation can have devastating consequences. The most commonly known amyloid diseases are Alzheimer's, Parkinson's, and Transmissible Spongiform Encephalopathies (TSEs). The pathophysiology of prion-like diseases involves the structural transformation of wild-type (wt) proteins to transmissible forms that can convert healthy proteins, generating aggregates. The mutant form of tumor suppressor protein, p53, has recently been shown to exhibit prion-like properties...
December 20, 2017: Accounts of Chemical Research
https://www.readbyqxmd.com/read/29259137/distinct-differences-in-prion-like-seeding-and-aggregation-between-tau-protein-variants-provide-mechanistic-insights-into-tauopathies
#9
Kevin H Strang, Cara L Croft, Zachary A Sorrentino, Paramita Chakrabarty, Todd E Golde, Benoit I Giasson
The accumulation of aberrantly aggregated microtubule-associated protein tau (MAPT)1 defines a spectrum of tauopathies, including Alzheimer's disease. Mutations in the MAPT gene cause frontotemporal dementia with Parkinsonism linked to chromosome 17 (FTDP-17), characterized by neuronal pathological tau inclusions in the form of neurofibrillary tangles and Pick bodies, and in some cases glial tau pathology. Increasing evidence points to the importance of prion-like seeding as a mechanism for the pathological spread in tauopathy and other neurodegenerative diseases...
December 19, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/29246602/variable-tau-accumulation-in-murine-models-with-abnormal-prion-protein-deposits
#10
Pedro Piccardo, Declan King, Deborah Brown, Rona M Barron
The conversion of cellular prion protein (PrP) into a misfolded isoform is central to the development of prion diseases. However, the heterogeneous phenotypes observed in prion disease may be linked with the presence of other misfolded proteins in the brain. While hyperphosphorylated tau (p.tau) is characteristic of Alzheimer's disease (AD), p.tau is also observed in human prion diseases. To explore this association in the absence of potential effects due to aging, drug treatment, agonal stage and postmortem delay we analyzed p...
December 15, 2017: Journal of the Neurological Sciences
https://www.readbyqxmd.com/read/29238218/breaking-the-cycle-cholesterol-cycling-and-synapse-damage-in-response-to-amyloid-%C3%AE
#11
Clive Bate
Soluble amyloid-β (Aβ) oligomers, a key driver of pathogenesis in Alzheimer disease, bind to cellular prion proteins (PrPC) expressed on synaptosomes resulting in increased cholesterol concentrations, movement of cytoplasmic phospholipase A2 (cPLA2) to lipid rafts and activation of cPLA2. The formation of Aβ-PrPC-cPLA2 complexes was controlled by the cholesterol ester cycle. Thus, Aβ activated cholesterol ester hydrolases which released cholesterol from stores of cholesterol esters; the increased cholesterol concentrations stabilised Aβ-PrPC-cPLA2 complexes...
2017: Journal of Experimental Neuroscience
https://www.readbyqxmd.com/read/29237931/tau-mediated-neurodegeneration-and-potential-implications-in-diagnosis-and-treatment-of-alzheimer-s-disease
#12
REVIEW
Xi-Lin Wu, Juan Piña-Crespo, Yun-Wu Zhang, Xiao-Chun Chen, Hua-Xi Xu
OBJECTIVE: To review recent research advances on tau, a major player in Alzheimer's disease (AD) pathogenesis, a biomarker for AD onset, and potential target for AD therapy. DATA SOURCES: This review was based on a comprehensive search using online literature databases, including PubMed, Web of Science, and Google Scholar. STUDY SELECTION: Literature search was based on the following keywords: Alzheimer's disease, tau protein, biomarker, cerebrospinal fluid (CSF), therapeutics, plasma, imaging, propagation, spreading, seeding, prion, conformational templating, and posttranslational modification...
December 20, 2017: Chinese Medical Journal
https://www.readbyqxmd.com/read/29237120/ultrafast-time-resolved-studies-on-fluorescein-for-recognition-strands-architecture-in-amyloid-fibrils
#13
Piotr Hanczyc, Alexander A Mikhailovsky, David R Boyer, Michael R Sawaya, Alan J Heeger, David Eisenberg
Protein aggregation is associated with numerous devastating diseases such as Alzheimer's, Parkinson's, and prion diseases. Development of therapeutics would benefit from knowledge of the structural organization of protein molecules in these amyloid aggregates, particularly in their aqueous biological milieu. However, detailed structural studies to date have been mainly on the solid state, and have required large quantities of purified aggregate. Moreover, these conventional methods require the aggregated assembly to remain structurally stable over days or weeks required to perform the experiment, whereas the pathologically relevant species of in vivo aggregates may be shorter lived...
December 13, 2017: Journal of Physical Chemistry. B
https://www.readbyqxmd.com/read/29229786/seed-induced-a%C3%AE-deposition-is-modulated-by-microglia-under-environmental-enrichment-in-a-mouse-model-of-alzheimer-s-disease
#14
Stephanie Ziegler-Waldkirch, Paolo D Errico, Jonas-Frederic Sauer, Daniel Erny, Shakuntala Savanthrapadian, Desirée Loreth, Natalie Katzmarski, Thomas Blank, Marlene Bartos, Marco Prinz, Melanie Meyer-Luehmann
Alzheimer's disease (AD) is characterized by severe neuronal loss as well as the accumulation of amyloid-β (Aβ), which ultimately leads to plaque formation. Although there is now a general agreement that the aggregation of Aβ can be initiated by prion-like seeding, the impact and functional consequences of induced Aβ deposits (Aβ seeding) on neurons still remain open questions. Here, we find that Aβ seeding, representing early stages of plaque formation, leads to a dramatic decrease in proliferation and neurogenesis in two APP transgenic mouse models...
December 11, 2017: EMBO Journal
https://www.readbyqxmd.com/read/29227178/neuronal-pathophysiology-featuring-prpc-and-its-control-over-ca2-metabolism
#15
Alessandro Bertoli, M Catia Sorgato
Calcium (Ca2+) is an intracellular second messenger that ubiquitously masters remarkably diverse biological processes, including cell death. Growing evidence substantiates an involvement of the prion protein (PrPC) in regulating neuronal Ca2+ homeostasis, which could rationalize most of the wide range of functions ascribed to the protein. We have recently demonstrated that PrPC controls extracellular Ca2+ fluxes, and mitochondrial Ca2+ uptake, in neurons stimulated with glutamate (De Mario et al., J Cell Sci 2017; 130:2736-46), suggesting that PrPC protects neurons from threatening Ca2+ overloads and excitotoxicity...
December 11, 2017: Prion
https://www.readbyqxmd.com/read/29226873/modeling-prion-like-processing-of%C3%A2-tau%C3%A2-protein-in-alzheimer-s-disease-for%C3%A2-pharmaceutical-development
#16
Claude M Wischik, Björn O Schelter, Damon J Wischik, John M D Storey, Charles R Harrington
 Following our discovery of a fragment from the repeat domain of tau protein as a structural constituent of the PHF-core in Alzheimer's disease (AD), we developed an assay that captured several key features of the aggregation process. Tau-tau binding through the core tau fragment could be blocked by the same diaminophenothiazines found to dissolve proteolytically stable PHFs isolated from AD brain. We found that the PHF-core tau fragment is inherently capable of auto-catalytic self-propagation in vitro, or "prion-like processing", that has now been demonstrated for several neurodegenerative disorders...
December 8, 2017: Journal of Alzheimer's Disease: JAD
https://www.readbyqxmd.com/read/29214587/rare-neurodegenerative-diseases-clinical-and-genetic-update
#17
Antoni Matilla-Dueñas, Marc Corral-Juan, Agustí Rodríguez-Palmero Seuma, Dolores Vilas, Lourdes Ispierto, Sara Morais, Jorge Sequeiros, Isabel Alonso, Víctor Volpini, Carmen Serrano-Munuera, Guillem Pintos-Morell, Ramiro Álvarez, Ivelisse Sánchez
More than 600 human disorders afflict the nervous system. Of these, neurodegenerative diseases are usually characterised by onset in late adulthood, progressive clinical course, and neuronal loss with regional specificity in the central nervous system. They include Alzheimer's disease and other less frequent dementias, brain cancer, degenerative nerve diseases, encephalitis, epilepsy, genetic brain disorders, head and brain malformations, hydrocephalus, stroke, Parkinson's disease, multiple sclerosis, amyotrophic lateral sclerosis (ALS or Lou Gehrig's Disease), Huntington's disease, and Prion diseases, among others...
2017: Advances in Experimental Medicine and Biology
https://www.readbyqxmd.com/read/29203673/evidence-for-sortilin-modulating-regional-accumulation-of-human-tau-prions-in-transgenic-mice
#18
Noah R Johnson, Carlo Condello, Shenheng Guan, Abby Oehler, Julia Becker, Marta Gavidia, George A Carlson, Kurt Giles, Stanley B Prusiner
Misfolding of tau proteins into prions and their propagation along neural circuits are thought to result in neurodegeneration causing Alzheimer's disease, progressive supranuclear palsy, chronic traumatic encephalopathy, and other tauopathies. Little is known about the molecular processes mediating tau prion replication and spreading in different brain regions. Using transgenic (Tg) mice with a neuronal promoter driving expression of human mutant (P301S) tau, we found that tau prion formation and histopathologic deposition is largely restricted to the hindbrain...
December 4, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/29202042/relative-impact-of-complement-receptors-cd21-35-cr2-1-on-scrapie-pathogenesis-in-mice
#19
Sarah J Kane, Eric Swanson, Elizabeth O Gordon, Savannah Rocha, Heather R Bender, Luke R Donius, Adriano Aguzzi, Jonathan P Hannan, Mark D Zabel
Complement receptors 1 and 2 (CR1/2 or CD35/CD21) recognize complement-opsonized antigens to initiate innate and adaptive immunity, respectively. CD35 stimulates phagocytosis on macrophages and antigen presentation on follicular dendritic cells (FDCs). CD21 helps activate B cells as part of the B cell coreceptor with CD19 and CD81. Differential splicing of transcripts from the mouse Cr2 gene generates isoforms with both shared and unique complement binding capacities and cell-type expression. In mouse models, genetic depletion of Cr2 causes either a delay or complete prevention of prion disease, but the relative importance of CD35 versus CD21 in promoting prion disease remains unknown...
November 2017: MSphere
https://www.readbyqxmd.com/read/29187283/new-insights-into-transglutaminase-2-and-links-to-neurodegenerative-diseases
#20
Boram Min, Kwang Chul Chung
Formation of toxic protein aggregates is a common feature and mainly contributes to the pathogenesis of neurodegenerative diseases (NDDs), which include amyotrophic lateral sclerosis (ALS), Alzheimer's, Parkinson's, Huntington's, and prion diseases. The transglutaminase 2 (TG2) gene encodes a multifunctional enzyme, displaying four types of activity, such as transamidation, GTPase, protein disulfide isomerase, and protein kinase activities. Many studies demonstrated that the calcium-dependent transamidation activity of TG2 affected the formation of insoluble and toxic amyloid aggregates that mainly consisted of NDD-related proteins...
November 29, 2017: BMB Reports
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