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Prion and autophagy

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https://www.readbyqxmd.com/read/29720937/the-nlrp3-caspase-1-inflammasome-negatively-regulates-autophagy-via-tlr4-trif-in-prion-peptide-infected-microglia
#1
Mengyu Lai, Hao Yao, Syed Zahid Ali Shah, Wei Wu, Di Wang, Ying Zhao, Lu Wang, Xiangmei Zhou, Deming Zhao, Lifeng Yang
Prion diseases are neurodegenerative disorders characterized by the accumulation of misfolded prion protein, spongiform changes in the brain, and brain inflammation as a result of the wide-spread activation of microglia. Autophagy is a highly conserved catabolic process for the clearance of cytoplasmic components, including protein aggregates and damaged organelles; this process also eliminates pathological PrPSc as it accumulates during prion infection. The NALP3 inflammasome is a multiprotein complex that is a component of the innate immune system and is responsible for the release of pro-inflammatory cytokines...
2018: Frontiers in Aging Neuroscience
https://www.readbyqxmd.com/read/29700113/autophagy-regulates-exosomal-release-of-prions-in-neuronal-cells
#2
Basant A Abdulrahman, Dalia H Abdelaziz, Hermann M Schatzl
Prions are protein-based infectious agents that autocatalytically convert the cellular prion protein PrPC to its pathological isoform PrPSc Subsequent aggregation and accumulation of PrPSc in nervous tissues causes several invariably fatal neurodegenerative diseases in humans and animals. Prions can infect recipient cells when packaged into endosome-derived nanoparticles called exosomes, which are present in biological fluids such as blood, urine, and saliva. Autophagy is a basic cellular degradation and recycling machinery that also affects exosomal processing, but whether autophagy controls release of prions in exosomes is unclear...
April 26, 2018: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/29416016/pharmacological-activation-of-autophagy-favors-the-clearing-of-intracellular-aggregates-of-misfolded-prion-protein-peptide-to-prevent-neuronal-death
#3
Stefano Thellung, Beatrice Scoti, Alessandro Corsaro, Valentina Villa, Mario Nizzari, Maria Cristina Gagliani, Carola Porcile, Claudio Russo, Aldo Pagano, Carlo Tacchetti, Katia Cortese, Tullio Florio
According to the "gain-of-toxicity mechanism", neuronal loss during cerebral proteinopathies is caused by accumulation of aggregation-prone conformers of misfolded cellular proteins, although it is still debated which aggregation state actually corresponds to the neurotoxic entity. Autophagy, originally described as a variant of programmed cell death, is now emerging as a crucial mechanism for cell survival in response to a variety of cell stressors, including nutrient deprivation, damage of cytoplasmic organelles, or accumulation of misfolded proteins...
February 7, 2018: Cell Death & Disease
https://www.readbyqxmd.com/read/29361800/heat-shock-proteins-and-autophagy-pathways-in-neuroprotection-from-molecular-bases-to-pharmacological-interventions
#4
REVIEW
Botond Penke, Ferenc Bogár, Tim Crul, Miklós Sántha, Melinda E Tóth, László Vígh
Neurodegenerative diseases (NDDs) such as Alzheimer's disease, Parkinson's disease and Huntington's disease (HD), amyotrophic lateral sclerosis, and prion diseases are all characterized by the accumulation of protein aggregates (amyloids) into inclusions and/or plaques. The ubiquitous presence of amyloids in NDDs suggests the involvement of disturbed protein homeostasis (proteostasis) in the underlying pathomechanisms. This review summarizes specific mechanisms that maintain proteostasis, including molecular chaperons, the ubiquitin-proteasome system (UPS), endoplasmic reticulum associated degradation (ERAD), and different autophagic pathways (chaperon mediated-, micro-, and macro-autophagy)...
January 22, 2018: International Journal of Molecular Sciences
https://www.readbyqxmd.com/read/29242534/the-celecoxib-derivatives-ar-12-and-ar-14-induce-autophagy-and-clear-prion-infected-cells-from-prions
#5
Basant A Abdulrahman, Dalia Abdelaziz, Simrika Thapa, Li Lu, Shubha Jain, Sabine Gilch, Stefan Proniuk, Alexander Zukiwski, Hermann M Schatzl
Prion diseases are fatal infectious neurodegenerative disorders that affect both humans and animals. The autocatalytic conversion of the cellular prion protein (PrPC ) into the pathologic isoform PrPSc is a key feature in prion pathogenesis. AR-12 is an IND-approved derivative of celecoxib that demonstrated preclinical activity against several microbial diseases. Recently, AR-12 has been shown to facilitate clearance of misfolded proteins. The latter proposes AR-12 to be a potential therapeutic agent for neurodegenerative disorders...
December 14, 2017: Scientific Reports
https://www.readbyqxmd.com/read/29184404/autophagic-flux-induced-by-graphene-oxide-has-a-neuroprotective-effect-against-human-prion-protein-fragments
#6
Jae-Kyo Jeong, You-Jin Lee, Seung Yol Jeong, Sooyeon Jeong, Geon-Woong Lee, Sang-Youel Park
Graphene oxide (GO) is a nanomaterial with newly developing biological applications. Autophagy is an intracellular degradation system that has been associated with the progression of neurodegenerative disorders. Although induction of autophagic flux by GO has been reported, the underlying signaling pathway in neurodegenerative disorders and how this is involved in neuroprotection remain obscure. We show that GO itself activates autophagic flux in neuronal cells and confers a neuroprotective effect against prion protein (PrP) (106-126)-mediated neurotoxicity...
2017: International Journal of Nanomedicine
https://www.readbyqxmd.com/read/29038292/proteolysis-suppresses-spontaneous-prion-generation-in-yeast
#7
Atsushi Okamoto, Nao Hosoda, Anri Tanaka, Gary P Newnam, Yury O Chernoff, Shin-Ichi Hoshino
Prions are infectious proteins that cause fatal neurodegenerative disorders including Creutzfeldt-Jakob and bovine spongiform encephalopathy (mad cow) diseases. The yeast [ PSI + ] prion is formed by the translation-termination factor Sup35, is the best-studied prion, and provides a useful model system for studying such diseases. However, despite recent progress in the understanding of prion diseases, the cellular defense mechanism against prions has not been elucidated. Here, we report that proteolytic cleavage of Sup35 suppresses spontaneous de novo generation of the [ PSI + ] prion...
December 8, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28903070/role-of-the-ampk-pathway-in-promoting-autophagic-flux-via-modulating-mitochondrial-dynamics-in-neurodegenerative-diseases-insight-into-prion-diseases
#8
REVIEW
Syed Zahid Ali Shah, Deming Zhao, Tariq Hussain, Lifeng Yang
Neurons are highly energy demanding cells dependent on the mitochondrial oxidative phosphorylation system. Mitochondria generate energy via respiratory complexes that constitute the electron transport chain. Adenosine triphosphate depletion or glucose starvation act as a trigger for the activation of adenosine monophosphate-activated protein kinase (AMPK). AMPK is an evolutionarily conserved protein that plays an important role in cell survival and organismal longevity through modulation of energy homeostasis and autophagy...
November 2017: Ageing Research Reviews
https://www.readbyqxmd.com/read/28869476/pazopanib-reduces-phosphorylated-tau-levels-and-alters-astrocytes-in-a-mouse-model-of-tauopathy
#9
Monica Javidnia, Michaeline L Hebron, Yue Xin, Nikolas G Kinney, Charbel E-H Moussa
Hyperphosphorylation and aggregation of tau protein is a critical factor in many neurodegenerative diseases. These diseases are increasing in prevalence, and there are currently no cures. Previous work from our group and others has shown that tyrosine kinase inhibitors (TKIs) can stimulate autophagy, decrease pathological proteins, and improve symptoms in models of neurodegeneration. Here we examined the role of pazopanib in mouse models that express either human mutant P301L tau (TauP301L) or triple mutant amyloid precursor protein (3x-AβPP)...
2017: Journal of Alzheimer's Disease: JAD
https://www.readbyqxmd.com/read/28842471/isgylation-a-key-to-lock-the-cell-gates-for-preventing-the-spread-of-threats
#10
REVIEW
Carolina Villarroya-Beltri, Susana Guerra, Francisco Sánchez-Madrid
Interferon stimulated gene 15 (ISG15) is an ubiquitin-like protein whose expression and conjugation to targets (ISGylation) is induced by infection, interferon (IFN)-α and -β, ischemia, DNA damage and aging. Attention has historically focused on the antiviral effects of ISGylation, which blocks the entry, replication or release of different intracellular pathogens. However, recently, new functions of ISGylation have emerged that implicate it in multiple cellular processes, such as DNA repair, autophagy, protein translation and exosome secretion...
September 15, 2017: Journal of Cell Science
https://www.readbyqxmd.com/read/28832529/assessment-of-autophagy-in-neurons-and-brain-tissue
#11
REVIEW
Irene Benito-Cuesta, Héctor Diez, Lara Ordoñez, Francisco Wandosell
Autophagy is a complex process that controls the transport of cytoplasmic components into lysosomes for degradation. This highly conserved proteolytic system involves dynamic and complex processes, using similar molecular elements and machinery from yeast to humans. Moreover, autophagic dysfunction may contribute to a broad spectrum of mammalian diseases. Indeed, in adult tissues, where the capacity for regeneration or cell division is low or absent (e.g., in the mammalian brain), the accumulation of proteins/peptides that would otherwise be recycled or destroyed may have pathological implications...
August 23, 2017: Cells
https://www.readbyqxmd.com/read/28790319/novel-animal-model-defines-genetic-contributions-for-neuron-to-neuron-transfer-of-%C3%AE-synuclein
#12
Trevor Tyson, Megan Senchuk, Jason F Cooper, Sonia George, Jeremy M Van Raamsdonk, Patrik Brundin
Cell-to-cell spreading of misfolded α-synuclein (α-syn) is suggested to contribute to the progression of neuropathology in Parkinson's disease (PD). Compelling evidence supports the hypothesis that misfolded α-syn transmits from neuron-to-neuron and seeds aggregation of the protein in the recipient cells. Furthermore, α-syn frequently appears to propagate in the brains of PD patients following a stereotypic pattern consistent with progressive spreading along anatomical pathways. We have generated a C. elegans model that mirrors this progression and allows us to monitor α-syn neuron-to-neuron transmission in a live animal over its lifespan...
August 8, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28715601/methamphetamine-increases-prion-protein-and-induces-dopamine-dependent-expression-of-protease-resistant-prpsc
#13
M Ferrucci, L Ryskalin, F Biagioni, S Gambardella, C L Busceti, A Falleni, G Lazzeri, F Fornai
The cellular prion protein (PrPc) is physiologically expressed within selective brain areas of mammals. Alterations in the secondary structure of this protein lead to scrapie-like prion protein (PrPsc), which precipitates in the cell. PrPsc has been detected in infectious, inherited or sporadic neurodegenerative disorders. Prion protein metabolism is dependent on autophagy and ubiquitin proteasome. Despite not being fully elucidated, the physiological role of prion protein relates to chaperones which rescue cells under stressful conditions...
July 1, 2017: Archives Italiennes de Biologie
https://www.readbyqxmd.com/read/28449707/altered-ca-2-homeostasis-induces-calpain-cathepsin-axis-activation-in-sporadic-creutzfeldt-jakob-disease
#14
Franc Llorens, Katrin Thüne, Beata Sikorska, Matthias Schmitz, Waqas Tahir, Natalia Fernández-Borges, Maria Cramm, Nadine Gotzmann, Margarita Carmona, Nathalie Streichenberger, Uwe Michel, Saima Zafar, Anna-Lena Schuetz, Ashish Rajput, Olivier Andréoletti, Stefan Bonn, Andre Fischer, Pawel P Liberski, Juan Maria Torres, Isidre Ferrer, Inga Zerr
Sporadic Creutzfeldt-Jakob disease (sCJD) is the most prevalent form of human prion disease and it is characterized by the presence of neuronal loss, spongiform degeneration, chronic inflammation and the accumulation of misfolded and pathogenic prion protein (PrPSc ). The molecular mechanisms underlying these alterations are largely unknown, but the presence of intracellular neuronal calcium (Ca2+ ) overload, a general feature in models of prion diseases, is suggested to play a key role in prion pathogenesis...
April 27, 2017: Acta Neuropathologica Communications
https://www.readbyqxmd.com/read/28435839/the-frequency-of-yeast-psi-prion-formation-is-increased-during-chronological-ageing
#15
Shaun H Speldewinde, Chris M Grant
Ageing involves a time-dependent decline in a variety of intracellular mechanisms and is associated with cellular senescence. This can be exacerbated by prion diseases which can occur in a sporadic manner, predominantly during the later stages of life. Prions are infectious, self-templating proteins responsible for several neurodegenerative diseases in mammals and several prion-forming proteins have been found in yeast. We show here that the frequency of formation of the yeast [PSI(+) ] prion, which is the altered form of the Sup35 translation termination factor, is increased during chronological ageing...
March 27, 2017: Microbial Cell
https://www.readbyqxmd.com/read/28428740/protein-quality-control-by-molecular-chaperones-in-neurodegeneration
#16
REVIEW
Aaron Ciechanover, Yong Tae Kwon
Protein homeostasis (proteostasis) requires the timely degradation of misfolded proteins and their aggregates by protein quality control (PQC), of which molecular chaperones are an essential component. Compared with other cell types, PQC in neurons is particularly challenging because they have a unique cellular structure with long extensions. Making it worse, neurons are postmitotic, i.e., cannot dilute toxic substances by division, and, thus, are highly sensitive to misfolded proteins, especially as they age...
2017: Frontiers in Neuroscience
https://www.readbyqxmd.com/read/28413194/dual-role-of-cellular-prion-protein-in-normal-host-and-alzheimer-s-disease
#17
REVIEW
Takashi Onodera
Using PrP(C)-knockout cell lines, it has been shown that the inhibition of apoptosis through STI1 is mediated by PrP(C)-dependent SOD activation. Antioxidant PrP(C) may contribute to suppression of inflammasome activation. PrP(C) is functionally involved in copper metabolism, signal transduction, neuroprotection, and cell maturation. Recently several reports have shown that PrP(C) participates in trans-membrane signaling processes associated with hematopoietic stem cell replication and neuronal differentiation...
2017: Proceedings of the Japan Academy. Series B, Physical and Biological Sciences
https://www.readbyqxmd.com/read/28077650/melanin-or-a-melanin-like-substance-interacts-with-the-n-terminal-portion-of-prion-protein-and-inhibits-abnormal-prion-protein-formation-in-prion-infected-cells
#18
Taichi Hamanaka, Keiko Nishizawa, Yuji Sakasegawa, Ayumi Oguma, Kenta Teruya, Hiroshi Kurahashi, Hideyuki Hara, Suehiro Sakaguchi, Katsumi Doh-Ura
Prion diseases are progressive fatal neurodegenerative illnesses caused by the accumulation of transmissible abnormal prion protein (PrP). To find treatments for prion diseases, we searched for substances from natural resources that inhibit abnormal PrP formation in prion-infected cells. We found that high-molecular-weight components from insect cuticle extracts reduced abnormal PrP levels. The chemical nature of these components was consistent with that of melanin. In fact, synthetic melanin produced from tyrosine or 3-hydroxy-l-tyrosine inhibited abnormal PrP formation...
March 15, 2017: Journal of Virology
https://www.readbyqxmd.com/read/27911875/autophagy-flux-induced-by-ginsenoside-rg3-attenuates-human-prion-protein-mediated-neurotoxicity-and-mitochondrial-dysfunction
#19
Ji-Hong Moon, Ju-Hee Lee, You-Jin Lee, Sang-Youel Park
Mitochondrial quality control is a process by which mitochondria undergo successive rounds of fusion and fission with dynamic exchange of components to segregate functional and damaged elements. Removal of mitochondrion that contains damaged components is accomplished via autophagy. In this study, we investigated whether ginsenoside Rg3, an active ingredient of the herbal medicine ginseng that is used as a tonic and restorative agent, could attenuate prion peptide, PrP (106-126)-induced neurotoxicity and mitochondrial damage...
December 27, 2016: Oncotarget
https://www.readbyqxmd.com/read/27702699/targeting-chaperones-heat-shock-factor-1-and-unfolded-protein-response-promising-therapeutic-approaches-for-neurodegenerative-disorders
#20
REVIEW
Shambhunath Bose, Jungsook Cho
Protein misfolding, which is known to cause several serious diseases, is an emerging field that addresses multiple therapeutic areas. Misfolding of a disease-specific protein in the central nervous system ultimately results in the formation of toxic aggregates that may accumulate in the brain, leading to neuronal cell death and dysfunction, and associated clinical manifestations. A large number of neurodegenerative diseases in humans, including Alzheimer's, Parkinson's, Huntington's, and prion diseases, are primarily caused by protein misfolding and aggregation...
May 2017: Ageing Research Reviews
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