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Prion and autophagy

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https://www.readbyqxmd.com/read/29038292/proteolysis-suppresses-spontaneous-prion-generation-in-yeast
#1
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-Jacob 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...
October 16, 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
#2
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
#3
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
#4
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
#5
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
#6
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
#7
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
#8
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 (PrP(Sc)). The molecular mechanisms underlying these alterations are largely unknown, but the presence of intracellular neuronal calcium (Ca(2+)) 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
#9
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
#10
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
#11
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
#12
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
#13
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
#14
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
https://www.readbyqxmd.com/read/27689885/prion-aggregates-are-recruited-to-the-insoluble-protein-deposit-ipod-via-myosin-2-based-vesicular-transport
#15
Rajesh Kumar, Peter P Nawroth, Jens Tyedmers
Aggregation of amyloidogenic proteins is associated with several neurodegenerative diseases. Sequestration of misfolded and aggregated proteins into specialized deposition sites may reduce their potentially detrimental properties. Yeast exhibits a distinct deposition site for amyloid aggregates termed "Insoluble PrOtein Deposit (IPOD)", but nothing is known about the mechanism of substrate recruitment to this site. The IPOD is located directly adjacent to the Phagophore Assembly Site (PAS) where the cell initiates autophagy and the Cytoplasm-to-Vacuole Targeting (CVT) pathway destined for delivery of precursor peptidases to the vacuole...
September 2016: PLoS Genetics
https://www.readbyqxmd.com/read/27629560/prnp-prion-protein-regulates-the-secretion-of-exosomes-modulating-cav1-caveolin-1-suppressed-autophagy
#16
Marcos V S Dias, Bianca L Teixeira, Bruna R Rodrigues, Rita Sinigaglia-Coimbra, Isabel Porto-Carreiro, Martín Roffé, Glaucia N M Hajj, Vilma R Martins
Prion protein modulates many cellular functions including the secretion of trophic factors by astrocytes. Some of these factors are found in exosomes, which are formed within multivesicular bodies (MVBs) and secreted into the extracellular space to modulate cell-cell communication. The mechanisms underlying exosome biogenesis were not completely deciphered. Here, we demonstrate that primary cultures of astrocytes and fibroblasts from prnp-null mice secreted lower levels of exosomes than wild-type cells. Furthermore, prnp-null astrocytes exhibited reduced MVB formation and increased autophagosome formation...
November 2016: Autophagy
https://www.readbyqxmd.com/read/27430567/parkin-overexpression-ameliorates-prp106-126-induced-neurotoxicity-via-enhanced-autophagy-in-n2a-cells
#17
Sher Hayat Khan, Deming Zhao, Syed Zahid Ali Shah, Mohammad Farooque Hassan, Ting Zhu, Zhiqi Song, Xiangmei Zhou, Lifeng Yang
Transmissible spongiform encephalopathies (TSEs) are caused by the accumulation of the abnormal prion protein scrapie (PrP(Sc)). Prion protein aggregation, misfolding, and cytotoxicity in the brain are the major causes of neuronal dysfunction and ultimate neurodegeneration in all TSEs. Parkin, an E3 ubiquitin ligase, has been studied extensively in all major protein misfolding aggregating diseases, especially Parkinson's disease and Alzheimer's disease, but the role of parkin in TSEs remains unknown. Here we investigated the role of parkin in a prion disease cell model in which neuroblastoma2a (N2a) cells were treated with prion peptide PrP106-126...
May 2017: Cellular and Molecular Neurobiology
https://www.readbyqxmd.com/read/27413109/from-the-cover-arsenic-induces-accumulation-of-%C3%AE-synuclein-implications-for-synucleinopathies-and-neurodegeneration
#18
Aram B Cholanians, Andy V Phan, Eric J Ditzel, Todd D Camenisch, Serrine S Lau, Terrence J Monks
Synucleinopathies, including Parkinson's disease (PD), are neurodegenerative diseases characterized by accumulation of α-synuclein (SYN), a small neuronal protein with prion like properties that plays a central role in PD pathogenesis. SYN can misfold and generate toxic oligomers/aggregates, which can be cytotoxic. Environmental arsenic (As)-containing pesticide use correlates with increased incidence of PD. Moreover, because As exposure can lead to inhibition of autophagic flux we hypothesize that As can facilitate the accumulation of toxic SYN oligomers/aggregates and subsequent increases in markers of autophagy...
October 2016: Toxicological Sciences: An Official Journal of the Society of Toxicology
https://www.readbyqxmd.com/read/27344333/overexpression-of-plk3-mediates-the-degradation-of-abnormal-prion-proteins-dependent-on-chaperone-mediated-autophagy
#19
Hui Wang, Chan Tian, Jing Sun, Li-Na Chen, Yan Lv, Xiao-Dong Yang, Kang Xiao, Jing Wang, Cao Chen, Qi Shi, Qi-Xiang Shao, Xiao-Ping Dong
Polo-like kinase 3 (PLK3) is the main cause of cell cycle reentry-related neuronal apoptosis which has been implicated in the pathogenesis of prion diseases. Previous work also showed the regulatory activity of exogenous PLK3 on the degradation of PrP (prion protein) mutants and pathogenic PrP(Sc); however, the precise mechanisms remain unknown. In this study, we identified that the overexpression of PLK3-mediated degradation of PrP mutant and PrP(Sc) was repressed by lysosome rather than by proteasomal and macroautophagy inhibitors...
August 2017: Molecular Neurobiology
https://www.readbyqxmd.com/read/27181519/stress-granules-at-the-intersection-of-autophagy-and-als
#20
REVIEW
Zachary Monahan, Frank Shewmaker, Udai Bhan Pandey
Amyotrophic lateral sclerosis (ALS) is a progressive, fatal disease caused by loss of upper and lower motor neurons. The majority of ALS cases are classified as sporadic (80-90%), with the remaining considered familial based on patient history. The last decade has seen a surge in the identification of ALS-causing genes - including TARDBP (TDP-43), FUS, MATR3 (Matrin-3), C9ORF72 and several others - providing important insights into the molecular pathways involved in pathogenesis. Most of the protein products of ALS-linked genes fall into two functional categories: RNA-binding/homeostasis and protein-quality control (i...
October 15, 2016: Brain Research
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