Molecular Chaperones and Protein Folding As Therapeutic Targets in Parkinson's Disease and Other Synucleinopathies PDF Download
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Author: Applied Research Applied Research Press
Publisher: CreateSpace
ISBN: 9781516822478
Category :
Languages : en
Pages : 44
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Book Description
Changes in protein metabolism are key to disease onset and progression in many neurodegenerative diseases. As a prime example, in Parkinson's disease, folding, post-translational modification and recycling of the synaptic protein alpha-synuclein are clearly altered, leading to a progressive accumulation of pathogenic protein species and the formation of intracellular inclusion bodies. Altered protein folding is one of the first steps of an increasingly understood cascade in which alpha-synuclein forms complex oligomers and finally distinct protein aggregates, termed Lewy bodies and Lewy neurites. In neurons, an elaborated network of chaperone and co-chaperone proteins is instrumental in mediating protein folding and re-folding. In addition to their direct influence on client proteins, chaperones interact with protein degradation pathways such as the ubiquitin-proteasome-system or autophagy in order to ensure the effective removal of irreversibly misfolded and potentially pathogenic proteins. Because of the vital role of proper protein folding for protein homeostasis, a growing number of studies have evaluated the contribution of chaperone proteins to neurodegeneration. We herein review our current understanding of the involvement of chaperones, co-chaperones and chaperone-mediated autophagy in synucleinopathies with a focus on the Hsp90 and Hsp70 chaperone system. We discuss genetic and pathological studies in Parkinson's disease as well as experimental studies in models of synucleinopathies that explore molecular chaperones and protein degradation pathways as a novel therapeutic target. To this end, we examine the capacity of chaperones to prevent or modulate neurodegeneration and summarize the current progress in models of Parkinson's disease and related neurodegenerative disorders.
Author: Applied Research Applied Research Press
Publisher: CreateSpace
ISBN: 9781516822478
Category :
Languages : en
Pages : 44
Get Book Here
Book Description
Changes in protein metabolism are key to disease onset and progression in many neurodegenerative diseases. As a prime example, in Parkinson's disease, folding, post-translational modification and recycling of the synaptic protein alpha-synuclein are clearly altered, leading to a progressive accumulation of pathogenic protein species and the formation of intracellular inclusion bodies. Altered protein folding is one of the first steps of an increasingly understood cascade in which alpha-synuclein forms complex oligomers and finally distinct protein aggregates, termed Lewy bodies and Lewy neurites. In neurons, an elaborated network of chaperone and co-chaperone proteins is instrumental in mediating protein folding and re-folding. In addition to their direct influence on client proteins, chaperones interact with protein degradation pathways such as the ubiquitin-proteasome-system or autophagy in order to ensure the effective removal of irreversibly misfolded and potentially pathogenic proteins. Because of the vital role of proper protein folding for protein homeostasis, a growing number of studies have evaluated the contribution of chaperone proteins to neurodegeneration. We herein review our current understanding of the involvement of chaperones, co-chaperones and chaperone-mediated autophagy in synucleinopathies with a focus on the Hsp90 and Hsp70 chaperone system. We discuss genetic and pathological studies in Parkinson's disease as well as experimental studies in models of synucleinopathies that explore molecular chaperones and protein degradation pathways as a novel therapeutic target. To this end, we examine the capacity of chaperones to prevent or modulate neurodegeneration and summarize the current progress in models of Parkinson's disease and related neurodegenerative disorders.
Author: Stephan N. Witt
Publisher: John Wiley & Sons
ISBN: 1118063899
Category : Science
Languages : en
Pages : 516
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Book Description
How protein chaperones protect cells from neurodegenerative diseases Including contributions from leading experts, Protein Chaperones and Protection from Neurodegenerative Diseases provides an in-depth exploration of how protein chaperones are involved in shielding cells from toxic aggregated or misfolded protein states that cause ALS, Parkinson's, and related diseases. Examining how different protein chaperones ameliorate the toxicity of proteins that are known to cause neurodegenerative damage, the book addresses both research and clinical perspectives on chaperone and anti-chaperone properties. The intersection of molecular chaperones and neurodegeneration is an intensely studied area, partly because of the potential for manipulating the expression of molecular chaperones to thwart the progression of debilitating diseases, and partly because of the ever-aging global population. Discussing the potential to harness the power of protein chaperones, and future directions for research, discovery, and therapeutics, this book is essential reading for scientists working in the fields of biochemistry, molecular medicine, pharmacology and drug discovery, biotechnology and pharmaceutical companies, advanced students, and anyone interested in this cutting-edge topic.
Author: Chaari Ali
Publisher: LAP Lambert Academic Publishing
ISBN: 9783659517242
Category :
Languages : en
Pages : 64
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Book Description
Protein misfolding and amyloid formation is an underlying pathological hallmark in a number of prevalent diseases of protein aggregation, including Parkinson's disease (PD), Alzheimer's disease and Type 2 diabetes. Most importantly, the severity of these diseases appears to correlate with the degree of the deposition of amyloid aggregates. The misfolding of -synuclein, a protein involved in PD, followed by its aggregation has been shown to be highly cytotoxic and to play a key role in the death of neurons. Thus, the modulation of the aggregation process, promoting the proper folding of -synuclein, may be considered as an attractive avenue for a therapeutic intervention. Indeed, molecular chaperones have been shown to assist in the maintenance of a functional proteome in vivo and to prevent protein misfolding, aggregation and amyloid formation."
Author: Robert D. E. Sewell
Publisher: CRC Press
ISBN: 9780849373107
Category : Science
Languages : en
Pages : 0
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Book Description
Research focused on protein folding, misfolding, and aggregation is leading to major advances across biochemistry and medicine. The elucidation of a folding code is proving to be of extreme importance in the postgenomic era, where a number of orphan genes have been identified for which no clear function has yet been established. This research is starting to shed light on the molecular and biochemical basis of a number of neurodegenerative diseases of dramatic impact. Protein Misfolding in Neurodegenerative Diseases: Mechanisms and Therapeutic Strategies addresses key issues concerning protein misfolding and aggregation in neurodegenerative diseases. Building on recent developments, including the recognition of protein misfolding as both a marker and a causal agent, the text presents the work of those who are actively pursuing more effective treatments, as well as preventative measures, and a possible cure. These include the use of molecular chaperones to control misfolding and novel pharmaceuticals, as well as the potential role of various inhibitors and NSAIDS. A Comprehensive Multifaceted Examination of the Complex Causal Agents Implicated in Protein Misfolding Divided into five sections, this groundbreaking text provides up-to-date accounts for Alzheimer’s, Parkinson’s, Huntington’s, Amyotrophic Lateral Sclerosis and Transmissible Spongiform Encephalitis. It also explores the highly likelihood that multiple factors, including oxidative stress, play a role in these complex diseases.
Author: Applied Research Applied Research Press
Publisher:
ISBN: 9781517765194
Category :
Languages : en
Pages : 118
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Book Description
This book contains open access research articles from December of 2013 published in Acta Neuropathologica Communications. Topics include: Myositis facilitates preclinical accumulation of pathological prion protein in muscle; Molecular chaperones and protein folding as therapeutic targets in Parkinson's disease and other synucleinopathies; Genetic CJD with a novel E200G mutation in the prion protein gene and comparison with E200K mutation cases; Heavy metals in locus ceruleus and motor neurons in motor neuron disease; Impaired plasticity of cortical dendritic spines in P301S tau transgenic mice; A central role for dityrosine crosslinking of Amyloid-beta in Alzheimer's disease; Neurodegeneration progresses despite complete elimination of clinical relapses in a mouse model of multiple sclerosis; T cell-activation in neuromyelitis optica lesions plays a role in their formation.
Author: Colin R Martin
Publisher: Academic Press
ISBN: 0128159596
Category : Medical
Languages : en
Pages : 1548
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Book Description
The Neuroscience of Parkinson’s Disease (two volume set) provides a single source of material covering different scientific domains of neuropathology underlying this condition. The book covers a wide range of subjects and unravels the complex relationships between genetics, molecular biology, pharmaceutical chemistry, neurobiology, imaging, assessments, and treatment regimens. The book also fills a much-needed gap as a "one-stop" synopsis of everything to do with the neurology and neuroscience related to Parkinson’s disease—from chemicals and cells to individuals. It is an invaluable resource for neuroscientists, neurologists, and anyone in the field. Offers the most comprehensive coverage of a broad range of topics related to Parkinson's disease Serves as a foundational collection for neuroscientists and neurologists on the biology of disease and brain dysfunction Contains in each chapter an abstract, key facts, mini dictionary of terms, and summary points to aid in understanding Features preclinical and clinical studies to help researchers map out key areas for research and further clinical recommendations Serves as a "one-stop" source for everything you need to know about Parkinson’s disease
Author: Veerle Baekelandt
Publisher: Academic Press
ISBN: 012805266X
Category : Medical
Languages : en
Pages : 324
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Book Description
Disease-Modifying Targets in Neurodegenerative Disorders: Paving the Way for Disease-Modifying Therapies examines specific neurodegenerative disorders in comprehensive chapters written by experts in the respective fields. Each chapter contains a summary of the disease management field, subsequently elaborating on the molecular mechanisms and promising new targets for disease-modifying therapies. This overview is ideal for neuroscientists, biomedical researchers, medical doctors, and caregivers, not only providing readers with a summary of the way patients are treated today, but also offering a glance at the future of neurodegenerative disorder treatment. Provides a comprehensive overview of how key proteins in neurodegenerative disorders can be used as targets to modify disease progress Summarizes how patients are treated today, providing a glance at future disease management Includes intelligible and informative information that is perfect for non-specialists, medical practitioners, and scientists Written and peer reviewed by outstanding scientists in their respective fields
Author: Panayiotis Vlamos
Publisher: Springer
ISBN: 3319573799
Category : Medical
Languages : en
Pages : 307
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Book Description
The 2nd World Congress on Genetics, Geriatrics and Neurodegenerative Disease Research (GeNeDis 2016), will focus on recent advances in geriatrics and neurodegeneration, ranging from basic science to clinical and pharmaceutical developments and will provide an international focum for the latest scientific discoveries, medical practices, and care initiatives. Advances information technologies will be discussed along with their implications for various research, implementation, and policy concerns. In addition, the conference will address European and global issues in the funding of long-term care and medico-social policies regarding elderly people. GeNeDis 2016 takes place in Sparta, Greece, 20-23 October, 2016. This volume focuses on thesessions that address neurodegenerative diseases.
Author: Rodrigo Franco
Publisher: Royal Society of Chemistry
ISBN: 1782621881
Category : Medical
Languages : en
Pages : 537
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Book Description
Parkinson's Disease is the second most common neurodegenerative disorder affecting millions of people worldwide. In order to find neuroprotective strategies, a clear understanding of the mechanisms involved in the dopaminergic death of cells that progresses the disease is needed. Oxidative stress can be defined as an imbalance between the production of reactive species and the ability to detoxify them and their intermediates or by-products. Oxidative damage to lipids, proteins, and DNA has been detected in autopsies from individuals with Parkinson’s Disease and so links can be made between oxidative stress and Parkinson’s Disease pathogenesis. This book provides a thorough review of the mechanisms by which oxidative stress and redox signalling mediate Parkinson’s Disease. Opening chapters bring readers up to speed on basic knowledge regarding oxidative stress and redox signalling, Parkinson’s Disease, and neurodegeneration before the latest advances in this field are explored in detail. Topics covered in the following chapters include the role of mitochondria, dopamine metabolism, metal homeostasis, inflammation, DNA-damage and thiol-signalling. The role of genetics and gene-environment interactions are also explored before final chapters discuss the identification of potential biomarkers for diagnosis and disease progression and the future of redox/antioxidant based therapeutics. Written by recognized experts in the field, this book will be a valuable source of information for postgraduate students and academics, clinicians, toxicologists and risk assessment groups. Importantly, it presents the current research that might later lead to redox or antioxidant – based therapeutics for Parkinson’s disease.
Author: Matthias P. Mayer
Publisher: Frontiers Media SA
ISBN: 2889451259
Category :
Languages : en
Pages : 71
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Book Description
Members of the HSP70 family form a central hub of the molecular chaperone network, controlling protein homeostasis in prokaryotes and in the ATP-containing compartments of the eukaryotic cells. The heat-inducible form HSPA1A (HSP70), its constitutive cytosolic cognate HSPA8 (Hsc70), its endoplasmic reticulum form HSPA5 (BiP), and its mitochondrial form HSPA9 (Mortalin), as well as the more distantly related HSPHs (HSP110s), make up 1-2 % of the total mass of proteins in human cells. They use the energy of ATP-hydrolysis to prevent and forcefully revert the process of protein misfolding and aggregation during and following various stresses, presumably by working as unfoldases to lift aberrant conformers out of kinetic traps. As such, HSP70s, in cooperation with their J-domain co-chaperones and nucleotide exchange factors (NEFs) and co-disaggregases, form an efficient network of cellular defenses against the accumulation of cytotoxic misfolded protein conformers, which may cause degenerative diseases such as Parkinson's and Alzheimer's disease, diabetes, and aging in general. In addition to their function in repair of stress-induced damage, HSP70s fulfill many housekeeping functions, including assisting the de novo folding and maturation of proteins, driving the translocation of protein precursors across narrow membrane pores into organelles, and by controlling the oligomeric state of key regulator protein complexes involved in signal transduction and vesicular trafficking. For reasons not well understood, HSP70s are also found on the surface of some animal cells, in particular cancer cells where they may serve as specific targets for cancer immunotherapy. Here, we gathered seven mini reviews, each presenting a complementary aspect of HSP70’s structure and function in bacteria and eukaryotes, under physiological and stressful conditions. These articles highlight how, the various members of this conserved family of molecular chaperones, assisted by their various J-domain and NEF cochaperones and co-disaggregases, harness ATP hydrolysis to perform a great diversity of life-sustaining cellular functions using a similar molecular mechanism.
