https://www.parkinson.org/Understanding-Parkinsons/Causes Here is a list of diseases that are commonly associated with protein aggregation and its effects on the cells of the body: Identifying the precise pathways of protein dysfunction and disease can help researchers determine potential therapies to slow or halt the progression of the above diseases. Indeed. chronic hemodialysis consists not only of providing the patient with safe and well-tolerated dialysis sessions but also of maintaining good general condition, adequate nutritional status and well-being in the long term. Found insideThis book addresses molecular mechanisms of protein misfolding and the role of lipids and related molecules in these complex processes. IntroductionThe biological function of a protein depends on its tridimensional structure, which is determined by its amino acid sequence during the process of protein folding. In some cases, the deposition of one type of protein can be experimentally induced by aggregated assemblies of other proteins that are rich in β-sheet structure, possibly because of structural complementarity of the protein molecules. Identified Prion Diseases. However, some proteinaceous lesions lack birefringence and contain few or no classical amyloid fibrils, such as the diffuse deposits of A? Proteinopathy Aggregating protein(s) Alzheimer’s disease Amyloid beta (Ab) peptide; Tau Parkinson’s disease α-synuclein Multiple tauopathies Tau protein (microtubule associated) Huntington’s disease Huntingtin with tandem glutamine repeats Amyotrophic lateral sclerosis Superoxide dismutase 1 Spongiform encephalopathies Prion proteins (toxic) Familial … The proteopathies (also known as proteinopathies, protein conformational disorders, or protein misfolding diseases) include such diseases as Creutzfeldt-Jakob disease and other prion diseases, Alzheimer's disease, Parkinson's disease, amyloidosis, and a wide range of other disorders (see List of Proteopathies). It is hypothesized that chaperones and co-chaperones (proteins that assist protein folding) may antagonize proteotoxicity during aging and in protein misfolding-diseases to maintain proteostasis. Therefore, this book represents an exciting documentation of the beginning of a new era in the pharmaceutical industry. In addition, scientists from basic research, clinic and industry actively involved in new developments discuss. [78] In some proteopathies, inhibiting the toxic effects of protein oligomers might be beneficial. [2][4][5][6][7][8] The term proteopathy was first proposed in 2000 by Lary Walker and Harry LeVine. They have been most thoroughly studied with regard to prion disease, and are referred to as protein strains. Protein misfolding is linked to disease. Often the proteins fail to fold into their normal configuration; in this misfolded state, the proteins can become toxic in some way (a gain of toxic function) or they can lose their normal function. For example, proteins that are normally unfolded or relatively unstable as monomers (that is, as single, unbound protein molecules) are more likely to misfold into an abnormal conformation. [74] In immunoglobulin light chain amyloidosis (AL amyloidosis), chemotherapy can be used to lower the number of the blood cells that make the light chain protein that forms amyloid in various bodily organs. Many of these diseases are associated with aging, but the mechanism for this connection is unknown. The best known form of such inducible proteopathy is prion disease, which can be transmitted by exposure of a host organism to purified prion protein in a disease-causing conformation. In Protein Misfolding and Disease: Principles and Protocols, notable experts in conformational disease review the latest thinking about the molecular processes underlying these diseases and describe cutting-edge biochemical, genomic, cellular, and chemical laboratory techniques for studying their genesis and pathologies. Nephrogenic diabetes insipidus (NDI)—mutations in the gene encoding for the precursors of the antidiuretic hormone arginine vasopressin (AVP) cause incompetent folding of the responsible protein. For example, cystic fibrosis is caused by a defective cystic fibrosis transmembrane conductance regulator (CFTR) protein,[3] and in amyotrophic lateral sclerosis / frontotemporal lobar degeneration (FTLD), certain gene-regulating proteins inappropriately aggregate in the cytoplasm, and thus are unable to perform their normal tasks within the nucleus. A century-old debate on protein aggregation Found insideIn this text, new information about the structure of sigma 1 receptor, its binding sites are provided as well as its expression in many cell types. Here is a list of diseases that are commonly associated with protein aggregation and its effects on the cells of the body: Alzheimer’s disease (AD)—when amyloid and tau proteins unfold in and around brain cells, proteins form plaques and tangles that cause these neurons to lose function. The majority of conditions arise sporadically, with only … This book gives a comprehensive overview of the possible mechanisms involved in Protein Misfolding Disorders and possible therapeutic strategies to treat these diseases. Cystic fibrosis (CF)—mutations within the cystic fibrosis transmembrane regulator gene (CFTR) cause CFTR protein misfolding, rendering these proteins unable to move salts in and out of the cell. The book is fully illustrated and chapters include comprehensive reference sections. Essential reading for scientists involved in prion research. ; proteopathic ... photo src: www.youtube.com Weight gain is an increase in body weight. [83][80][85][86] In some cases, multiple therapeutic agents may be combined to improve effectiveness.[80][87]. Human cells produce at least 30,000 different proteins. The concept of proteopathy can trace its origins to the mid-19th century, when, in 1854, Rudolf Virchow coined the term amyloid ("starch-like") to describe a substance in cerebral corpora amylacea that exhibited a chemical reaction resembling that of cellulose. Would love your thoughts, please comment. Thomas P.J. The first resource of its kind, this book covers cutting-edge research on the use of nanoparticles for in vivo diagnostic medical imaging and therapy. In all of these instances, an aberrant form of the protein itself appears to be the pathogenic agent. http://amyloidosis.org/facts/wild-type/ In the aging brain, multiple proteopathies can overlap. The degree of func-tional correction achieved depends on the absolute amount of protein rescued, its intrinsic activity, and its new stability at the In general, such heterologous seeding is less efficient than is seeding by a corrupted form of the same protein. The misfolding, aggregation, and tissue accumulation of proteins are common events in diverse chronic diseases, known as protein misfolding disorders. Models, Molecular. [13][14] Because proteins share a common structural feature known as the polypeptide backbone, all proteins have the potential to misfold under some circumstances. https://www.ninds.nih.gov/disorders/patient-caregiver-education/fact-sheets/machado-joseph-disease-fact-sheet Their stabilizing effect on mutant pro-teins allows their correct delivery and activity. The proteopathies (also known as proteinopathies, protein conformational disorders, or protein misfolding diseases) include such diseases as Creutzfeldt-Jakob disease and other prion diseases, Alzheimer's disease, Parkinson's disease, amyloidosis, and a wide range of other disorders (see List of Proteopathies). [23][24] In the aging brain, multiple proteopathies can overlap. Examples of this are the spastic paraplegia attributable to mutations in mitochondrial protease/chaperone complexes. The loss of skeletal muscle mass and strength substantially impairs physical performance and quality of life. This book details some approaches to the treatment of muscle wasting. The development of effective treatments for many proteopathies has been challenging. Parkinson’s disease (PD) is caused by a progressive loss of nerve cells in the part of the brain responsible for dopamine production, enabling cell messaging that allows body movement—PD ultimately leads to tremors, slow movements, and muscle rigidity. Protein misfolding induced by missense mutations has been identified as the cause of many genetic (or in this case conformational) diseases. A protein is considered to be misfolded if it cannot achieve its normal native state. This can be due to mutations in the amino acid sequence or a disruption of the normal folding process by external factors. cystic fibrosis transmembrane conductance regulator, Odontogenic ameloblast-associated protein, "Noncerebral Amyloidoses: Aspects on Seeding, Cross-Seeding, and Transmission", "Biology and genetics of prions causing neurodegeneration", "Diffuse, lake-like amyloid-beta deposits in the parvopyramidal layer of the presubiculum in Alzheimer disease", "Conjoint pathologic cascades mediated by ALS/FTLD-U linked RNA-binding proteins TDP-43 and FUS", "RNA binding proteins and the genesis of neurodegenerative diseases", "Self-propagation of pathogenic protein aggregates in neurodegenerative diseases", "The amyloid state of proteins in human diseases", "Label-free vibrational imaging of different Aβ plaque types in Alzheimer's disease reveals sequential events in plaque development", "Proteopathic Strains and the Heterogeneity of Neurodegenerative Diseases", "A general model of prion strains and their pathogenicity", "The neuropathology of chronic traumatic encephalopathy", "Correlation of Alzheimer disease neuropathologic changes with cognitive status: a review of the literature", "Dementia with Lewy bodies: Definition, diagnosis, and pathogenic relationship to Alzheimer's disease", "Molecular chaperones antagonize proteotoxicity by differentially modulating protein aggregation pathways", "A chaperome subnetwork safeguards proteostasis in aging and neurodegenerative disease", "Model systems of protein-misfolding diseases reveal chaperone modifiers of proteotoxicity", "From microbes to prions the final proof of the prion hypothesis", "The role of cofactors in prion propagation and infectivity", "Transmission and spreading of tauopathy in transgenic mouse brain", "Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein", "α-Synuclein propagates from mouse brain to grafted dopaminergic neurons and seeds aggregation in cultured human cells", "Transfer of host-derived α synuclein to grafted dopaminergic neurons in rat", "Superoxide dismutase 1 and tgSOD1 mouse spinal cord seed fibrils, suggesting a propagative cell death mechanism in amyotrophic lateral sclerosis", "Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells", "Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates", "Prion-Like Characteristics of Polyglutamine-Containing Proteins", "A seeding reaction recapitulates intracellular formation of Sarkosyl-insoluble transactivation response element (TAR) DNA-binding protein-43 inclusions", "Protein fibrils in nature can enhance amyloid protein A amyloidosis in mice: Cross-seeding as a disease mechanism", "Induction of AApoAII amyloidosis by various heterogeneous amyloid fibrils", "Induction of tau pathology by intracerebral infusion of amyloid-beta -containing brain extract and by amyloid-beta deposition in APP x Tau transgenic mice", "Molecular cross talk between misfolded proteins in animal models of Alzheimer's and prion diseases", "Cerebral amyloid angiopathies: a pathologic, biochemical, and genetic view", "Targeting amyloid-beta in glaucoma treatment", "Trinucleotide repeats: a structural perspective", "CADASIL: Notch signaling defect or protein accumulation problem? Eventually, irreversible degeneration and cell death linked to defective huntingtin leads to mood changes, obsessive-compulsive disorder (OCD), decreased thinking and reasoning, and abnormal involuntary body movements. A hallmark event in neurodegenerative diseases (NDs) is the misfolding, aggregation, and accumulation of proteins, leading to cellular dysfunction, loss of synaptic connections, and brain damage. Misfolding, however, is not only spread from protein to protein, but also from neuron to neuron. In 1859, Friedreich and Kekulé demonstrated that, rather than consisting of cellulose, "amyloid" actually is rich in protein. This volume of Advances in Protein Chemistry provides a broad, yet deep look at the cellular components that assist protein folding in the cell. If you continue to use this site we will assume that you are happy with it. These misfolded proteins can form fibrillar aggregates within the cell’s endoplasmic reticulum (ER), causing cell degradation, increased urine production, and dehydration. Found inside – Page iThis is the first book to assemble the leading researchers in the field of LRRK2 biology and neurology and provide a snapshot of the current state of knowledge, encompassing all major aspects of its function and dysfunction. Recent evidence has shown that the formation and accumulation of protein aggregates may be a process frequently occurring during … Figure 50: Neurodegenerative Disease, Global, List of All Pipeline Programs, 2017 Part 35 79. Cystic fibrosis. [81] Because TTR is mainly produced in the liver, TTR amyloidosis can be slowed in some hereditary cases by liver transplantation. disease]; proteopathies pl . https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3819655/ Protein misfolding and disease; protein refolding and therapy. The volume begins with several concepts and approaches developed in the recent past including a connection to the research field of aging, where protein misfolding diseases have been equated to premature aging processes, and the book’s ... The condition mostly affects older men and can cause organ failure, heart rhythm issues, and heart failure. Aβ, tau, α-synuclein, prion) by recognizing a common amyloid protein conformation. Prion diseases are a rare group of neurodegenerative disorders caused by abnormally folded protein in your brain. The misfolded protein forms clumps that damage nerve cells, leading to a progressive decline in brain function. [27][28][29], Some proteins can be induced to form abnormal assemblies by exposure to the same (or similar) protein that has folded into a disease-causing conformation, a process called 'seeding' or 'permissive templating'. 3, No. https://www.cdc.gov/prions/cjd/about.html protein]; -pathy [suff. There is now evidence that other proteopathies can be induced by a similar mechanism, including A? [5][15][16] In nearly all instances, the disease-causing molecular configuration involves an increase in beta-sheet secondary structure of the protein. protein]; -pathy [ suff . [1][2] Often the proteins fail to fold into their normal configuration; in this misfolded state, the proteins can become toxic in some way (a toxic gain-of-function) or they can lose their normal function. Protein misfolding and its consequences for disease. Chem. Ideal for graduate and undergraduate courses, the book includes PC and Macintosh versions of two programs for simulating and manipulating any aspect of synaptic transmission."--BOOK JACKET. https://pubmed.ncbi.nlm.nih.gov/22200539/ https://febs.onlinelibrary.wiley.com/doi/full/10.1111/j.1742-4658.2006.05181.x [83][84], Several other treatment strategies for proteopathies are being investigated, including small molecules and biologic medicines such as small interfering RNAs, antisense oligonucleotides, peptides, and engineered immune cells. Protein Misfolding and Disease. Gaucher’s disease (GD)—this heritable gene mutation causes protein misfolding and degradation of an enzyme that enables the breakdown of fatty substances in the spleen, liver, and bone tissue. [80] Transthyretin (TTR) amyloidosis (ATTR) results from the deposition of misfolded TTR in multiple organs. While the literature abounds, the field has lacked a comprehensive accounting of this progress. Emerging Protein Biotherapeutics consolidate Amyloid / metabolism. The book emphasizes therapeutics in an amyloid disease context to help students, faculty, … 2.ofer KF, Tatzelt J, Haass C. The two faces of protein misfolding: Winklh gain- and loss-of-function in neurodegenerative diseases. Found insideThis book opens an exciting door to provide up-to-date information about the function and the mechanisms of the amyloid formation process from the structural, biophysical, biomedical, and nanotechnological perspective, combining the new ... Over time, clumps of degenerated proteins start to aggregate in the cell, causing various types of dysfunction and eventually cell death. [1], The concept of proteopathy can trace its origins to the mid-19th century, when, in 1854, Rudolf Virchow coined the term amyloid ("starch-like") to describe a substance in cerebral corpora amylacea that exhibited a chemical reaction resembling that of cellulose. In all of these instances, an aberrant form of the protein itself appears to be the pathogenic agent. Bind, dissociate and prevent formation of pathological misfolded protein assemblies at key stages (oligomers, fibrils, plaques). The diseases caused by protein misfolding, i.e. 3. ; proteopathic adj) refers to a class of diseases in which certain proteins become structurally abnormal, and thereby disrupt the function of cells, tissues and organs of the body. When proteins unfold improperly or misfold, they can no longer carry out their cellular responsibilities and begin to degenerate. Metastable proteins tend to populate misfolded species that are prone to forming toxic aggregates, including soluble oligomers and fibrillar amyloid deposits, which are linked with neurodegeneration in Alzheimer and Parkinson disease, and many other pathologies. The proteopathies (also known as proteinopathies, protein conformational disorders, or protein misfolding diseases) include such diseases as Creutzfeldt–Jakob disease and other prion diseases, Alzheimer's disease, Parkinson's disease, amyloidosis, Multiple System Atrophy, and a wide range of other disorders (see List of Proteopathies). When proteins do not fold correctly, or misfold, they can aggregate together and form big clumps in the cells where they form, causing diseases such as Alzheimer’s, Parkinson’s, multiple sclerosis (MS), diabetes, ALS, schizophrenia and many others.. protein]; -pathy [suff. The book emphasizes therapeutics in an amyloid disease context to help students, faculty, scientific researchers, and doctors working with protein misfolding diseases bridge the gap between basic science and pharmaceutical applications to ... In medicine, proteopathy (Proteo- [pref. Figure 51: Neurodegenerative Disease, Global, First-in-Class Molecular Target Matrix Assessment for Protein Misfolding, 2017 83 [25] For example, in addition to tauopathy and Aβ-amyloidosis (which coexist as key pathologic features of Alzheimer's disease), many Alzheimer patients have concomitant synucleinopathy (Lewy bodies) in the brain. Cystic fibrosis (CF) is an inherited, multiorgan, multifactorial protein misfolding disease with its major pathologic impact being on respiratory function. An increasingly aging population will add to the number of individuals suffering from amyloid. There is also experimental evidence for cross-seeding between prion protein and A?. For example, AA amyloidosis can be stimulated in mice by such diverse macromolecules as silk, the yeast amyloid Sup35, and curli fibrils from the bacterium Escherichia coli. In medicine, proteopathy (/proʊtiːˈɒpəθiː/; from proteo- [pref. [5][15][17][18][19] The abnormal proteins in some proteopathies have been shown to fold into multiple 3-dimensional shapes; these variant, proteinaceous structures are defined by their different pathogenic, biochemical, and conformational properties. https://www.nhs.uk/conditions/alzheimers-disease/causes/. The Folding@home project (FAH) is dedicated to understanding protein folding, the diseases that result from protein misfolding and aggregation, and novel computational ways to develop new drugs in general. In some cases, misfolding of the protein results in a loss of its usual function. Because proteins share a common structural feature known as the polypeptide backbone, all proteins have the potential to misfold under some circumstances. [3] The proteopathies (also known as proteinopathies, protein conformational disorders, or protein misfolding diseases) include such diseases as Creutzfeldt–Jakob disease and other prion diseases, Alzheimer's disease, Parkinson's disease, amyloidosis, multiple system atrophy, and a wide range of other disorders. 7-9 Loss of protein function results from early degradation, mislocalization, structural alteration or aggregation 10-13 leading to pathological dysfunctions. More than a quick survey, this comprehensive text includes USMLE sample exams from Bhagavan himself, a previous coauthor. In 1859, Friedreich and Kekulé demonstrated that, rather than consisting of cellulose, "amyloid" actually is rich in protein. https://rarediseases.org/rare-diseases/nephrogenic-diabetes-insipidus/ Protein misfolding and aggregation is the common cause and pathological mechanism of neurodegenerative diseases such as Alzheimer’s disease (AD), amyotrophic lateral sclerosis (ALS), PD, and Huntington’s disease (HD). Found insideThis book is a collection of an expert team of agronomists, chemists, biologists and policy makers who discuss some of the processes involved in developing a naturally-sourced bioactive compound into a drug therapy. This second volume follows on from Part I by reviewing the variety of animal models of PD current available (from drosophila to rodents to non-human primate species) and their specific contributions to PD research. protein misfolding diseases. Metastable proteins tend to populate misfolded species that are prone to forming toxic aggregates, including soluble oligomers and fibrillar amyloid deposits, which are linked with neurodegeneration in Alzheimer and Parkinson disease, and many other pathologies. Over time, clumps of degenerated proteins start to aggregate in the cell, causing various types of dysfunction and eventually cell death. https://www.mayoclinic.org/diseases-conditions/cystic-fibrosis/symptoms-causes/syc-20353700 As a result, mucus accumulates within the respiratory, digestive, and reproductive systems, causing damage and, eventually, respiratory failure. Found insideThis book is a printed edition of the Special Issue "Extracellular Matrix in Development and Disease" that was published in IJMS Despite these controls, a range of debilitating human diseases is associated with protein misfolding events that result in the malfunctioning of the cellular machinery. Proteins are complex molecules that play many critical roles within the human body. https://febs.onlinelibrary.wiley.com/doi/full/10.1111/j.1742-4658.2006.05181.x, https://medlineplus.gov/genetics/understanding/howgeneswork/protein/, https://academic.oup.com/jmcb/article/2/4/180/865830, https://www.parkinson.org/Understanding-Parkinsons/Causes, https://rarediseases.org/rare-diseases/nephrogenic-diabetes-insipidus/, https://www.ninds.nih.gov/disorders/patient-caregiver-education/fact-sheets/machado-joseph-disease-fact-sheet, https://pubmed.ncbi.nlm.nih.gov/22200539/, https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3819655/, https://fapnewstoday.com/what-is-familial-amyloid-polyneuropathy/, https://www.cdc.gov/prions/cjd/about.html, https://www.mayoclinic.org/diseases-conditions/cystic-fibrosis/symptoms-causes/syc-20353700, https://www.nhs.uk/conditions/alzheimers-disease/causes/, Ali Ghani, Edmonton fitness advocate gives tips to achieve healthy New Year goals. This book represents essential reading for researchers and practicing clinicians in nutrition, dietetics, geriatrics, nursing, neurology, and psychology, as well as researchers, such as neuroscientists, molecular and cellular biochemists, ... Humans can either inherit this prion or receive it through transmission, but either form causes severe mental and physical impairment as well as eventual death. The aim of this book is to present an up-to-date view of the role of genetics in modern medicine. [10] Furthermore, evidence has emerged that small, non-fibrillar protein aggregates known as oligomers are toxic to the cells of an affected organ, and that amyloidogenic proteins in their fibrillar form may be relatively benign. An effective therapy must solve three major challenges in the treatment of misfolded protein diseases: Target a broad spectrum of misfolded proteins (e.g. amyloidosis, amyloid A (AA) amyloidosis, and apolipoprotein AII amyloidosis, tauopathy, synucleinopathy, and the aggregation of superoxide dismutase-1 (SOD1), polyglutamine, and TAR DNA-binding protein-43 (TDP-43). The role of metal ions in protein folding and structure is a critical topic to a range of scientists in numerous fields, particularly those working in structural biology and bioinorganic chemistry, those studying protein folding and disease ... The current list of protein misfolding disorders includes, but is not limited to, numerous neurodegenerative diseases such as PD, Down’s syndrome, AD, and Huntington’s disease; transmissible encephalopathies; Gerstmann–Straussler–Scheinker disease; fatal familial insomnia; multiple system atrophy; numerous synucleinopathies and taupathies; … Retinitis pigmentosa (RP)—mutations in any of the genes that create photoreceptors in the retina can lead to abnormally functioning or toxic proteins. As we discussed earlier, many diseases are caused by protein misfolding, which is often associated with aggregation. [49] In general, such heterologous seeding is less efficient than is seeding by a corrupted form of the same protein. This book is about calreticulin, a multifunctional calcium binding protein first discovered over 20 years ago. This book presents contemporary views on the genetic, biochemical, and immunological determinants of this disease. This book also concerns the issue of Alzheimer's disease prevention through lifestyle and physical activity. Many of these roles occur at the cellular level and are undetectable to us as we go about our daily lives—until something goes wrong. Diseases. Furthermore, evidence has emerged that small, non-fibrillar protein aggregates known as oligomers are toxic to the cells of an affected organ, and that amyloidogenic proteins in their fibrillar form may be relatively benign. The way this happens is also still not very clear, but it is suspected that misfolded proteins may be taken up from the extracellular space into neurons, where they begin to infect susceptible proteins and further spread pathological misfolding. This Monograph offers a comprehensive and up-to-date overview of AATD. The folds aren't random and give the molecule a specific shape and function. Humans. The best known forms of inducible proteopathy are prion diseases,[32] which can be transmitted by exposure of a host organism to purified prion protein in a disease-causing conformation. 2003; 4: 49-60. We use cookies to ensure that we give you the best experience on our website. This book provides readers with a timely update on this rapidly advancing area of investigation, presenting an invaluable resource for researchers in the field. Diseases arising as a result of protein misfolding are classified based on the location of the protein deposition. ", "Seipinopathy: a novel endoplasmic reticulum stress-associated disease", "Amyloid fibril proteins and amyloidosis: chemical identification and clinical classification International Society of Amyloidosis 2016 Nomenclature Guidelines", "Prion-Like Protein Aggregates and Type 2 Diabetes", "Pharmaceutical amyloidosis associated with subcutaneous insulin and enfuvirtide administration", "The cystic fibrosis transmembrane conductance regulator (CFTR) and its stability", "Alzheimer's disease: the challenge of the second century", "Pathogenesis, diagnosis and treatment of systemic amyloidosis", "Vaccination strategies in tauopathies and synucleinopathies", "Recent advances in understanding and treating immunoglobulin light chain amyloidosis", "Liver transplantation in transthyretin amyloidosis: issues and challenges", "Liver transplantation for hereditary transthyretin amyloidosis", "Survival After Transplantation in Patients With Mutations Other Than Val30Met: Extracts From the FAP World Transplant Registry", "Mechanism of Action and Clinical Application of Tafamidis in Hereditary Transthyretin Amyloidosis", "Single-stranded RNAs use RNAi to potently and allele-selectively inhibit mutant huntingtin expression", https://en.wikipedia.org/w/index.php?title=Proteopathy&oldid=1033194177, Short description is different from Wikidata, Creative Commons Attribution-ShareAlike License, Galectin-7 amyloidosis (primary localized cutaneous amyloidosis), This page was last edited on 12 July 2021, at 05:55.

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