Relevant bibliographies by topics / Amyloid Proteins (Amyloidosis)

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  2. Dissertations / Theses
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Academic literature on the topic 'Amyloid Proteins (Amyloidosis)'

Author: Grafiati
Published: 7 September 2023

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Journal articles on the topic "Amyloid Proteins (Amyloidosis)"

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Bajic, Vladan P., Adil Salhi, Katja Lakota, Aleksandar Radovanovic, Rozaimi Razali, Lada Zivkovic, Biljana Spremo-Potparevic, et al. "DES-Amyloidoses “Amyloidoses through the looking-glass”: A knowledgebase developed for exploring and linking information related to human amyloid-related diseases." PLOS ONE 17, no. 7 (July 25, 2022): e0271737. http://dx.doi.org/10.1371/journal.pone.0271737.

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More than 30 types of amyloids are linked to close to 50 diseases in humans, the most prominent being Alzheimer’s disease (AD). AD is brain-related local amyloidosis, while another amyloidosis, such as AA amyloidosis, tends to be more systemic. Therefore, we need to know more about the biological entities’ influencing these amyloidosis processes. However, there is currently no support system developed specifically to handle this extraordinarily complex and demanding task. To acquire a systematic view of amyloidosis and how this may be relevant to the brain and other organs, we needed a means to explore "amyloid network systems" that may underly processes that leads to an amyloid-related disease. In this regard, we developed the DES-Amyloidoses knowledgebase (KB) to obtain fast and relevant information regarding the biological network related to amyloid proteins/peptides and amyloid-related diseases. This KB contains information obtained through text and data mining of available scientific literature and other public repositories. The information compiled into the DES-Amyloidoses system based on 19 topic-specific dictionaries resulted in 796,409 associations between terms from these dictionaries. Users can explore this information through various options, including enriched concepts, enriched pairs, and semantic similarity. We show the usefulness of the KB using an example focused on inflammasome-amyloid associations. To our knowledge, this is the only KB dedicated to human amyloid-related diseases derived primarily through literature text mining and complemented by data mining that provides a novel way of exploring information relevant to amyloidoses.
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Wisniowski, Brendan, and Ashutosh Wechalekar. "Confirming the Diagnosis of Amyloidosis." Acta Haematologica 143, no. 4 (2020): 312–21. http://dx.doi.org/10.1159/000508022.

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Amyloidosis is a general term for diseases characterised by the deposition of insoluble amyloid fibrils in organs or tissues, leading to organ dysfunction and, in many cases, death. Amyloid fibrils are derived from soluble precursor proteins, with the number of known amyloidogenic proteins increasing over time. The identity of the precursor protein often predicts the disease phenotype, although many of the amyloidoses have overlapping clinical features. Most patients with amyloidosis will require biopsy of an involved organ or tissue to confirm the diagnosis. Cardiac transthyretin amyloidosis, however, may be diagnosed without a biopsy provided stringent criteria are met. Where amyloid is confirmed histologically, the identity of the amyloidogenic protein must be determined, given several of the amyloidoses have disease-specific therapies. Laser capture microdissection and tandem mass spectrometry, LCM-MS, has revolutionised amyloid subtyping, being able to identify the amyloidogenic protein more reliably than antibody-based methods such as immunohistochemistry. Here we summarise the biopsy approach to amyloidosis, as well as the non-biopsy diagnosis of cardiac transthyretin amyloidosis. Proteomic and antibody-based methods for amyloid subtyping are reviewed. Finally, an algorithm for confirming the diagnosis of amyloidosis is presented.
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Koike, Haruki, and Masahisa Katsuno. "The Ultrastructure of Tissue Damage by Amyloid Fibrils." Molecules 26, no. 15 (July 29, 2021): 4611. http://dx.doi.org/10.3390/molecules26154611.

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Amyloidosis is a group of diseases that includes Alzheimer’s disease, prion diseases, transthyretin (ATTR) amyloidosis, and immunoglobulin light chain (AL) amyloidosis. The mechanism of organ dysfunction resulting from amyloidosis has been a topic of debate. This review focuses on the ultrastructure of tissue damage resulting from amyloid deposition and therapeutic insights based on the pathophysiology of amyloidosis. Studies of nerve biopsy or cardiac autopsy specimens from patients with ATTR and AL amyloidoses show atrophy of cells near amyloid fibril aggregates. In addition to the stress or toxicity attributable to amyloid fibrils themselves, the toxicity of non-fibrillar states of amyloidogenic proteins, particularly oligomers, may also participate in the mechanisms of tissue damage. The obscuration of the basement and cytoplasmic membranes of cells near amyloid fibrils attributable to an affinity of components constituting these membranes to those of amyloid fibrils may also play an important role in tissue damage. Possible major therapeutic strategies based on pathophysiology of amyloidosis consist of the following: (1) reducing or preventing the production of causative proteins; (2) preventing the causative proteins from participating in the process of amyloid fibril formation; and/or (3) eliminating already-deposited amyloid fibrils. As the development of novel disease-modifying therapies such as short interfering RNA, antisense oligonucleotide, and monoclonal antibodies is remarkable, early diagnosis and appropriate selection of treatment is becoming more and more important for patients with amyloidosis.
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Acquasaliente, Laura, and Vincenzo De Filippis. "The Role of Proteolysis in Amyloidosis." International Journal of Molecular Sciences 24, no. 1 (December 31, 2022): 699. http://dx.doi.org/10.3390/ijms24010699.

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Amyloidoses are a group of diseases associated with deposits of amyloid fibrils in different tissues. So far, 36 different types of amyloidosis are known, each due to the misfolding and accumulation of a specific protein. Amyloid deposits can be found in several organs, including the heart, brain, kidneys, and spleen, and can affect single or multiple organs. Generally, amyloid-forming proteins become prone to aggregate due to genetic mutations, acquired environmental factors, excessive concentration, or post-translational modifications. Interestingly, amyloid aggregates are often composed of proteolytic fragments, derived from the degradation of precursor proteins by yet unidentified proteases, which display higher amyloidogenic tendency compared to precursor proteins, thus representing an important mechanism in the onset of amyloid-based diseases. In the present review, we summarize the current knowledge on the proteolytic susceptibility of three of the main human amyloidogenic proteins, i.e., transthyretin, β-amyloid precursor protein, and α-synuclein, in the onset of amyloidosis. We also highlight the role that proteolytic enzymes can play in the crosstalk between intestinal inflammation and amyloid-based diseases.
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Guan, Jian, Shikha Mishra, Rodney H. Falk, and Ronglih Liao. "Current perspectives on cardiac amyloidosis." American Journal of Physiology-Heart and Circulatory Physiology 302, no. 3 (February 2012): H544—H552. http://dx.doi.org/10.1152/ajpheart.00815.2011.

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Amyloidosis represents a group of diseases in which proteins undergo misfolding to form insoluble fibrils with subsequent tissue deposition. While almost all deposited amyloid fibers share a common nonbranched morphology, the affected end organs, clinical presentation, treatment strategies, and prognosis vary greatly among this group of diseases and are largely dependent on the specific amyloid precursor protein. To date, at least 27 precursor proteins have been identified to result in either local tissue or systemic amyloidosis, with nine of them manifesting in cardiac deposition and resulting in a syndrome termed “cardiac amyloidosis” or “amyloid cardiomyopathy.” Although cardiac amyloidosis has been traditionally considered to be a rare disorder, as clinical appreciation and understanding continues to grow, so too has the prevalence, suggesting that this disease may be greatly underdiagnosed. The most common form of cardiac amyloidosis is associated with circulating amyloidogenic monoclonal immunoglobulin light chain proteins. Other major cardiac amyloidoses result from a misfolding of products of mutated or wild-type transthyretin protein. While the various cardiac amyloidoses share a common functional consequence, namely, an infiltrative cardiomyopathy with restrictive pathophysiology leading to progressive heart failure, the underlying pathophysiology and clinical syndrome varies with each precursor protein. Herein, we aim to provide an up-to-date overview of cardiac amyloidosis from nomenclature to molecular mechanisms and treatment options, with a particular focus on amyloidogenic immunoglobulin light chain protein cardiac amyloidosis.
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Czyżewska, Emilia. "Amyloidoses – pathogenesis, classification, diagnosis." Diagnostyka Laboratoryjna 56, no. 4 (July 9, 2021): 1–13. http://dx.doi.org/10.5604/01.3001.0015.0266.

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Amyloidoses – also known as amyloidosis or betafibrillosis – a diverse group of diseases in which amorphous protein with a changed conformational structure is deposited extracellularly, leading to the failure of many organs. The basic classifications of amyloidoses take into account: the type of precursor protein, the division into generalized (systemic) amyloidoses, in which amyloid deposits accumulate in many organs, vessel walls and connective tissue (e.g. AL amyloidosis) and local (localized) amyloidoses – limited to only one organ (e.g. corneal amyloidosis) as well as congenital and acquired diseases. Symptoms of amyloidosis are non-specific and not very characteristic, moreover, their severity depends on the type of disease and organ involvement. The diagnosis of amyloidosis should be considered in patients with heart failure without coronary artery disease, with neuropathy, or proteinuria or hepatomegaly of unclear origin. Diagnosis of amyloidosis is based on the evaluation of tissue biopsy samples and the presence of abnormal proteins, i.e. amyloid, or on the fibrillary evaluation confirmation of the filamentous nature of amyloid deposits using electron microscopy. The next step is differential diagnosis and amyloid differential identification, which is based on immunohistochemical and immunofluorescence studies using labeled antibodies. The "gold standard" used in typing amyloidosis and identifying an amyloidogenic protein is mass spectrometry. Laboratory tests are used to assess organ involvement, which is the basis of the prognostic classification.
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Ablasser, Klemens, Nicolas Verheyen, Theresa Glantschnig, Giulio Agnetti, and Peter P. Rainer. "Unfolding Cardiac Amyloidosis –From Pathophysiology to Cure." Current Medicinal Chemistry 26, no. 16 (August 26, 2019): 2865–78. http://dx.doi.org/10.2174/0929867325666180104153338.

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Deposition of amyloidogenic proteins leading to the formation of amyloid fibrils in the myocardium causes cardiac amyloidosis. Although any form of systemic amyloidosis can affect the heart, light-chain (AL) or transthyretin amyloidosis (ATTR) account for the majority of diagnosed cardiac amyloid deposition. The extent of cardiac disease independently predicts mortality. Thus, the reversal of arrest of adverse cardiac remodeling is the target of current therapies. Here, we provide a condensed overview on the pathophysiology of AL and ATTR cardiac amyloidoses and describe treatments that are currently used or investigated in clinical or preclinical trials. We also briefly discuss acquired amyloid deposition in cardiovascular disease other than AL or ATTR.
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Rognoni, Paola, Giulia Mazzini, Serena Caminito, Giovanni Palladini, and Francesca Lavatelli. "Dissecting the Molecular Features of Systemic Light Chain (AL) Amyloidosis: Contributions from Proteomics." Medicina 57, no. 9 (August 31, 2021): 916. http://dx.doi.org/10.3390/medicina57090916.

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Amyloidoses are characterized by aggregation of proteins into highly ordered amyloid fibrils, which deposit in the extracellular space of tissues, leading to organ dysfunction. In AL (amyloid light chain) amyloidosis, the most common form in Western countries, the amyloidogenic precursor is a misfolding-prone immunoglobulin light chain (LC), which, in the systemic form, is produced in excess by a plasma cell clone and transported to target organs though blood. Due to the primary role that proteins play in the pathogenesis of amyloidoses, mass spectrometry (MS)-based proteomic studies have gained an established position in the clinical management and research of these diseases. In AL amyloidosis, in particular, proteomics has provided important contributions for characterizing the precursor light chain, the composition of the amyloid deposits and the mechanisms of proteotoxicity in target organ cells and experimental models of disease. This review will provide an overview of the major achievements of proteomic studies in AL amyloidosis, with a presentation of the most recent acquisitions and a critical discussion of open issues and ongoing trends.
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Khoor, Andras, and Thomas V. Colby. "Amyloidosis of the Lung." Archives of Pathology & Laboratory Medicine 141, no. 2 (February 1, 2017): 247–54. http://dx.doi.org/10.5858/arpa.2016-0102-ra.

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Context.—Amyloidosis is a heterogeneous group of diseases characterized by the deposition of congophilic amyloid fibrils in the extracellular matrix of tissues and organs. To date, 31 fibril proteins have been identified in humans, and it is now recommended that amyloidoses be named after these fibril proteins. Based on this classification scheme, the most common forms of amyloidosis include systemic AL (formerly primary), systemic AA (formerly secondary), systemic wild-type ATTR (formerly age-related or senile systemic), and systemic hereditary ATTR amyloidosis (formerly familial amyloid polyneuropathy). Three different clinicopathologic forms of amyloidosis can be seen in the lungs: diffuse alveolar-septal amyloidosis, nodular pulmonary amyloidosis, and tracheobronchial amyloidosis. Objective.—To clarify the relationship between the fibril protein–based amyloidosis classification system and the clinicopathologic forms of pulmonary amyloidosis and to provide a useful guide for diagnosing these entities for the practicing pathologist. Data Sources.—This is a narrative review based on PubMed searches and the authors' own experiences. Conclusions.—Diffuse alveolar-septal amyloidosis is usually caused by systemic AL amyloidosis, whereas nodular pulmonary amyloidosis and tracheobronchial amyloidosis usually represent localized AL amyloidosis. However, these generalized scenarios cannot always be applied to individual cases. Because the treatment options for amyloidosis are dependent on the fibril protein–based classifications and whether the process is systemic or localized, the workup of new clinically relevant cases should include amyloid subtyping (preferably with mass spectrometry–based proteomic analysis) and further clinical investigation.
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Spodzieja, Marta, Sylwia Rodziewicz-Motowidło, and Aneta Szymanska. "Hyphenated Mass Spectrometry Techniques in the Diagnosis of Amyloidosis." Current Medicinal Chemistry 26, no. 1 (March 14, 2019): 104–20. http://dx.doi.org/10.2174/0929867324666171003113019.

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Amyloidoses are a group of diseases caused by the extracellular deposition of proteins forming amyloid fibrils. The amyloidosis is classified according to the main protein or peptide that constitutes the amyloid fibrils. The most effective methods for the diagnosis of amyloidosis are based on mass spectrometry. Mass spectrometry enables confirmation of the identity of the protein precursor of amyloid fibrils in biological samples with very high sensitivity and specificity, which is crucial for proper amyloid typing. Due to the fact that biological samples are very complex, mass spectrometry is usually connected with techniques such as liquid chromatography or capillary electrophoresis, which enable the separation of proteins before MS analysis. Therefore mass spectrometry constitutes an important part of the so called “hyphenated techniques” combining, preferentially in-line, different analytical methods to provide comprehensive information about the studied problem. Hyphenated methods are very useful in the discovery of biomarkers in different types of amyloidosis. In systemic forms of amyloidosis, the analysis of aggregated proteins is usually performed based on the tissues obtained during a biopsy of an affected organ or a subcutaneous adipose tissue. In some cases, when the diagnostic biopsy is not possible due to the fact that amyloid fibrils are formed in organs like the brain (Alzheimer’s disease), the study of biomarkers presented in body fluids can be carried out. Currently, large-scale studies are performed to find and validate more effective biomarkers, which can be used in diagnostic procedures. We would like to present the methods connected with mass spectrometry which are used in the diagnosis of amyloidosis based on the analysis of proteins occurring in tissues, blood and cerebrospinal fluid.
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Dissertations / Theses on the topic "Amyloid Proteins (Amyloidosis)"

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Bartlam, Mark Gerrard. "Structural studies of amyloid proteins." Thesis, University of Oxford, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.342536.

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Terry, Carolyn Jane. "Structural studies of plasma proteins of medical interest." Thesis, University of Oxford, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.302858.

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Skullerud, Andrine. "Characterization of antibodies specific for amyloid proteins." Thesis, Uppsala universitet, Institutionen för medicinsk cellbiologi, 2015. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-254597.

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Amyloidosis is a group of diseases caused by proteins that have lost their correct three-dimensional conformation and instead assemble into insoluble fibrils in various tissues and organs. Today, more than 30 different proteins that can give rise to amyloid fibrils have been identified. Each protein that assembles into fibrils causes a specific disease. For clinical diagnosis of amyloid, antibodies are one of the most important tools. In this study, antibodies generated towards various amyloid-specific peptides were characterized and validated. This was assessed by immunohistochemistry, slot blot and SDS-PAGE and western blot. Congo red, an amyloid specific dye, was used for detection of amyloid. Immunohistochemical staining and slot blot analysis indicated that each antiserum used in this study was amyloid-specific. Antigen retrieval can facilitate staining by the techniques ability to break cross-linkages caused by fixation in formaldehyde. The results from the characterization of antisera in this study should be a great helpin clinical work on amyloid, and ensure correct diagnosis.
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Franco, Daniel A., Seth Truran, Volkmar Weissig, Diana Guzman-Villanueva, Nina Karamanova, Subhadip Senapati, Camelia Burciu, et al. "Monosialoganglioside-Containing Nanoliposomes Restore Endothelial Function Impaired by AL Amyloidosis Light Chain Proteins." WILEY-BLACKWELL, 2016. http://hdl.handle.net/10150/621716.

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Light chain amyloidosis (AL) is associated with high mortality, especially in patients with advanced cardiovascular involvement. It is caused by toxicity of misfolded light chain proteins (LC) in vascular, cardiac, and other tissues. There is no treatment to reverse LC tissue toxicity. We tested the hypothesis that nanoliposomes composed of monosialoganglioside, phosphatidylcholine, and cholesterol (GM1 ganglioside-containing nanoliposomes [NLGM1]) can protect against LC-induced human microvascular dysfunction and assess mechanisms behind the protective effect.
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Nerelius, Charlotte. "Protein misfolding and amyloid formation : strategies for prevention /." Uppsala : Department of Anatomy, Physiology and Biochemistry, Swedish University of Agricultural Sciences, 2009. http://epsilon.slu.se/200941.pdf.

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Sarlo, Katherine. "Some biological properties of the mouse acute phase reactant serum amyloid p-component /." The Ohio State University, 1985. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487262513407963.

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Lannergård, Anders. "Serum Amyloid A Protein (SAA) in Healthy and Infected Individuals." Doctoral thesis, Uppsala University, Department of Medical Sciences, 2005. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-5774.

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Serum amyloid A protein (SAA) is an acute phase protein that has recently gained increasing interest as a potential marker for disease and treatment monitoring. We investigated SAA and CRP levels in (a) patients with various common infectious diseases (n=98), (b) patients with pyelonephritis (n=37) versus patients with cystitis (n=32), (c) healthy individuals of varying ages (n=231), (d) very immature newborn infants with or without nosocomial infections (NIs) (n=72) and (e) patients with bacterial infections treated with cefuroxime (n=81).

SAA significantly correlated with CRP in viral as well as in bacterial infections (for the total group: r2=0.757, p<0.0001) and showed a systemic inflammatory response in 90% of the patients with cystitis as compared with 23% for CRP. Equally high efficiencies (0.96 and 0.94 for SAA and CRP, respectively) were observed in discriminating between pyelonephritis and cystitis. SAA and high sensitive (hs) CRP were lower in umbilical cords (p<0.0001) and higher in elderly adults (p<0.0001-0.03) than in the other age groups; higher in immature newborn infants than in term infants; and higher in the NI group than in the non-NI group. Interindividual variabilities of the time course of the biomarkers SAA and CRP were considerable. Because of the smoothed distribution of SAA and CRP (i.e. elevations were both essentially unchanged during the first 3 days of cefuroxime treatment), these markers were not useful when deciding parenteral-oral switch of therapy, which occurred within this time period in most cases.

SAA is a sensitive systemic marker in cystitis. SAA and hsCRP in umbilical cord blood are close to the detection limit and increase with age. They increase in relation to NI in very immature newborn infants and might therefore be used in diagnosis and monitoring. Finally, SAA and CRP in adults with bacterial infections could not predict an early parenteral-oral switch of antimicrobial therapy.

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Lundmark, Katarzyna. "Studies on pathogenesis of experimental AA amyloidosis : effects of amyloid enhancing factor and amyloid-like fibrils in rapid amyloid induction /." Linköping : Univ, 2001. http://www.bibl.liu.se/liupubl/disp/disp2001/med711s.pdf.

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Binger, Katrina Jean. "The reversibility of amyloid fibril formation." Connect to thesis, 2009. http://repository.unimelb.edu.au/10187/4912.

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The aggregation of misfolded proteins into amyloid fibrils is implicated in the pathogenesis of several human degenerative diseases, including Alzheimer’s, Parkinson’s and Type II diabetes. Links between the deposition of amyloid fibrils and the progression of these diseases are poorly understood, with much of the current research focused on monomer misfolding and subsequent assembly of oligomers and mature fibrils. This project examines the formation of human apolipoprotein (apo) C-II amyloid fibrils, with a focus on the stability and reversibility of amyloid fibril assembly.
The initial stages of the project were to develop a model for apoC-II amyloid fibril formation. This was achieved by analysis of the concentration dependent kinetics of apoC-II amyloid fibril formation, and correlation of these data with the final size distribution of the fibrils, determined by sedimentation velocity experiments. On the basis of these studies, a new reversible model for apoC-II amyloid fibril formation is proposed that includes fibril breaking and re-joining as integral parts of the assembly mechanism. The model was tested by rigorous experimentation, with antibody-labelling transmission electron microscopy providing direct evidence for spontaneous fibril breaking and re-joining.
The development of this model for apoC-II fibril assembly provided the foundation for experiments to investigate factors that promote, inhibit or reverse amyloid fibril formation. Factors that were considered include a molecular chaperone protein, αB-crystallin, and a chemical modification, methionine oxidation. Investigations on the effect of αB-crystallin revealed that the inhibition of apoC-II fibril formation occurs by two distinct mechanisms: transient interaction with monomer preventing oligomerisation, and binding to mature fibrils, which inhibits fibril elongation. Studies on the effect of methionine oxidation on apoC-II fibril formation showed that both the assembly and stability of the fibrils was affected by this modification. ApoC-II contains two methionine residues (Met-9 and Met-60), and upon oxidation of these residues fibril formation was inhibited. In addition, the treatment of pre-formed fibrils with hydrogen peroxide caused dissociation of the fibrils via the oxidation of Met-60, located with the fibril core structural region. The final chapter details the development of antibodies that specifically recognise the conformation of apoC-II amyloid fibrils, which provide the foundation for future studies to examine the role that apoC-II amyloid fibrils play in disease.
Overall, this thesis reveals the dynamic and reversible nature of amyloid fibril formation. New insight is also obtained of the general stability of amyloid fibrils and the processes that may regulate their formation, persistence and disease pathogenesis in vivo.
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Bhogal, Ranjev. "The characterisation of binding sites for islet amyloid polypeptide and calcitonin gene-related peptide in mammalian lung." Thesis, Imperial College London, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.261471.

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Books on the topic "Amyloid Proteins (Amyloidosis)"

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Sipe, Jean D. Amyloid proteins: The beta sheet conformation and disease. Weinheim: Wiley-VCH, 2005.

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Thomas, Scheibel, ed. Fibrous proteins. Austin, Tex: Landes Bioscience, 2008.

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Marina, Ramirez-Alvarado, Kelly Jeffery W, and Dobson C. M, eds. Protein misfolding diseases: Current and emerging principles and therapies. Hoboken, N.J: Wiley, 2010.

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Indu, Kheterpal, and Wetzel Ronald, eds. Amyloid, prions, and other protein aggregates Part C. Amsterdam: Elsevier/Academic, 2006.

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B, O'Doherty Cian, and Byrne Adam C, eds. Protein misfolding. New York: Nova Science Publishers, 2008.

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Indu, Kheterpal, and Wetzel Ronald, eds. Amyloid, prions, and other protein aggregates Part B. Amsterdam: Elsevier/Academic, 2006.

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C, Dowler Brynn, ed. Endocytosis: Structural components, functions, and pathways. Hauppauge, N.Y: Nova Science Publishers, 2010.

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Sipe, Jean D. Amyloid Proteins: The Beta Sheet Conformation and Disease. Wiley-VCH, 2005.

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Lachmann, Helen J., and Giampaolo Merlini. The patient with amyloidosis. Edited by Giuseppe Remuzzi. Oxford University Press, 2015. http://dx.doi.org/10.1093/med/9780199592548.003.0152.

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Amyloidosis is a disorder of protein folding in which normally soluble plasma proteins are deposited in the extracellular space in an abnormal insoluble fibrillar form. The process of amyloid formation and deposition causes cytotoxicity and progressive organ dysfunction. Amyloid is remarkably diverse and can be hereditary or acquired, localized or systemic, and lethal or merely an incidental finding. The most important numerically are AL amyloidosis, in which the fibrils are composed of monoclonal immunoglobulin light chains, and AA amyloidosis, in which the acute phase reactant Serum Amyloid A component forms the fibrils.The kidney is involved in 75% of patients with systemic amyloidosis. Heavy proteinuria or nephrotic syndrome is characteristic of most amyloid variants.Without treatment, systemic disease is usually fatal but measures that reduce the supply of amyloid fibril precursor proteins can result in regression of amyloid deposits, prevention of organ failure, and improved quality of life and survival. Early diagnosis, before irreversible organ damage has occurred, is the key to effective treatment. Recent advances in diagnosis and therapy have much improved the outlook of patients with AL amyloidosis, but agents with broader promise are under investigation.
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Amyloid Proteins Methods And Protocols. Humana Press, 2012.

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Book chapters on the topic "Amyloid Proteins (Amyloidosis)"

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Husby, Gunnar, and Knut Sletten. "Amyloid Proteins." In Amyloidosis, 23–34. Dordrecht: Springer Netherlands, 1986. http://dx.doi.org/10.1007/978-94-009-4309-4_2.

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Westermark, Per. "Endocrine Amyloid Fibril Proteins." In Amyloidosis, 39–42. Dordrecht: Springer Netherlands, 1986. http://dx.doi.org/10.1007/978-94-009-4309-4_4.

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Eriksen, Nils, and Earl P. Benditt. "Protein AA and Associated Proteins in Type-AA Amyloid Substance." In Amyloidosis, 3–10. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4613-2199-6_1.

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Benson, M. D. "Pathofibrillogenesis and Amyloid Proteins." In Amyloid and Amyloidosis 1990, 481–86. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3284-8_120.

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Shinoda, Tomotaka, Fuyuki Kametani, Hiroshi Tonoike, and Shozo Kito. "Salient Structural Features of Low Molecular Weight Amyloid Fibril Proteins in Familial Amyloid Polyneuropathy of Japanese Origin." In Amyloidosis, 331–37. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4613-2199-6_43.

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Linke, Reinhold P., Walter B. J. Nathrath, and Manfred Eulitz. "Classification of Amyloid Syndromes from Tissue Sections Using Antibodies Against Various Amyloid Fibril Proteins: Report of 142 Cases." In Amyloidosis, 599–605. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4613-2199-6_75.

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Sipe, J. D., F. C. De Beer, M. Pepys, A. Husebekk, B. Skogen, R. Kisilevsky, D. Selkoe, J. Buxbaum, R. P. Linke, and M. A. Gertz. "Report of Special Session on Bioassays and Standardization of Amyloid Proteins and Precursors." In Amyloid and Amyloidosis 1990, 883–89. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3284-8_216.

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Baba, Satoshi, Katsutoshi Miura, and Haruyuki Shirasawa. "In Vitro Assembly of Murine Amyloid a Protein, Two Murine Serum Amyloid a Proteins, and Normal Human Transthyretin to form Amyloid-Like Fibrils." In Amyloid and Amyloidosis 1990, 497–500. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3284-8_123.

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Rygg, M., G. Husby, B. Dowton, and G. Marhaug. "Primary Structure of Two Rabbit Serum Amyloid a Proteins (SAA) Based on cDNA Sequence." In Amyloid and Amyloidosis 1990, 40–43. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3284-8_10.

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Bellotti, V., A. Pucci, E. Arbustini, G. Merlini, M. Stoppin, G. Ferri, and E. F. Osserman. "High Molecular Weight Proteins, Sensitive to Collagenase Digestion are Intimate Constituents of Amyloid Deposits." In Amyloid and Amyloidosis 1990, 519–22. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3284-8_128.

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Conference papers on the topic "Amyloid Proteins (Amyloidosis)"

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Gurian, Jordana Gaudie, Maria Ondina Machado Diniz, Amanda Nascimento Bispo, Aline Boaventura Ferreira, and Fernando Elias Borges. "Case report: amyloidosis." In XIV Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2023. http://dx.doi.org/10.5327/1516-3180.141s1.361.

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Introduction: Amyloidosis is caused by the deposition of low molecular weight proteins in the extracellular space. Amyloid deposits can cause several clinical manifestations, according to the type, quantity and location, among them: renal and cardiac failure, neuropathy and joint manifestations. The definitive diagnosis is made by tissue biopsy, showing positivity for Congo red. Treatment is complex and depends on the type, but includes, for example, chemotherapy and hematopoietic cell transplantation. The aim is to report a case of amyloidosis in a patient at Hospital Geral de Goiânia. Information was obtained through clinical follow-up in a neurology ward. Case report: Male patient, 40 years old, with visual clouding and progression to bilateral total amaurosis. During the initial neurological investigation, signs of optic neuritis were found and the patient underwent pulse therapy, with no improvement. When returning to the neurologist, an Hb of 5 was found, as well as a significant change in renal function, and he was referred to the General Hospital of Goiânia for investigation. The patient had bilateral amaurosis, mydriatic pupils with mild plegia, without other neurological alterations, however, with systolic murmur, in addition to polyarthritis. Echo: moderate increase in myocardial thickness. diastolic dysfunction of ve and type 1. Necessary to rule out deposit/infiltrative disease. Due to the persistence of renal failure and the need to maintain hemodialysis, a renal biopsy was performed, obtaining positivity for Congo red in the tubules and glomerular wall. Conclusion: A previously healthy young patient with a subacute clinical picture was diagnosed with amyloidosis after a confirmatory biopsy. This report aims to contribute to future studies in this area because it is a disease that is still little known and needs further studies.
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Gonzalez, Deilys, Duncan Brown, Montserrat Vera Llonch, Aaron Yarlas, Kristen McCausland, and Asia Sikora Kessler. "Treatment satisfaction for gene silencing pharmacotherapies for the treatment of hereditary transthyretin amyloidosis with polyneuropathy." In XIII Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1516-3180.517.

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Background and Aims: Hereditary transthyretin amyloidosis (hATTR) is a rare, progressive, systemic, fatal condition in which misfolded transthyretin proteins form amyloid in tissues and organs, often manifesting in polyneuropathy (hATTR-PN). The FDA has approved 2 gene-silencing pharmacotherapies for hATTR-PN: inotersen, administered subcutaneously; and patisiran, administered intravenously. Patient satisfaction for each treatment was examined during a period overlapping with the COVID-19 pandemic. Methods: Patients with hATTR-PN (with and without accompanying cardiomyopathy) in the United States participated in an observational, online survey between January 1 and October 25, 2020. The Treatment Satisfaction Questionnaire for Medication, version II (TSQMvII), was administered to 29 patients currently being treated with inotersen (n=11) or patisiran (n=18). TSQMvII produces 4 scale scores—Effectiveness, Side Effects, Convenience, and Global Satisfaction—ranging from 0 to 100. Higher scores indicate greater satisfaction. TSQMvII scores were descriptively compared between treatment groups. Results: Patients receiving inotersen indicated greater satisfaction with convenience than patients receiving patisiran (mean, 76.3 [SD=19.4] vs 58.6 [15.3], respectively), and less dissatisfaction with treatment side effects (86.1 [16.4] vs 68.3 [19.0]). Ratings were comparable between treatments with respect to effectiveness (72.0 [21.5] vs 67.1 [19.7]) and global satisfaction (78.0 [20.0] vs 74.5 [21.7]). Conclusions: While inotersen and patisiran were rated similarly in effectiveness and overall treatment satisfaction, inotersen was associated with less dissatisfaction with side effects and greater convenience, with the latter possibly reflecting differences in mode of administration (ie, at home vs visit to a clinical site), which may be particularly important during a pandemic.
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Senhorinha, Gláucia Maria, Arlys Emanuel Mendes da Silva Santos, and Douglas Daniel Dophine. "The role of metabolic syndrome in Alzheimer’s disease." In XIII Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1516-3180.319.

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Background: Metabolic syndrome (MS) leads to the deposits formation of insoluble protein aggregates, neuroinflammation, oxidative stress, neuronal insulin resistance, progressive insulin resistance, desensitization and β-amyloid amyloidosis in the brain, besides direct ischemic effects which are closely associated with Alzheimer’s disease (AD).1 Objectives: The present study seeks to understand the role of the metabolic syndrome in the pathophysiology of Alzheimer’s disease and to describe preventive and therapeutic interventions. Methods: PUBMED and Web of Science were the databases used, the following descriptors were used to search the articles: “Alzheimer Disease” OR “Alzheimer Dementia” AND “Metabolic Syndrome”. Results: The studies in general have shown that MS is related to AD through brain insulin resistance, triggered by oxidative stress and neuroinflammation. It is related to the progressive atrophy of brain regions involved in the progression of AD. Insulin resistance in the brain is related to the progressive atrophy of the brain regions from initial progression of AD. These regions are cingulate cortices, medial temporal lobe, prefrontal gyri and other regions.³ Thus, there is an inhibition of the mechanisms of beta-amyloid removal, leading to its accumulation, which generates neuroinflammation, that in turn potentiates insulin resistance in the central nervous system, contributing to the genesis and progression of cognitive damage.2,3 Conclusions: Insulin resistance plays a major role in the initiation and perpetuation of cognitive impairment in AD. Furthermore, the components of the MS associated with AD, when treated with preventive and therapeutic measures, break this association by promoting rebalancing of the metabolism.
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Reports on the topic "Amyloid Proteins (Amyloidosis)"

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Elmann, Anat, Orly Lazarov, Joel Kashman, and Rivka Ofir. therapeutic potential of a desert plant and its active compounds for Alzheimer's Disease. United States Department of Agriculture, March 2015. http://dx.doi.org/10.32747/2015.7597913.bard.

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We chose to focus our investigations on the effect of the active forms, TTF and AcA, rather than the whole (crude) extract. 1. To establish cultivation program designed to develop lead cultivar/s (which will be selected from the different Af accessions) with the highest yield of the active compounds TTF and/or achillolide A (AcA). These cultivar/s will be the source for the purification of large amounts of the active compounds when needed in the future for functional foods/drug development. This task was completed. 2. To determine the effect of the Af extract, TTF and AcA on neuronal vulnerability to oxidative stress in cultured neurons expressing FAD-linked mutants.Compounds were tested in N2a neuroblastoma cell line. In addition, we have tested the effects of TTF and AcA on signaling events promoted by H₂O₂ in astrocytes and by β-amyloid in neuronal N2a cells. 3. To determine the effect of the Af extract, TTF and AcA on neuropathology (amyloidosis and tau phosphorylation) in cultured neurons expressing FAD-linked mutants. 4. To determine the effect of A¦ extract, AcA and TTF on FAD-linked neuropathology (amyloidosis, tau phosphorylation and inflammation) in transgenic mice. 5. To examine whether A¦ extract, TTF and AcA can reverse behavioral deficits in APPswe/PS1DE9 mice, and affect learning and memory and cognitive performance in these FAD-linked transgenic mice. Background to the topic.Neuroinflammation, oxidative stress, glutamate toxicity and amyloid beta (Ab) toxicity are involved in the pathogenesis of Alzheimer's diseases. We have previously purified from Achilleafragrantissimatwo active compounds: a protective flavonoid named 3,5,4’-trihydroxy-6,7,3’-trimethoxyflavone (TTF, Fl-72/2) and an anti-inflammatory sesquiterpenelactone named achillolide A (AcA). Major conclusions, solutions, achievements. In this study we could show that TTF and AcA protected cultured astrocytes from H₂O₂ –induced cell death via interference with cell signaling events. TTF inhibited SAPK/JNK, ERK1/2, MEK1 and CREBphosphorylation, while AcA inhibited only ERK1/2 and MEK1 phosphorylation. In addition to its protective activities, TTF had also anti-inflammatory activities, and inhibited the LPS-elicited secretion of the proinflammatorycytokinesInterleukin 6 (IL-6) and IL-1b from cultured microglial cells. Moreover, TTF and AcA protected neuronal cells from glutamate and Abcytotoxicity by reducing the glutamate and amyloid beta induced levels of intracellular reactive oxygen species (ROS) and via interference with cell signaling events induced by Ab. These compounds also reduced amyloid precursor protein net processing in vitro and in vivo in a mouse model for Alzheimer’s disease and improvedperformance in the novel object recognition learning and memory task. Conclusion: TTF and AcA are potential candidates to be developed as drugs or food additives to prevent, postpone or ameliorate Alzheimer’s disease. Implications, both scientific and agricultural.The synthesis ofAcA and TTF is very complicated. Thus, the plant itself will be the source for the isolation of these compounds or their precursors for synthesis. Therefore, Achilleafragrantissima could be developed into a new crop with industrial potential for the Arava-Negev area in Israel, and will generate more working places in this region.
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