Relevant bibliographies by topics / Type II diabetes; Amyloidosis; IAPP

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Academic literature on the topic 'Type II diabetes; Amyloidosis; IAPP'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Type II diabetes; Amyloidosis; IAPP"

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Pytowski, Lior, Chiu Fan Lee, Alex C. Foley, David J. Vaux, and Létitia Jean. "Liquid–liquid phase separation of type II diabetes-associated IAPP initiates hydrogelation and aggregation." Proceedings of the National Academy of Sciences 117, no. 22 (May 15, 2020): 12050–61. http://dx.doi.org/10.1073/pnas.1916716117.

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Amyloidoses (misfolded polypeptide accumulation) are among the most debilitating diseases our aging societies face. Amyloidogenesis can be catalyzed by hydrophobic–hydrophilic interfaces (e.g., air–water interface in vitro [AWI]). We recently demonstrated hydrogelation of the amyloidogenic type II diabetes-associated islet amyloid polypeptide (IAPP), a hydrophobic–hydrophilic interface-dependent process with complex kinetics. We demonstrate that human IAPP undergoes AWI-catalyzed liquid–liquid phase separation (LLPS), which initiates hydrogelation and aggregation. Insulin modulates these processes but does not prevent them. Using nonamyloidogenic rat IAPP, we show that, whereas LLPS does not require the amyloidogenic sequence, hydrogelation and aggregation do. Interestingly, both insulin and rat sequence delayed IAPP LLPS, which may reflect physiology. By developing an experimental setup and analysis tools, we show that, within the whole system (beyond the droplet stage), macroscopic interconnected aggregate clusters form, grow, fuse, and evolve via internal rearrangement, leading to overall hydrogelation. As the AWI-adsorbed gelled layer matures, its microviscosity increases. LLPS-driven aggregation may be a common amyloid feature and integral to pathology.
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Gudkova, Alexandra Ya, Olga I. Antimonova, and Mikhail M. Shavlovsky. "Role of pancreatic amyloidosis in pathogenesis of type 2 diabetes mellitus." Medical academic journal 19, no. 2 (September 18, 2019): 27–36. http://dx.doi.org/10.17816/maj19227-36.

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The occurrence of type 2 diabetes mellitus (T2DM) in developed countries is currently becoming epidemic primarily due to the changes in quality of life. This disease typically makes progress for a long time, and its clinical pattern is mostly related to various micro- and macrovascular complications. In addition to said complications the pancreas itself often undergoes damage associated with amyloid formation in islets of Langerhans which results in a toxic effect on the hormone-producing islet cells. Ultimately, hormone overproduction in T2DM shifts to hormone deficiency. The crucial causative factor of the development of pancreatic amyloidosis in T2DM is а short peptide hormone, amylin (IAPP), which is cosecreted with insulin and considered to be a kind of insulin antagonist. The present review reports structure, functions and amyloidogenic properties of human IAPP. The basic concepts of molecular and cellular aspects concerning pathogenesis of pancreatic amyloidosis have been provided. Patterns of the development of pancreatic amyloid lesions and possible approaches for early diagnosis and treatment of this significant complication of T2DM have been discussed.
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Roesti, Elisa S., Christina N. Boyle, Daniel T. Zeman, Marcos Sande-Melon, Federico Storni, Gustavo Cabral-Miranda, Alexander Knuth, Thomas A. Lutz, Monique Vogel, and Martin F. Bachmann. "Vaccination Against Amyloidogenic Aggregates in Pancreatic Islets Prevents Development of Type 2 Diabetes Mellitus." Vaccines 8, no. 1 (March 2, 2020): 116. http://dx.doi.org/10.3390/vaccines8010116.

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Type 2 diabetes mellitus (T2DM) is a chronic progressive disease characterized by insulin resistance and insufficient insulin secretion to maintain normoglycemia. The majority of T2DM patients bear amyloid deposits mainly composed of islet amyloid polypeptide (IAPP) in their pancreatic islets. These—originally β-cell secretory products—extracellular aggregates are cytotoxic for insulin-producing β-cells and are associated with β-cell loss and inflammation in T2DM advanced stages. Due to the absence of T2DM preventive medicaments and the presence of only symptomatic drugs acting towards increasing hormone secretion and action, we aimed at establishing a novel disease-modifying therapy targeting the cytotoxic IAPP deposits in order to prevent the development of T2DM. We generated a vaccine based on virus-like particles (VLPs), devoid of genomic material, coupled to IAPP peptides inducing specific antibodies against aggregated, but not monomeric IAPP. Using a mouse model of islet amyloidosis, we demonstrate in vivo that our vaccine induced a potent antibody response against aggregated, but not soluble IAPP, strikingly preventing IAPP depositions, delaying onset of hyperglycemia and the induction of the associated pro-inflammatory cytokine Interleukin 1β (IL-1β). We offer the first cost-effective and safe disease-modifying approach targeting islet dysfunction in T2DM, preventing pathogenic aggregates without disturbing physiological IAPP function.
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Akter, Rehana, Ping Cao, Harris Noor, Zachary Ridgway, Ling-Hsien Tu, Hui Wang, Amy G. Wong, et al. "Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology." Journal of Diabetes Research 2016 (2016): 1–18. http://dx.doi.org/10.1155/2016/2798269.

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The hormone islet amyloid polypeptide (IAPP, or amylin) plays a role in glucose homeostasis but aggregates to form islet amyloid in type-2 diabetes. Islet amyloid formation contributes toβ-cell dysfunction and death in the disease and to the failure of islet transplants. Recent work suggests a role for IAPP aggregation in cardiovascular complications of type-2 diabetes and hints at a possible role in type-1 diabetes. The mechanisms of IAPP amyloid formationin vivoorin vitroare not understood and the mechanisms of IAPP inducedβ-cell death are not fully defined. Activation of the inflammasome, defects in autophagy, ER stress, generation of reactive oxygen species, membrane disruption, and receptor mediated mechanisms have all been proposed to play a role. Open questions in the field include the relative importance of the various mechanisms ofβ-cell death, the relevance of reductionist biophysical studies to the situationin vivo, the molecular mechanism of amyloid formationin vitroandin vivo, the factors which trigger amyloid formation in type-2 diabetes, the potential role of IAPP in type-1 diabetes, the development of clinically relevant inhibitors of islet amyloidosis toxicity, and the design of soluble, bioactive variants of IAPP for use as adjuncts to insulin therapy.
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Westermark, Gunilla T., and Per Westermark. "Transthyretin and Amyloid in the Islets of Langerhans in Type-2 Diabetes." Experimental Diabetes Research 2008 (2008): 1–7. http://dx.doi.org/10.1155/2008/429274.

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Transthyretin (TTR) is a major amyloid fibril protein in certain systemic forms of amyloidosis. It is a plasma protein, mainly synthesized by the liver but expression occurs also at certain minor locations, including the endocrine cells in the islets of Langerhans. With the use of immunohistochemistry and in situ hybridization, we have studied the distribution of transthyretin-containing cells in islets of Langerhans in type-2 diabetic and nondiabetic individuals. TTR expression was particularly seen in alpha (glucagon) cells. Islets from type-2 diabetic patients had proportionally more transthyretin-reactive islet cells, including beta cells. A weak transthyretin immunoreaction in IAPP-derived amyloid occurred in some specimens. In seeding experiments in vitro, we found that TTR fibrils did not seed IAPP while IAPP fibrils seeded TTR. It is suggested that islet expression of transthyretin may be altered in type-2 diabetes.
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Raleigh, Daniel, Xiaoxue Zhang, Benoît Hastoy, and Anne Clark. "The β-cell assassin: IAPP cytotoxicity." Journal of Molecular Endocrinology 59, no. 3 (October 2017): R121—R140. http://dx.doi.org/10.1530/jme-17-0105.

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Islet amyloid polypeptide (IAPP) forms cytotoxic oligomers and amyloid fibrils in islets in type 2 diabetes (T2DM). The causal factors for amyloid formation are largely unknown. Mechanisms of molecular folding and assembly of human IAPP (hIAPP) into β-sheets, oligomers and fibrils have been assessed by detailed biophysical studies of hIAPP and non-fibrillogenic, rodent IAPP (rIAPP); cytotoxicity is associated with the early phases (oligomers/multimers) of fibrillogenesis. Interaction with synthetic membranes promotes β-sheet assembly possibly via a transient α-helical molecular conformation. Cellular hIAPP cytotoxicity can be activated from intracellular or extracellular sites. In transgenic rodents overexpressing hIAPP, intracellular pro-apoptotic signals can be generated at different points in β-cell protein synthesis. Increased cellular trafficking of proIAPP, failure of the unfolded protein response (UPR) or excess trafficking of misfolded peptide via the degradation pathways can induce apoptosis; these data indicate that defects in intracellular handling of hIAPP can induce cytotoxicity. However, there is no evidence for IAPP overexpression in T2DM. Extracellular amyloidosis is directly related to the degree of β-cell apoptosis in islets in T2DM. IAPP fragments, fibrils and multimers interact with membranes causing disruption in vivo and in vitro. These findings support a role for extracellular IAPP in β-sheet conformation in cytotoxicity. Inhibitors of fibrillogenesis are useful tools to determine the aberrant mechanisms that result in hIAPP molecular refolding and islet amyloidosis. However, currently, their role as therapeutic agents remains uncertain.
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NAKAZATO, Masamitsu, and Shigeru MATSUKURA. "New Type of Amyloidosis. Islet Amyloid Polypeptide(IAPP/Amylin) in Non-Insulin-Dependent Diabetes Mellitus." Internal Medicine 32, no. 12 (1993): 928–29. http://dx.doi.org/10.2169/internalmedicine.32.928.

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Tomasello, Marianna Flora, Alessandro Sinopoli, and Giuseppe Pappalardo. "On the Environmental Factors Affecting the Structural and Cytotoxic Properties of IAPP Peptides." Journal of Diabetes Research 2015 (2015): 1–15. http://dx.doi.org/10.1155/2015/918573.

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Pancreatic islets in type 2 diabetes mellitus (T2DM) patients are characterized by reducedβ-cells mass and diffuse extracellular amyloidosis. Amyloid deposition involves the islet amyloid polypeptide (IAPP), a neuropancreatic hormone cosecreted with insulin byβ-cells. IAPP is physiologically involved in glucose homeostasis, but it may turn toxic toβ-cells owing to its tendency to misfold giving rise to oligomers and fibrils. The process by which the unfolded IAPP starts to self-assemble and the overall factors promoting this conversion are poorly understood. Other open questions are related to the nature of the IAPP toxic species and how exactlyβ-cells die. Over the last decades, there has been growing consensus about the notion that early molecular assemblies, notably small hIAPP oligomers, are the culprit ofβ-cells decline. Numerous environmental factors might affect the conformational, aggregation, and cytotoxic properties of IAPP. Herein we review recent progress in the field, focusing on the influences that membranes, pH, and metal ions may have on the conformational conversion and cytotoxicity of full-length IAPP as well as peptide fragments thereof. Current theories proposed for the mechanisms of toxicity will be also summarized together with an outline of the underlying molecular links between IAPP and amyloid beta (Aβ) misfolding.
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Nguyen, Phuong Trang, Nagore Andraka, Carole Anne De Carufel, and Steve Bourgault. "Mechanistic Contributions of Biological Cofactors in Islet Amyloid Polypeptide Amyloidogenesis." Journal of Diabetes Research 2015 (2015): 1–13. http://dx.doi.org/10.1155/2015/515307.

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Type II diabetes mellitus is associated with the deposition of fibrillar aggregates in pancreatic islets. The major protein component of islet amyloids is the glucomodulatory hormone islet amyloid polypeptide (IAPP). Islet amyloid fibrils are virtually always associated with several biomolecules, including apolipoprotein E, metals, glycosaminoglycans, and various lipids. IAPP amyloidogenesis has been originally perceived as a self-assembly homogeneous process in which the inherent aggregation propensity of the peptide and its local concentration constitute the major driving forces to fibrillization. However, over the last two decades, numerous studies have shown a prominent role of amyloid cofactors in IAPP fibrillogenesis associated with the etiology of type II diabetes. It is increasingly evident that the biochemical microenvironment in which IAPP amyloid formation occurs and the interactions of the polypeptide with various biomolecules not only modulate the rate and extent of aggregation, but could also remodel the amyloidogenesis process as well as the structure, toxicity, and stability of the resulting fibrils.
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Fortin, Jessica S., and Marie-Odile Benoit-Biancamano. "Inhibition of islet amyloid polypeptide aggregation and associated cytotoxicity by nonsteroidal anti-inflammatory drugs." Canadian Journal of Physiology and Pharmacology 94, no. 1 (January 2016): 35–48. http://dx.doi.org/10.1139/cjpp-2015-0117.

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Nonsteroidal anti-inflammatory drugs (NSAIDs) constitute an important pharmacotherapeutic class that, over the past decade, have expanded in application to a panoply of medical conditions. They have been tested for neurodegenerative diseases such as Alzheimer’s to reduce inflammation and also in the attempt to abrogate amyloid deposition. However, the use of NSAIDs as aggregation inhibitors has not been extensively studied in pancreatic amyloid deposition. Pancreatic amyloidosis involves the misfolding of islet amyloid polypeptide (IAPP) and contributes to the progression of type-2 diabetes in humans and felines. To ascertain their antiamyloidogenic activity, several NSAIDs were tested using fluorometric thioflavin-T assays, circular dichroism, photo-induced cross-linking assays, and cell culture. Celecoxib, diclofenac, indomethacin, meloxicam, niflumic acid, nimesulide, phenylbutazone, piroxicam, sulindac, and tenoxicam reduced fibrillization at a molar ratio of 1:10. The circular dichroism spectra of diclofenac, piroxicam, and sulindac showed characteristic spectral signatures found in predominantly α-helical structures. The oligomerization of human IAPP was abrogated with diclofenac and sulindac at a molar ratio of 1:5. The cytotoxic effects of pre-incubated human IAPP on cultured INS-1 cells were noticeably reduced in the presence of diclofenac, meloxicam, phenylbutazone, sulindac, and tenoxicam at a molar ratio of 1:10. Our results demonstrate that NSAIDs can provide chemical scaffolds to generate new and promising antiamyloidogenic agents that can be used alone or as a coadjuvant therapy.
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Dissertations / Theses on the topic "Type II diabetes; Amyloidosis; IAPP"

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Badman, Michael Keith. "Cellular mechanisms for islet amyloid formation and degradation." Thesis, University of Oxford, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.294384.

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Christakopoulos, Fotios. "Modeling of beta-cell Metabolic Activity and Islet Function : a Systems Approach to Type II Diabetes." Thesis, KTH, Skolan för teknik och hälsa (STH), 2016. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-192692.

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Diabetes has gained growing attendance as one of the key non communicable diseases (NCD) with the World Health Organization identifying it as the focus of the World Health Day 2016. It is reported that more than 420 million people suffer from diabetes, a number predicted to rise in the coming years. This report forms part of a broader, long term focus project that aims to establish a systems approach to type 2 diabetes (T2D), the variant that accounts for more than 90% of reported diabetes cases. The broader project objectives are to identify possible biomarkers for the onset and the progression of T2D as a precursor to enable potential future approaches to delay onset, or even reverse disease states, via active bio-compounds and/or establishment of beneficial nutritional patterns. The 6-month master’s work reported here is sub-project that focused specifically on cell level vesicle trafficking processes. These processes are believed to be crucial in understanding the formation amyloid plaques, which compromise or kill the insulin secreting beta cells. Up until now, there has been a lack of appropriate experimental techniques to directly observe this process in live cells.  Hence we have developed 2 new techniques: (i)               a method of imaging the actin and tubulin network reorganization during exocytosis of the insulin containing granules while exploring novel ways of characterizing the network. (ii)             a method of imaging the granules themselves and using particle tracking microrheology to analyze their movement patterns during stimulation with glucose. These new techniques open the door to follow up experiments which would allow development of a cell scale mathematical model or simulation correlating short term glucose dynamics to risk of amyloid plaque formation and T2D.
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Miraee-Nedjad, Samaneh. "Early events in the onset of type II diabetes : effects of aggregated amylin (IAPP) on the islet proteome and metabolic pathways." Thesis, University of Manchester, 2013. https://www.research.manchester.ac.uk/portal/en/theses/early-events-in-the-onset-of-type-ii-diabetes-effects-of-aggregated-amylin-iapp-on-the-isletproteome-and-metabolic-pathways(55b2f0a5-f312-4276-8dfd-d94a0ee04232).html.

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Many diseases are caused by proteins or peptides folding incorrectly and aggregating into fibrils or plaques, including Alzheimer’s disease, Parkinson's disease and type II diabetes. Amyloid formation in the human pancreas occurs via the aggregation of a 37 amino acid peptide called amylin or IAPP which is shown to be toxic to pancreatic β cells. Amylin (IAPP) aggregation initiates a large number of events, leading ultimately to cell death. However the exact cytotoxic action of human IAPP and also the underlying molecular events leading from amylin (IAPP) aggregation to β cell death is still unknown. The toxic effect of human amylin (IAPP) is thought to involve changes in the expression of several genes and proteins. Further transcriptional and proteomics studies in this field can therefore facilitate the identifications of new targets whose expression are affected by amylin (IAPP). These information could be further used to construct an integrated model of the signalling and regulatory pathways through which amylin (IAPP) interacts with cellular metabolism.To investigate the effects of amylin (IAPP) aggregation on the islets proteome in this study, rat Rin-5F cell line, reported as a model of pancreatic β cell, was used. MTT assay was initially performed to determine the effect of IAPP on the cell viability at different time points. The isolated proteins form the untreated and IAPP treated Rin-5F cells were then fractionated by off gel electrophoresis and analysed by quantitative label free LC- MS/MS approach.Label free quantification of IAPP treated Rin-5F cells has identified the altered expression of many proteins, some of which were previously suggested in the literature to be involved in the pathogenesis of type 2 diabetes. These proteins were map to several pathways (including glycolysis and proteasome) whose expressions were significantly affected upon amylin (IAPP) exposure. The IAPP responsive proteins were also structured into a well connected network. Some of the hub proteins identified in this network were greatly affected as the result of IAPP treatments of RIN-5F cells. Our data therefore revealed the effect of IAPP on several proteins and pathways that might be important in the pathogenesis of type 2 diabetes.
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Radovan, Diana [Verfasser]. "Fluorescence microscopy studies on the fibrillation of IAPP at model and cellular lipid interfaces, from mechanism to potential strategies in type II diabetes mellitus / von Diana Radovan." 2009. http://d-nb.info/99895683X/34.

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Book chapters on the topic "Type II diabetes; Amyloidosis; IAPP"

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Berends, M. J. H., M. G. Nieuwenhuis, C. J. M. Lips, A. P. R. Blok, E. C. M. Ooms, and R. W. Veldhuizen. "A Comparative Study Between Human B-Cell Insulin and Islet Amyloid Polypeptide (IAPP) Storage and Amyloid Deposition in Type 2 Diabetes Mellitus and in Non-Diabetics." In Amyloid and Amyloidosis 1990, 457–61. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3284-8_114.

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2

Montane, Joel, and Anna Novials. "The Role of Human IAPP in Stress and Inflammatory Processes in Type 2 Diabetes." In Exploring New Findings on Amyloidosis. InTech, 2016. http://dx.doi.org/10.5772/63010.

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