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Dissertations / Theses on the topic 'Islet Amyloid Polypeptide – genetics'

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Published: 4 June 2021

Last updated: 1 February 2022

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1

Paulsson, Johan F. "Proislet Amyloid Polypeptide (proIAPP) : Impaired Processing is an Important Factor in Early Amyloidogenesis in Type 2 Diabetes." Doctoral thesis, Linköping : Linköping University, 2006. http://www.bibl.liu.se/liupubl/disp/disp2006/med967s.pdf.

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2

Wiltzius, Jed John William. "Structural studies of islet amyloid polypeptide." Diss., Restricted to subscribing institutions, 2008. http://proquest.umi.com/pqdweb?did=1691848941&sid=6&Fmt=2&clientId=1564&RQT=309&VName=PQD.

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3

Jaikaran, Emma Tracy Araminta Sunita. "Factors influencing human islet amyloid polypeptide fibril formation." Thesis, University of Oxford, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.342537.

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4

Hull, Rebecca L. "Pro-islet amyloid polypeptide and type 2 diabetes." Thesis, University of Nottingham, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.285837.

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5

Westwell-Roper, Clara Yolande. "Islet amyloid polypeptide aggregation is a local trigger for pancreatic islet inflammation." Thesis, University of British Columbia, 2014. http://hdl.handle.net/2429/46729.

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Patients with type 2 diabetes experience an inevitable deterioration of glycemic control leading to long-term complications and dependence on exogenous insulin. Amyloid deposition, macrophage infiltration, and upregulation of pro-inflammatory cytokines are common pathological features of both type 2 diabetic and transplanted islets. Islet amyloid is comprised primarily of aggregates of islet amyloid polypeptide (IAPP), a peptide that is co-secreted with insulin by beta cells. IAPP fibrils share a common cross-β-sheet structure with other amyloids of mammalian and microbial origin that activate

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6

MacArthur, Diane L. A. "Amyloid fibril formation in islets of transgenic mice expressing human islet amyloid polypeptide." Thesis, University of Oxford, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.325942.

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7

Higham, Claire Emily. "Biophysical properties, fibril formation and processing of islet amyloid polypeptide." Thesis, University of Oxford, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.312105.

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8

Bhogal, Rashpal Kaur. "Factors influencing islet amyloid polypeptide degradation, cytotoxicity and fibril formation." Thesis, University of Oxford, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.401100.

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9

Oskarsson, Marie. "Islet amyloid polypeptide (IAPP) in Type 2 diabetes and Alzheimer disease." Doctoral thesis, Uppsala universitet, Institutionen för medicinsk cellbiologi, 2015. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-265501.

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The misfolding and aggregation of the beta cell hormone islet amyloid polypeptide (IAPP) into amyloid fibrils is the main pathological finding in islets of Langerhans in type 2 diabetes. Pathological assemblies of IAPP are cytotoxic and believed to contribute to the loss of insulin-producing beta cells. Changes in the microenvironment that could trigger the aggregation of IAPP are largely unknown. So is the possibility that islet amyloid can spread within or between tissues. The present thesis have explored the roles of glycosaminoglycan heparan sulfate (HS) and the novel anti-amyloid chaperon

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10

Courtade, Jaques. "Impaired pro-islet amyloid polypeptide processing promotes beta-cell dysfunction in diabetes and islet transplants." Thesis, University of British Columbia, 2016. http://hdl.handle.net/2429/59064.

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Soaring rates of diabetes highlight the importance of controlling this global epidemic, with an estimated 415 million people thought to be living with diabetes in 2015. The defining characteristic of diabetes is elevated fasting blood glucose levels, or hyperglycemia, which if not controlled promotes long-term complications such as neuropathy, kidney failure and damage to blood vessels. Glucose homeostasis is primarily controlled by pancreatic islets, cell clusters that mediate the endocrine functions of the pancreas. To manage circulating glucose concentrations, islet beta cells synthesize pr

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11

Schultz, Sebastian. "Studies on Islet Amyloid Polypeptide Aggregation : From Model Organism to Molecular Mechanisms." Doctoral thesis, Linköpings universitet, Cellbiologi, 2011. http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-70094.

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The proper folding of a protein into its defined three--‐dimensional structure is one of the many fundamental challenges a cell encounters. A number of tightly controlled pathways have evolved to assist in the proper folding of a protein, but also to aid in the removal of misfolded proteins. Despite the presence of these pathways accumulation of misfolded proteins can still occur. Amyloid deposits consist of misfolded proteins with a characteristic highly ordered fibrillar structure that will exert affinity for the amyloid dye Congo red and has a unique X-ray diffraction pattern. Currently 27

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12

Arnelo, Urban. "Islet amyloid polypeptide in the control of food intake : an experimental study in the rat /." Stockholm, 1997. http://diss.kib.ki.se/1997/91-628-2778-2.

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13

Bailey, James. "Phenomenological modeling of the nucleated polymerization of human islet amyloid polypeptide : a combined experimental and theoretical approach." Thesis, University of British Columbia, 2008. http://hdl.handle.net/2429/2441.

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The inverse scattering problem is based on the scattering theory in physics, where measured data such as radiation from an object is used to determine the unique structure of the object in question. This approach has been widely successful in fields ranging from geophysics and medical imaging, to quantum field theory. In 1996 Henrik Flyvbjerg suggested that a similar approach could be used to study a reaction far from equilibrium of the self-assembly of a nucleation dependent biopolymer and, under certain conditions, uniquely determine the kinetics of the assembly. Here we use this approach to

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14

Wang, Feng. "Interaction between pancreatic cancer and beta cells : intraislet significance of islet amyloid polypeptide /." Stockholm, 1998. http://diss.kib.ki.se/1998/91-628-3300-6/.

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15

Brown, Anne M. "Insights into Mechanisms of Amyloid Toxicity: Molecular Dynamics Simulations of the Amyloid andbeta-peptide (Aandbeta) and Islet Amyloid Polypeptide (IAPP)." Diss., Virginia Tech, 2016. http://hdl.handle.net/10919/73773.

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Aggregation of proteins into amyloid deposits is a common feature among dozens of diseases. Two such diseases that feature amyloid deposits are Alzheimer's disease (AD) and type 2 diabetes (T2D). AD toxicity has been associated with the aggregation and accumulation of the amyloid β-peptide (Aβ); Aβ exerts its toxic effects through interactions with neuronal cell membranes. A characteristic feature of T2D is the deposition of the islet amyloid polypeptide (IAPP) in the pancreatic islets of Langerhans. It is currently unknown if IAPP aggregation is a cause or consequence of T2D, but it does lead

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16

Ma, Zhi. "Islet amyloid polypeptide (IAPP) : mechanisms of amyloidogenesis in the pancreatic islets and potential roles in diabetes mellitus /." Linköping : Univ, 2001. http://www.bibl.liu.se/liupubl/disp/disp2001/med655s.pdf.

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17

Karlsson, Ella. "Studies of neuropeptides in pancreatic beta cell function with special emphasis on islet amyloid polypeptide (IAPP)." Doctoral thesis, Uppsala University, Department of Medical Cell Biology, 2000. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-560.

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<p>The presence of protein amyloid in pancreas and its association to diabetes was first described 100 years ago in 1901, but was not identified as Islet Amyloid Polypeptide (IAPP) until 1986. The aim of the present work was to determine the role of the beta cell hormone, IAPP, in normal pancreatic islet physiology and during early disturbances of islet function.</p><p>Intra-islet peptides, i.e. chromogranin peptides and an extra-islet peptide, i.e. leptin, were studied to identify possible endogenous regulators of IAPP and insulin secretion. Chromogranin-B, but not chromogranin-A or pancreast

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18

Carmen, Helder. "The role of the cellular membrane environment in mediating fibrillization and toxicity of islet amyloid polypeptide." Thesis, University of Oxford, 2016. https://ora.ox.ac.uk/objects/uuid:e4641aca-4f99-408a-94d8-3819f8bf726e.

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Islet amyloid polypeptide (IAPP) is a peptide that is produced by the beta cells in the pancreas. A misfolded, aggregated form of this peptide is associated with Type 2 Diabetes and is found as large brils in pancreata, intimately associated with the islet architecture. The role of these brils is though to be benign in terms of membrane damage. However, smaller oligomers that assemble en-route to becoming brils are thought to be toxic to cells. In addition, the assembly of the peptide into amyloid is known to be accelerated by lipid and the assembly process itself has been shown to cause damag

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19

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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20

Allsop, Ben. "The role of amylin in Alzheimer's disease." Thesis, University of Manchester, 2017. https://www.research.manchester.ac.uk/portal/en/theses/the-role-of-amylin-in-alzheimers-disease(0667f0c6-8621-4a0b-b9ab-10d3d3730cd2).html.

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Type II diabetes mellitus (T2D) and Alzheimer's disease (AD) share aetiology and have a high incidence of co-morbidity. Evidence suggests that both diseases are caused by the pathogenic aggregation of an intrinsically disordered native amyloid peptide. Furthermore, T2D and AD share risk factors such as age, obesity and vascular health. Recent studies demonstrate that amylin, an amyloidogenic pancreatic hormone deposited in the pancreas in T2D, is also deposited in the brain in AD. We hypothesised that amylin directly contributes to AD through deposition in the brain and activation of pathogeni

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21

Tran, Thi Thuy Linh. "Étude théorique de peptides amyloidogènes : Ensemble conformationnel, oligomérisation et inhibition par des ligands peptidomimétiques." Thesis, Université Paris-Saclay (ComUE), 2016. http://www.theses.fr/2016SACLS518.

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De nombreuses protéines associées aux maladies neurodégénératives humaines sont intrinsèquement désordonnées. Ce sont des protéines qui sont dépourvues de structure tertiaire ou secondaire stable dans des conditions physiologiques. Plus précisément, les protéines intrinsèquement désordonnées (IDPs) subissent diverses changements conformationnels entre la pelote aléatoire, des conformations hélicoïdales et des structures en feuillet-β, ces deux dernières étant généralement impliquées dans la reconnaissance protéine-protéine. Parmi une vingtaine de peptides amyloïdogènes connus liés aux maladies

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22

Salazar, Vázquez Lilian Shadai. "How protein misfolding can lead to cellular dysfunction and disease : the case of islet amyloid polypeptide involved in type 2 diabetes mellitus." Thesis, Sorbonne université, 2019. https://accesdistant.sorbonne-universite.fr/login?url=http://theses-intra.upmc.fr/modules/resources/download/theses/2019SORUS371.pdf.

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Pour avoir une fonction biologique, une protéine se replie dans une structure spécifique. La cellule contrôle le repliement correct des protéines et dispose de mécanismes pour détecter et éliminer les protéines mal repliées. Néanmoins, certaines protéines évitent ce processus de contrôle. Les protéines amyloïdes sont des protéines mal repliées qui forment un type caractéristique de fibrilles amyloïdes allongées; en fonction de la séquence protéique et du site de dépôt de l'amyloïde, ils sont liés à différentes maladies. Le polypeptide amyloïde d'îlot (IAPP), un peptide de 37 acides aminés copr

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23

Weirich, Franziska [Verfasser], Henrike [Gutachter] Heise, and Manuel [Gutachter] Etzkorn. "Structural characterization of recombinant fibrillar human Islet Amyloid Polypeptide by solid-state Nuclear Magnetic Resonance Spectroscopy / Franziska Weirich ; Gutachter: Henrike Heise, Manuel Etzkorn." Düsseldorf : Universitäts- und Landesbibliothek der Heinrich-Heine-Universität Düsseldorf, 2017. http://d-nb.info/1137699930/34.

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24

Andreetto, Erika [Verfasser], Aphrodite Akademischer Betreuer] Kapurniotu та Horst [Akademischer Betreuer] [Kessler. "Identification of sequences of the interaction interface of β-amyloid peptide (Aβ) and islet amyloid polypeptide (IAPP) and synthesis and characterization of IAPP-derived inhibitors of Aβ aggregation / Erika Andreetto. Gutachter: Horst Kessler ; Aphrodite Kapurniotu. Betreuer: Aphrodite Kapurniotu". München : Universitätsbibliothek der TU München, 2011. http://d-nb.info/1056936630/34.

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25

Lesma, Jacopo. "β-Hairpin peptidomimetics as inhibitors of hIAPP amyloid protein aggregation : design, synthesis and evaluation Introducing sequential aza-amino acids units induces repeated ß-turns and helical conformations in peptides β-Hairpin peptide mimics decrease human Islet Amyloid Polypeptide (hIAPP) Aggregation". Thesis, université Paris-Saclay, 2020. http://www.theses.fr/2020UPASQ018.

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Le diabète de type 2 (DT2), qui compte plus de 400 millions de cas dans le monde, représente 90 % du nombre total de cas de diabète. T2D est une maladie dégénérative associée à la résistance à l’insuline et à la mort des β-cellules pancréatiques liées aux dépôts de la protéine amyloïde hIAPP (également appelée amyline), qui sont observés dans le pancréas de plus de 95 % des patients atteints de DT2. Les traitements actuellement disponibles sont symptomatiques et caractérisés soit par des effets secondaires significatifs, soit par un faible impact sur l’incidence des pathologies associées et la

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26

"Genetic association of islet amyloid polypeptide (IAPP) encoding pathways in pancreatic beta-cells with type 2 diabetes complemented by functional study." Thesis, 2011. http://library.cuhk.edu.hk/record=b6075147.

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Lam, Kwok Lim.<br>"October 2010."<br>Thesis (Ph.D.)--Chinese University of Hong Kong, 2011.<br>Includes bibliographical references (leaves 142-173).<br>Electronic reproduction. Hong Kong : Chinese University of Hong Kong, [2012] System requirements: Adobe Acrobat Reader. Available via World Wide Web.<br>Abstract also in Chinese.

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27

"The role of cystic fibrosis transmembrane conductance regulator in insulin secretion in pancreatic islet β-cells". 2013. http://library.cuhk.edu.hk/record=b5549850.

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囊性纖維化（CF）是由囊性纖維化跨膜電導調節器（CFTR）的突變引起的一種隱性遺傳病。CF病人的肺、肝、胰腺、腸道與生殖道受到嚴重影響，其中有50%的成年病人患有糖尿病。由CF引起的糖尿病被稱為CF相關糖尿病（CFRD）, 关于它的病因至今仍然存有爭議。2007年，人們發現CFTR在分泌胰島素的胰島β細胞上有表達。儘管如此，β細胞上的CFTR与糖尿病发病的关系却一直被忽略。我們的研究目標是闡述β細胞上的CFTR在胰島素分泌中的作用。<br>在β細胞上，葡萄糖刺激的胰島素分泌伴隨著複雜的電活動，這種電活動被描述為細胞膜電位去极化疊加的動作電位的爆發。葡萄糖引起的ATP敏感的鉀離子通道（K[subscript Asubscript Tsubscript P]）的關閉被普遍認為是β細胞去極化的初始事件，初始的去極化啟動了電壓依賴的鈣離子通道，由此產生的鈣離子內流成為構成動作電位的去極化電流，引起了細胞內鈣離子的震盪，從而引起胰島素的釋放。雖然氯離子電流被認為參與了β細胞去極化電流，但是，人們仍然不能確定是哪一種氯離子通道介導了這個去極化電流。在我們研究的第一部分，CFTR被證明功能性的表達在β細胞上，並且可以被葡萄糖激活。CFTR可以被葡萄糖激活这一性质，在CFTR超表達的CHO 细胞上被進一步驗證。在原代培養的β細胞與β細胞株RIN-5F细胞中的葡萄糖引起的全細胞電流、膜電位的去極化、

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28

"Interactions driving the collapse of islet amyloid polypeptide: implications for amyloid aggregation." Doctoral diss., 2013. http://hdl.handle.net/2286/R.I.20957.

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abstract: Human islet amyloid polypeptide (hIAPP), also known as amylin, is a 37-residue intrinsically disordered hormone involved in glucose regulation and gastric emptying. The aggregation of hIAPP into amyloid fibrils is believed to play a causal role in type 2 diabetes. To date, not much is known about the monomeric state of hIAPP or how it undergoes an irreversible transformation from disordered peptide to insoluble aggregate. IAPP contains a highly conserved disulfide bond that restricts hIAPP(1-8) into a short ring-like structure: N_loop. Removal or chemical reduction of N_loop not only

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29

Park, Kirily. "Domains in islet amyloid polypeptide important in fibril formation and toxicity." Thesis, 2003. http://hdl.handle.net/2429/15100.

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Islet amyloid deposits are a characteristic pathologic lesion o f the pancreas in type 2 diabetes and are composed primarily of the islet beta cell peptide islet amyloid polypeptide (IAPP or amylin). Islet amyloid fibrils are toxic to insulin-producing beta cells. Heparan sulfate proteoglycans (HSPGs) are also a component of islet amyloid in vivo and accelerate amyloid fibril formation in vitro. Although the cause of amyloid formation in pancreatic islets is unknown, HSPGs have been proposed to play an initiating role. Impaired processing of proIAPP, the IAPP precursor, has also been imp

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30

Félix, Filipa Isabel Bernardo. "Islet amyloid polypeptide - IAPP - as a risk factor for diabetes mellitus." Master's thesis, 2018. http://hdl.handle.net/10451/32691.

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Tese de mestrado em Biologia Molecular e Genética, apresentada à Universidade de Lisboa, através da Faculdade de Ciências, em 2018<br>A Diabetes mellitus (DM) é definida como uma desordem metabólica caraterizada por hiperglicemia crónica e alterações no metabolismo de glícidos, lípidos e proteínas devido à insuficiente secreção e/ou ação de insulina. A DM pode ser dividida em duas grandes classes: a Diabetes tipo 1 (T1DM) que engloba 5-10% dos casos de doença e carateriza-se pela ocorrência da destruição auto imune das células β do pâncreas. A segunda classe denomina-se de diabetes tipo 2 (T2D

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31

Hsu, Yi-Hsuan, and 許以萱. "Exploring the effect of glycation on the aggregation of islet amyloid polypeptide." Thesis, 2018. http://ndltd.ncl.edu.tw/handle/t4kty9.

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32

"Immunoregulatory role of human islet amyloid polypeptide through FoxP3+CD4+CD25+ T regulatory cells." Thesis, 2010. http://library.cuhk.edu.hk/record=b6075044.

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Background. Islet amyloid polypeptide (IAPP, also known as amylin) is a 37-amino acid peptide principally co-secreted with insulin from the beta-cells of the pancreatic islets. Some of the physiological actions of human amylin (hIAPP) include glucose regulation, suppression of appetite and stimulation of renal sodium and water reabsorption. Amylin deficiency and diminished post-prandial amylin response have been reported in advanced stages of type 1 and type 2 diabetes. In autopsy specimens of type 2 diabetes, amyloid is found in 40--90% of cases. During the characterization of islet morpholog

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33

Farrim, Maria Inês de Jesus Duarte. "Triggering of intracellular aggregation and cytotoxicity by immature forms of human Islet Amyloid Polypeptide." Master's thesis, 2020. http://hdl.handle.net/10362/114041.

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Diabetes is a chronic metabolic disease with increasing numbers worldwide. Pancreatic deposits of human Islet Amyloid Polypeptide (hIAPP) represent the major histopathological hallmark of type 2 diabetes. IAPP is a hormone produced by β-cells, which is released upon glucose stimulation concomitantly with insulin, acting on gastric emptying and glycemic control. It is synthesized as preproIAPP (ppIAPP) hormone that is first processed to proIAPP (pIAPP) and finally to its mature form (matIAPP). Impairment in IAPP processing seems to be associated with the accumulation of immature IAP

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34

"In vitro and in vivo effects of exendin-4 on human islet amyloid polypeptide induced beta-cell dysfunction." 2013. http://library.cuhk.edu.hk/record=b5884428.

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Zhou, Yu.<br>Thesis (M.Phil.)--Chinese University of Hong Kong, 2013.<br>Includes bibliographical references (leaves 89-107).<br>Electronic reproduction. Hong Kong : Chinese University of Hong Kong, [2012] System requirements: Adobe Acrobat Reader. Available via World Wide Web.<br>Abstracts also in Chinese.

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35

Kazantzis, Athanasios [Verfasser]. "Solid-phase syntheses and studies of conformationally constrained analogues of the calcitonin gene peptide superfamily polypeptides calcitonin (Ct) and islet amyloid polypeptide (IAPP) = Festphasensynthesen und Untersuchungen von konformationell-eingeschränkten Analoga der Calcitonin-Gen-Peptid-Superfamilien-Polypeptide Calcitonin (Ct) und Islet-Amyloid-Polypeptid (IAPP) / vorgelegt von Athanasios Kazantzis." 2004. http://d-nb.info/970370571/34.

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Yan, Li-Mei [Verfasser]. "Identification and characterization of IAPP derived inhibitors of cytotoxic self-assembly and amyloidogenesis of islet amyloid polypeptide (IAPP) and ß-amyloid [beta amyloid] peptide (Aß) [A beta] / vorgelegt von Li-Mei Yan." 2010. http://d-nb.info/1009587390/34.

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"Phycocyanin protects INS-1E pancreatic beta cells against human islet amyloid polypeptide-induced apoptosis through attenuating oxidative stress and mitochondrial dysfunction." Thesis, 2010. http://library.cuhk.edu.hk/record=b6075047.

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Additionally, cyclosporin A, an inhibitor of the mitochondrial permeability transition (MPT) pore, failed to prevent hIAPP-induced DeltaPsim collapse, cytochrome c and AIF release and caspase-3 activation, indicating that the MPT pore was not involved in hIAPP-induced apoptosis. On the other hand, potential crosstalk between the extrinsic and intrinsic apoptotic pathways was demonstrated by cleavage of Bid by caspase-8 in the apoptotic process triggered by hIAPP.<br>It is widely accepted that human islet amyloid polypeptide (hIAPP) aggregation plays an important role in the loss of insulin-pro

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Misra, Anurag. "Crystal Structures of Sortase A from Streptococcus Penumoniae : Insights into Domain-Swapped Dimerization. Crystal Structures of Designed Peptides : Inhibitors of Human Islet Amyloid Polypeptide (hIAPP) Fibrillization Implicated in Type 2 Diabetes And Those Forming Self-Assembled Nanotubes." Thesis, 2014. http://etd.iisc.ernet.in/handle/2005/2692.

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Sortases are cell-membrane associated cysteine transpeptidases that are essential for the assembly and covalent anchoring of certain surface proteins to the cell wall in Gram-positive bacteria. Thus, they play critical roles in virulence, infection and colonization by pathogens. Sortases have been classified as type A, B, C, D, E and F based on their phylogeny and the target-protein motifs that they recognize. Sortase A (SrtA) enzymes participate in cell wall anchoring of proteins involved in bacterial adhesion, immune evasion, internalization, and phage recognition and in some cases pili form

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Fortin, Jessica. "Caractérisation du rôle de l’amyline (IAPP) dans le diabète de type 2 : études de dérivés peptidiques et de composés inhibiteurs de la formation d’amyloïde." Thèse, 2015. http://hdl.handle.net/1866/13373.

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L’amyloïdose, une maladie progressive et incurable, implique une vaste panoplie de pathologies et de pathogénèses, qui est expliquée par la grande variabilité biologique et structurale des protéines responsables de la formation des dépôts d’amyloïde. L’amyline (polypeptide amyloïde des îlots pancréatiques, IAPP) est une protéine très susceptible de subir des changements de conformation impliquant les feuillets bêta et conférant aussi des propriétés physicochimiques distinctes. Cette protéine prend alors une forme fibrillaire et se dépose dans les îlots de Langerhans chez les humains atteints d

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