Human Islet Amyloid Polypeptide Transgenic Mice:  In Vivo and Ex Vivo Models for the Role of hIAPP in  Type 2 Diabetes Mellitus

Höppener, Jo W.M.; Jacobs, H. M.; Wierup, Nils; Sotthewes, G.; Sprong, M.; Vos, Paul de; Berger, Ruud; Sundler, F.; Åhrén, Bo

doi:10.1155/2008/697035

Cited by 32 publications

(27 citation statements)

References 47 publications

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“…The latter two events are important features that prevent an individual from feeling hungry thereby averting the condition of having even more stored glucose being released into the blood. Since amylin is coreleased with insulin, consuming an excess amount of carbohydrates and fat may lead to an elevated amount of amylin being secreted that could eventually initiate amylin aggregation, since it was found that a high carbohydrate or high fat diet promoted amyloid formation in transgenic mice [32, 33]. …”

Section: Introductionmentioning

confidence: 99%

Amylin Uncovered: A Review on the Polypeptide Responsible for Type II Diabetes

Pillay

Gasqui

2013

BioMed Research International

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Amylin is primarily responsible for classifying type II diabetes as an amyloid (protein misfolding) disease as it has great potential to aggregate into toxic nanoparticles, thereby resulting in loss of pancreatic β-cells. Although type II diabetes is on the increase each year, possibly due to bad eating habits of modern society, research on the culprit for this disease is still in its early days. In addition, unlike the culprit for Alzheimer's disease, amyloid β-peptide, amylin has failed to receive attention worthy of being featured in an abundance of review articles. Thus, the aim of this paper is to shine the spotlight on amylin in an attempt to put it onto the top of researchers' to-do list since the secondary complications of type II diabetes have far-reaching and severe consequences on public health both in developing and fully developed countries alike. This paper will cover characteristics of the amylin aggregates, mechanisms of toxicity, and a particular focus on inhibitors of toxicity and techniques used to assess these inhibitors.

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Section: Introductionmentioning

confidence: 99%

Amylin Uncovered: A Review on the Polypeptide Responsible for Type II Diabetes

Pillay

Gasqui

2013

BioMed Research International

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“…Amyloidoses, including Alzheimer's disease (1), Parkinson's disease (2), type II diabetes (3), and spongiform encephalopathy (4), are associated with the formation of amyloid fibrils. The fibrillation process of amyloidogenic proteins is initiated by the conversion of innocuous proteins into oligomeric intermediates to form highly ordered, unbranched b-sheet structures (5).…”

Section: Introductionmentioning

confidence: 99%

Amyloid Fibrillation of Insulin under Water-Limited Conditions

Choi

Lee

Jin

et al. 2014

Biophysical Journal

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Amyloid fibrillation in water-organic mixtures has been widely studied to understand the effect of protein-solvent interactions on the fibrillation process. In this study, we monitored insulin fibrillation in formamide and its methyl derivatives (formamide, N-methyl formamide, N,N-dimethyl formamide) in the presence and absence of water. These model solvent systems mimic the cellular environment by providing denaturing conditions and a hydrophobic environment with limited water content. Thioflavin T (ThT) assay revealed that binary mixtures of water with formamide and its methyl derivatives enhanced fibrillation rates and ?-sheet abundance, whereas organic solvents suppressed insulin fibrillation. We utilized solution small-angle x-ray scattering (SAXS) and differential scanning calorimetry (DSC) to investigate the correlation between protein-solvent interactions and insulin fibrillation. SAXS experiments combined with simulated annealing of the protein indicated that the degree of denaturation of the hydrophobic core region at residues B11-B17 determines the fibrillation rate. In addition, DSC experiments suggested a crucial role of hydrophobic interactions in the fibrillation process. These results imply that an environment with limited water, which imitates a lipid membrane system, accelerates protein denaturation and the formation of intermolecular hydrophobic interactions during amyloid fibrillation.

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“…Chronic infusion of amylin into the brain reduces body weight gain and adiposity, while chronic infusion of an antagonist of amylin receptors into the brain increases body adiposity (Lutz et al, 2010;Wielinga et al, 2010). In vitro, amylin was found to inhibit both basal and insulin-stimulated glycogenesis in rat skeleton muscle (Leighton et al, 1988) and to impair glucose disposal in liver cells (Hoppener et al, 2008). Infusion of amylin in dogs also induced peripheral insulin resistance (Xinwei et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

Correlations between endogen amylin hormone and some hormonal, biochemical and bone parameters in pullets

Guzel

Güneş

2014

Rev. Bras. Cienc. Avic.

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The objective of this study was to assess the correlations of amylin (a pancreatic polypeptide hormone) with some hormonal, biochemical and bone parameters in pullets. Forty 18-week-old pullets were used. Plasma amylin, CT (calcitonin), 1,25 (OH)2 vitamin D (1,25 dihydroxycholecalciferol ), serum osteocalcin, glucose, ALP (alkaline phosphatase), cholesterol, and triglycerides, as well as weight, length and total volume of tibiotarsi were measured. Plasma amylin concentration was negatively correlated with serum cholesterol (p<0.05) and triglycerides (p<0.05) concentrations. Plasma amylin concentration was significantly and positively correlated with plasma calcitonin concentrations (p<0.001). Serum ALP and plasma amylin concentrations were positively correlated (p<0.01). There were no correlations between amylin hormone and other parameters. Based on these results, it is possible to conclude that endogen amylin may effect cholesterol, triglycerides, calcitonin, and ALP levels in pullets without changing some other hormonal, biochemical and bone parameters related to calcium and lipid metabolism.

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Human Islet Amyloid Polypeptide Transgenic Mice: In Vivo and Ex Vivo Models for the Role of hIAPP in Type 2 Diabetes Mellitus

Cited by 32 publications

References 47 publications

Amylin Uncovered: A Review on the Polypeptide Responsible for Type II Diabetes

Amylin Uncovered: A Review on the Polypeptide Responsible for Type II Diabetes

Amyloid Fibrillation of Insulin under Water-Limited Conditions

Correlations between endogen amylin hormone and some hormonal, biochemical and bone parameters in pullets

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