Causative factors for formation of toxic islet amyloid polypeptide oligomer in type 2 diabetes mellitus

References

• KlöppelGLöhrMHabichKOberholzerMHeitzPIslet pathology and the pathogenesis of type 1 and type 2 diabetes mellitus revisitedPathol Immunopathol Res198542110125
   Google Scholar
• ClarkANilssonMIslet amyloid: a complication of islet dysfunction or an aetiological factor in Type 2 diabetes?Diabetologia200447215716914722650
   PubMed Web of Science ®Google Scholar
• NguyenPTAndrakaNDe CarufelCABourgaultSMechanistic contributions of biological cofactors in islet amyloid polypeptide amyloidogenesisJ Diabetes Res2015
   Web of Science ®Google Scholar
• YoungAGedulinBVineWPercyARinkTGastric emptying is accelerated in diabetic BB rats and is slowed by subcutaneous injections of amylinDiabetologia19953866426487672483
   PubMed Web of Science ®Google Scholar
• WookeyPJLutzTAAndrikopoulosSAmylin in the periphery II: an updated mini-reviewSci World J2006616421655
   Web of Science ®Google Scholar
• GunasekaranUGannonMType 2 diabetes and the aging pancreatic beta cellAging (Albany NY)20113656521765202
   PubMedGoogle Scholar
• StroudJCLiuCTengPKEisenbergDToxic fibrillar oligomers of amyloid-β have cross-β structureProc Natl Acad Sci2012109207717772222547798
   PubMed Web of Science ®Google Scholar
• WiltziusJJSieversSASawayaMRAtomic structure of the cross-β spine of islet amyloid polypeptide (amylin)Protein Sci20081791467147418556473
   PubMed Web of Science ®Google Scholar
• MeierJJKayedRLinC-YInhibition of human IAPP fibril formation does not prevent β-cell death: evidence for distinct actions of oligomers and fibrils of human IAPPAm J Physiol Endocrinol Metab20062916E1317E132416849627
   PubMed Web of Science ®Google Scholar
• PounyYRapaportDMorANicolasPShaiYInteraction of antimicrobial dermaseptin and its fluorescently labeled analogs with phospholipid membranesBiochemistry1992314912416124231463728
   PubMed Web of Science ®Google Scholar
• OjciusDMYoungJDECytolytic pore-forming proteins and peptides: is there a common structural motif?Trends Biochem Sci1991162252291654003
   PubMed Web of Science ®Google Scholar
• JayasingheSALangenRLipid membranes modulate the structure of islet amyloid polypeptideBiochemistry20054436121131211916142909
   PubMed Web of Science ®Google Scholar
• DomanovYAKinnunenPKIslet amyloid polypeptide forms rigid lipid–protein amyloid fibrils on supported phospholipid bilayersJ Mol Biol20083761425418155730
   PubMed Web of Science ®Google Scholar
• AhmadEAhmadASinghSArshadMKhanAHKhanRHA mechanistic approach for islet amyloid polypeptide aggregation to develop anti-amyloidogenic agents for type-2 diabetesBiochimie201193579380521215287
   PubMed Web of Science ®Google Scholar
• AbediniARaleighDPThe role of His-18 in amyloid formation by human islet amyloid polypeptideBiochemistry20054449162841629116331989
   PubMed Web of Science ®Google Scholar
• JhaSSnellJMShefticSRpH dependence of amylin fibrillizationBiochemistry201453230031024377660
   PubMed Web of Science ®Google Scholar
• SakagashiraSSankeTHanabusaTMissense mutation of amylin gene (S20G) in Japanese NIDDM patientsDiabetes1996459127912818772735
   PubMed Web of Science ®Google Scholar
• SakagashiraSHiddingaHJTateishiKS20G mutant amylin exhibits increased in vitro amyloidogenicity and increased intracellular cytotoxicity compared to wild-type amylinAm J Pathol200015762101210911106582
   PubMed Web of Science ®Google Scholar
• MarekPAbediniASongBAromatic interactions are not required for amyloid fibril formation by islet amyloid polypeptide but do influence the rate of fibril formation and fibril morphologyBiochemistry200746113255326117311418
   PubMed Web of Science ®Google Scholar
• TuL-HRaleighDPRole of aromatic interactions in amyloid formation by islet amyloid polypeptideBiochemistry201352233334223256729
   PubMed Web of Science ®Google Scholar
• BernhardtNABerhanuWMHansmannUHMutations and seeding of amylin fibril-like oligomersJ Phys Chem B201311750160761608524294935
   PubMed Web of Science ®Google Scholar
• AbediniAMengFRaleighDPA single-point mutation converts the highly amyloidogenic human islet amyloid polypeptide into a potent fibrillization inhibitorJ Am Chem Soc200712937113001130117722920
   PubMed Web of Science ®Google Scholar
• MengFRaleighDPAbediniACombination of kinetically selected inhibitors in trans leads to highly effective inhibition of amyloid formationJ Am Chem Soc201013241143401434220873820
   PubMed Web of Science ®Google Scholar
• MillerCZerzeGlHMittalJMolecular simulations indicate marked differences in the structure of amylin mutants, correlated with known aggregation propensityJ Phys Chem B201311750160661607524245879
   PubMed Web of Science ®Google Scholar
• HaatajaLGurloTHuangCJButlerPCIslet amyloid in type 2 diabetes, and the toxic oligomer hypothesisEndocr Rev200829330331618314421
   PubMed Web of Science ®Google Scholar
• WestermarkPEngströmUJohnsonKHWestermarkGTBetsholtzCIslet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formationProc Natl Acad Sci19908713503650402195544
   PubMed Web of Science ®Google Scholar
• ButlerAEJangJGurloTCartyMDSoellerWCButlerPCDiabetes due to a progressive defect in β-cell mass in rats transgenic for human islet amyloid polypeptide (HIP rat) a new model for type 2 diabetesDiabetes20045361509151615161755
   PubMed Web of Science ®Google Scholar
• MatveyenkoAVButlerPCβ-Cell deficit due to increased apoptosis in the human islet amyloid polypeptide transgenic (HIP) rat recapitulates the metabolic defects present in type 2 diabetesDiabetes20065572106211416804082
   PubMed Web of Science ®Google Scholar
• HuangC-JLinC-YHaatajaLHigh expression rates of human islet amyloid polypeptide induce endoplasmic reticulum stress–mediated β-cell apoptosis, a characteristic of humans with type 2 but not type 1 diabetesDiabetes20075682016202717475933
   PubMed Web of Science ®Google Scholar
• SankeTBellGSampleCRubensteinASteinerDAn islet amyloid peptide is derived from an 89-amino acid precursor by proteolytic processingJ Biol Chem19882633317243172463053705
   PubMed Web of Science ®Google Scholar
• MarzbanLSoukhatchevaGVerchereCBRole of carboxypeptidase E in processing of pro-islet amyloid polypeptide in β-cellsEndocrinology200514641808181715618358
   PubMed Web of Science ®Google Scholar
• RobertsALeightonBToddJMolecular and functional characterization of amylin, a peptide associated with type 2 diabetes mellitusProc Natl Acad Sci19898624966296662690069
   PubMed Web of Science ®Google Scholar
• MarzbanLTrigo-GonzalezGZhuXRole of β-cell prohormone convertase (PC) 1/3 in processing of pro-islet amyloid polypeptideDiabetes200453114114814693708
   PubMed Web of Science ®Google Scholar
• MarzbanLRhodesCJSteinerDFHaatajaLHalbanPAVerchereCBImpaired NH2-terminal processing of human proislet amyloid polypeptide by the prohormone convertase PC2 leads to amyloid formation and cell deathDiabetes20065582192220116873681
   PubMed Web of Science ®Google Scholar
• WangJXuJFinnertyJFurutaMSteinerDFVerchereCBThe prohormone convertase enzyme 2 (PC2) is essential for processing pro-islet amyloid polypeptide at the NH2-terminal cleavage siteDiabetes200150353453911246872
   PubMed Web of Science ®Google Scholar
• TakataTOxfordJTDemelerBLampiKJDeamidation destabilizes and triggers aggregation of a lens protein, βA3-crystallinProtein Sci20081791565157518567786
   PubMed Web of Science ®Google Scholar
• NilssonMRDobsonCMChemical modification of insulin in amyloid fibrilsProtein Sci200312112637264114573875
   PubMed Web of Science ®Google Scholar
• BischoffRKolbeHVDeamidation of asparagine and glutamine residues in proteins and peptides: structural determinants and analytical methodologyJ Chromatogr B Biomed Sci Appl19946622261278
   Web of Science ®Google Scholar
• DunkelbergerEBBuchananLEMarekPCaoPRaleighDPZanniMTDeamidation accelerates amyloid formation and alters amylin fiber structureJ Am Chem Soc201213430126581266722734583
   PubMed Web of Science ®Google Scholar
• NilssonMRDriscollMRaleighDPLow levels of asparagine deamidation can have a dramatic effect on aggregation of amyloidogenic peptides: implications for the study of amyloid formationProtein Sci200211234234911790844
   PubMed Web of Science ®Google Scholar
• LaghaeiRMousseauNWeiGEffect of the disulfide bond on the monomeric structure of human amylin studied by combined Hamiltonian and temperature replica exchange molecular dynamics simulationsJ Phys Chem B2010114207071707720429571
   PubMed Web of Science ®Google Scholar
• VaianaSMBestRBYauW-MEatonWAHofrichterJEvidence for a partially structured state of the amylin monomerBiophys J200997112948295719948124
   PubMed Web of Science ®Google Scholar
• CopeSMShindeSBestRBGiovannaGVaianaSMCyclic N terminal fragment of amylin forms non amyloid fibers: implications for intra-and inter-molecular interactions in amylinBiophys J20131042389a390a
   Web of Science ®Google Scholar
• GoldsburyCGoldieKPellaudJAmyloid fibril formation from full-length and fragments of amylinJ Struct Biol2000130235236210940238
   PubMed Web of Science ®Google Scholar
• YonemotoITKroonGJDysonHJBalchWEKellyJWAmylin proprotein processing generates progressively more amyloidogenic peptides that initially sample the helical stateBiochemistry200847379900991018710262
   PubMed Web of Science ®Google Scholar
• KooBWMirankerADContribution of the intrinsic disulfide to the assembly mechanism of islet amyloidProtein Sci200514123123915576552
   PubMed Web of Science ®Google Scholar
• AbediniARaleighDPA role for helical intermediates in amyloid formation by natively unfolded polypeptides?Phys Biol20096101500519208933
   PubMed Web of Science ®Google Scholar
• MossutoMFBolognesiBGuixerBDisulfide bonds reduce the toxicity of the amyloid fibrils formed by an extracellular proteinAngew Chem Int Ed2011503170487051
   Web of Science ®Google Scholar
• MonsellierERamazzottiMTaddeiNChitiFAggregation propensity of the human proteomePLoS Comput Biol2008410e100019918927604
   PubMed Web of Science ®Google Scholar
• Uriu-AdamsJYKeenCLCopper, oxidative stress, and human healthMol Aspects Med2005264–526829816112185
   PubMedGoogle Scholar
• BrenderJRHartmanKNangaRPRRole of zinc in human islet amyloid polypeptide aggregationJ Am Chem Soc2010132268973898320536124
   PubMed Web of Science ®Google Scholar
• WardBWalkerKExleyCCopper (II) inhibits the formation of amylin amyloid in vitroJ Inorg Biochem2008102237137518022240
   PubMed Web of Science ®Google Scholar
• SinopoliAMagrìAMilardiDThe role of copper (II) in the aggregation of human amylinMetallomics20146101841185225080969
   PubMed Web of Science ®Google Scholar
• DrewSCMastersCLBarnhamKJAlanine-2 carbonyl is an oxygen ligand in Cu2+ coordination of Alzheimer’s disease amyloid-β peptide – relevance to N-terminally truncated formsJ Am Chem Soc2009131258760876119496610
   PubMed Web of Science ®Google Scholar
• YuY-PLeiPHuJWuW-HZhaoY-FLiY-MCopper-induced cytotoxicity: reactive oxygen species or islet amyloid polypeptide oligomer formationChem Commun2010463769096911
   Web of Science ®Google Scholar
• LeeECHaESinghSCopper (II)–human amylin complex protects pancreatic cells from amylin toxicityPhys Chem Chem Phys20131530125581257123793354
   PubMed Web of Science ®Google Scholar
• MirzabekovTALinM-CKaganBLPore formation by the cytotoxic islet amyloid peptide amylinJ Biol Chem19962714198819928567648
   PubMed Web of Science ®Google Scholar
• JansonJAshleyRHHarrisonDMcIntyreSButlerPCThe mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particlesDiabetes199948349149810078548
   PubMed Web of Science ®Google Scholar
• MaLLiXWangYZhengWChenTCu (II) inhibits hIAPP fibrillation and promotes hIAPP-induced beta cell apoptosis through induction of ROS-mediated mitochondrial dysfunctionJ Inorg Biochem201414014315225108186
   PubMed Web of Science ®Google Scholar
• ZorovDBJuhaszovaMSollottSJMitochondrial ROS-induced ROS release: an update and reviewBiochim Biophys Acta20061757550951716829228
   PubMed Web of Science ®Google Scholar
• MasadAHayesLTabnerBJCopper-mediated formation of hydrogen peroxide from the amylin peptide: a novel mechanism for degeneration of islet cells in type-2 diabetes mellitus?FEBS Lett2007581183489349317617411
   PubMed Web of Science ®Google Scholar
• TanakaAKanetoHMiyatsukaTRole of copper ion in the pathogenesis of type 2 diabetesEndocr J200956569970619461160
   PubMed Web of Science ®Google Scholar
• WatsonDJLanderADSelkoeDJHeparin-binding properties of the amyloidogenic peptides Aβ and amylin dependence on aggregation state and inhibition by congo redJ Biol Chem19972725031617316249395501
   PubMed Web of Science ®Google Scholar
• JhaSPatilSMGibsonJNelsonCEAlderNNAlexandrescuATMechanism of amylin fibrillization enhancement by heparinJ Biol Chem201128626228942290421555785
   PubMed Web of Science ®Google Scholar
• AlexandrescuATJhaSPatilSMGibsonJAlderNNNelsonCEEffects of heparin on amylin fibrillizationBiophys J20121023243a
   Web of Science ®Google Scholar