Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology

Type 2 diabetes as an inflammatory disease

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RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor

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Activation of the NLRP3 inflammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1β in type 2 diabetes

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Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients.

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A possible role for π‐stacking in the self‐assembly of amyloid fibrils

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Islet Amyloid Polypeptide, Islet Amyloid, and Diabetes Mellitus

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Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells.

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CD36 coordinates NLRP3 inflammasome activation by facilitating intracellular nucleation of soluble ligands into particulate ligands in sterile inflammation

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Diabetes Mellitus and the β Cell: The Last Ten Years

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Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation.

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Minireview: Secondary β-Cell Failure in Type 2 Diabetes—A Convergence of Glucotoxicity and Lipotoxicity

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The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles.

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Islet Amyloid: A Critical Entity in the Pathogenesis of Type 2 Diabetes

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Saturated Fatty Acids Synergize with Elevated Glucose to Cause Pancreatic β-Cell Death

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Peptide Conformation and Supramolecular Organization in Amylin Fibrils: Constraints from Solid-State NMR

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Multiple Amylin Receptors Arise from Receptor Activity-Modifying Protein Interaction with the Calcitonin Receptor Gene Product

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Recent advances in understanding leptin signaling and leptin resistance

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Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane

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Evidence of Cosecretion of Islet Amyloid Polypeptide and Insulin by β-Cells

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Pore Formation by the Cytotoxic Islet Amyloid Peptide Amylin

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Leptin responsiveness restored by amylin agonism in diet-induced obesity: Evidence from nonclinical and clinical studies

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Analysis of the Minimal Amyloid-forming Fragment of the Islet Amyloid Polypeptide

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Increased β-Cell Apoptosis Prevents Adaptive Increase in β-Cell Mass in Mouse Model of Type 2 Diabetes

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Co-localization of islet amyloid polypeptide and insulin in the B cell secretory granules of the human pancreatic islets

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Membrane Disruption and Early Events in the Aggregation of the Diabetes Related Peptide IAPP from a Molecular Perspective

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The effect of macromolecular crowding on protein aggregation and amyloid fibril formation

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Macromolecular Crowding and Protein Stability

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Amylin found in amyloid deposits in human type 2 diabetes mellitus may be a hormone that regulates glycogen metabolism in skeletal muscle.

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Atomic structure of the cross‐β spine of islet amyloid polypeptide (amylin)

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Conserved and Cooperative Assembly of Membrane-Bound α-Helical States of Islet Amyloid Polypeptide

Knight, J. D., Hebda, J. A., & Miranker, A. D. (2006) · Biochemistry · doi:10.1021/bi060579z · Cited by 310

Amylin replacement with pramlintide as an adjunct to insulin therapy improves long‐term glycaemic and weight control in Type 1 diabetes mellitus: a 1‐year, randomized controlled trial

Ratner, R. E., Dickey, R., Fineman, M., Maggs, D. G., Shen, L., Strobel, S. A., Weyer, C., & Kolterman, O. G. (2004) · Diabetic Medicine · doi:10.1111/j.1464-5491.2004.01319.x · Cited by 307

THE RELATION OE DIABETES MELLITUS TO LESIONS OF THE PANCREAS. HYALINE DEGENERATION OF THE ISLANDS OE LANGERHANS

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Islet amyloid and type 2 diabetes: from molecular misfolding to islet pathophysiology

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Protofibrillar Islet Amyloid Polypeptide Permeabilizes Synthetic Vesicles by a Pore-like Mechanism that May Be Relevant to Type II Diabetes

Anguiano, M., Nowak, R. J., & Lansbury, P. T. (2002) · Biochemistry · doi:10.1021/bi020314u · Cited by 293

Polymorphic Fibrillar Assembly of Human Amylin

Goldsbury, C. S., Cooper, G. J. S., Goldie, K. N., Müller, S. A., Saafi, E. L., Gruijters, W. T. M., Misur, M. P., Engel, A. H., Aebi, U., & Kistler, J. (1997) · Journal of Structural Biology · doi:10.1006/jsbi.1997.3858 · Cited by 293

Protein Stabilization by Macromolecular Crowding through Enthalpy Rather Than Entropy

Senske, M., Törk, L., Born, B., Havenith, M., Herrmann, C., & Ebbinghaus, S. (2014) · Journal of the American Chemical Society · doi:10.1021/ja503205y · Cited by 285

Molecular Crowding Accelerates Fibrillization of α-Synuclein: Could an Increase in the Cytoplasmic Protein Concentration Induce Parkinson's Disease?

Shtilerman, M. D., Ding, T. T., & Lansbury, P. T. (2002) · Biochemistry · doi:10.1021/bi0120906 · Cited by 280

Structure and membrane orientation of IAPP in its natively amidated form at physiological pH in a membrane environment

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An Amylin Receptor Is Revealed Following Co-Transfection of a Calcitonin Receptor with Receptor Activity Modifying Proteins-1 or -3

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Lipid Membranes Modulate the Structure of Islet Amyloid Polypeptide

Jayasinghe, S. A., & Langen, R. (2005) · Biochemistry · doi:10.1021/bi050840w · Cited by 262

An islet amyloid peptide is derived from an 89-amino acid precursor by proteolytic processing.

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Islet amyloid polypeptide‐induced membrane leakage involves uptake of lipids by forming amyloid fibers

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Mechanism of IAPP amyloid fibril formation involves an intermediate with a transient β-sheet

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Design of a mimic of nonamyloidogenic and bioactive human islet amyloid polypeptide (IAPP) as nanomolar affinity inhibitor of IAPP cytotoxic fibrillogenesis

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β-Cell Failure in Type 2 Diabetes: Postulated Mechanisms and Prospects for Prevention and Treatment

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Physical and structural basis for polymorphism in amyloid fibrils

Tycko, R. (2014) · Protein Science · doi:10.1002/pro.2544 · Cited by 241

Evidence for Proteotoxicity in β Cells in Type 2 Diabetes

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Amyloid Fiber Formation and Membrane Disruption are Separate Processes Localized in Two Distinct Regions of IAPP, the Type-2-Diabetes-Related Peptide

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The Interplay of Catalysis and Toxicity by Amyloid Intermediates on Lipid Bilayers: Insights from Type II Diabetes

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The aggregation potential of human amylin determines its cytotoxicity towards islet β‐cells

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Oxidative stress is induced by islet amyloid formation and time-dependently mediates amyloid-induced beta cell apoptosis

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Direct detection of transient α‐helical states in islet amyloid polypeptide

Williamson, J. A., & Miranker, A. D. (2006) · Protein Science · doi:10.1110/ps.062486907 · Cited by 215

Molecular membrane biology

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Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process

Wiltzius, J. J. W., Sievers, S. A., Sawaya, M. R., & Eisenberg, D. S. (2009) · Protein Science · doi:10.1002/pro.145 · Cited by 208

Mechanisms of islet amyloidosis toxicity in type 2 diabetes

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Identification of Hot Regions of the Aβ–IAPP Interaction Interface as High‐Affinity Binding Sites in both Cross‐ and Self‐Association

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IL-1 Blockade Attenuates Islet Amyloid Polypeptide-Induced Proinflammatory Cytokine Release and Pancreatic Islet Graft Dysfunction

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Impact of reconstituted cytosol on protein stability

Sarkar, M., Smith, A. E., & Pielak, G. J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1312678110 · Cited by 191

Toxic oligomers and islet beta cell death: guilty by association or convicted by circumstantial evidence?

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Effects of beta cell granule components on human islet amyloid polypeptide fibril formation

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Widespread Amyloid Deposition in Transplanted Human Pancreatic Islets

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Helix Stabilization Precedes Aqueous and Bilayer-Catalyzed Fiber Formation in Islet Amyloid Polypeptide

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Identification and Characterization of a Novel Molecular-recognition and Self-assembly Domain within the Islet Amyloid Polypeptide

Mazor, Y., Gilead, S., Benhar, I., & Gazit, E. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00887-2 · Cited by 186

The role of amylin in the control of energy homeostasis

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Sequence divergence in a specific region of islet amyloid polypeptide (IAPP) explains differences in islet amyloid formation between species

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Islet amyloid: From fundamental biophysics to mechanisms of cytotoxicity

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A Single-Point Mutation Converts the Highly Amyloidogenic Human Islet Amyloid Polypeptide into a Potent Fibrillization Inhibitor

Abedini, A., Meng, F., & Raleigh, D. P. (2007) · Journal of the American Chemical Society · doi:10.1021/ja072157y · Cited by 178

The Human Islet Amyloid Polypeptide Forms Transient Membrane-Active Prefibrillar Assemblies

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Structures of Rat and Human Islet Amyloid Polypeptide IAPP1−19 in Micelles by NMR Spectroscopy

Nanga, R. P. R., Brender, J., Xu, J., Veglia, G., & Ramamoorthy, A. (2008) · Biochemistry · doi:10.1021/bi8014357 · Cited by 172

The internal pH and membrane potential of the insulin-secretory granule

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Islet amyloid deposition limits the viability of human islet grafts but not porcine islet grafts

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Antiobesity Effects of the β-Cell Hormone Amylin in Diet-Induced Obese Rats: Effects on Food Intake, Body Weight, Composition, Energy Expenditure, and Gene Expression

Roth, J. D., Hughes, H., Kendall, E. S., Baron, A., & Anderson, C. M. (2006) · Endocrinology · doi:10.1210/en.2006-0393 · Cited by 171

Ionic Strength Effects on Amyloid Formation by Amylin Are a Complicated Interplay among Debye Screening, Ion Selectivity, and Hofmeister Effects

Marek, P., Patsalo, V., Green, D. F., & Raleigh, D. P. (2012) · Biochemistry · doi:10.1021/bi300574r · Cited by 168

Missense Mutation of Amylin Gene (S20G) in Japanese NIDDM Patients

Sakagashira, S., Sanke, T., Hanabusa, T., Shimomura, H., Ohagi, S., Kumagaye, K. Y., Nakajima, K., & Nanjo, K. (1996) · Diabetes · doi:10.2337/diab.45.9.1279 · Cited by 162

The Role of His-18 in Amyloid Formation by Human Islet Amyloid Polypeptide

Abedini, A., & Raleigh, D. P. (2005) · Biochemistry · doi:10.1021/bi051432v · Cited by 158

Impairment of the Ubiquitin-Proteasome Pathway Is a Downstream Endoplasmic Reticulum Stress Response Induced by Extracellular Human Islet Amyloid Polypeptide and Contributes to Pancreatic β-Cell Apoptosis

Casas, S., Gomis, R., Gribble, F. M., Altirriba, J., Knuutila, S., & Novials, A. (2007) · Diabetes · doi:10.2337/db07-0178 · Cited by 148

A Single Mutation in the Nonamyloidogenic Region of Islet Amyloid Polypeptide Greatly Reduces Toxicity

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Three-Dimensional Structure and Orientation of Rat Islet Amyloid Polypeptide Protein in a Membrane Environment by Solution NMR Spectroscopy

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Islet amyloid polypeptide toxicity and membrane interactions

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Analysis of amylin cleavage products provides new insights into the amyloidogenic region of human amylin

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β-Cell Deficit Due to Increased Apoptosis in the Human Islet Amyloid Polypeptide Transgenic (HIP) Rat Recapitulates the Metabolic Defects Present in Type 2 Diabetes

Matveyenko, A. V., & Butler, P. C. (2006) · Diabetes · doi:10.2337/db05-1672 · Cited by 144

S20G Mutant Amylin Exhibits Increased in Vitro Amyloidogenicity and Increased Intracellular Cytotoxicity Compared to Wild-Type Amylin

Sakagashira, S., Hiddinga, H. J., Tateishi, K., Sanke, T., Hanabusa, T., Nanjo, K., & Eberhardt, N. L. (2000) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64848-1 · Cited by 142

Aromatic Interactions Are Not Required for Amyloid Fibril Formation by Islet Amyloid Polypeptide but Do Influence the Rate of Fibril Formation and Fibril Morphology

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Hyperamylinemia Contributes to Cardiac Dysfunction in Obesity and Diabetes

Despa, S. I., Margulies, K. B., Chen, L., Knowlton, A. A., Havel, P. J., Taegtmeyer, H., Bers, D. M., & Despa, F. (2012) · Circulation Research · doi:10.1161/circresaha.111.258285 · Cited by 137

Human-IAPP disrupts the autophagy/lysosomal pathway in pancreatic β-cells: protective role of p62-positive cytoplasmic inclusions

Rivera, J. F., Gurlo, T., Daval, M., Huang, C. J., Matveyenko, A. V., Butler, P. C., & Costes, S. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2010.111 · Cited by 136

Fibril Structure of Human Islet Amyloid Polypeptide*♦

Bedrood, S., Li, Y.-Y., Isas, J., Hegde, B. G., Baxa, U., Haworth, I., & Langen, R. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.327817 · Cited by 136

Role of Aromatic Interactions in Amyloid Formation by Islet Amyloid Polypeptide

Tu, L., & Raleigh, D. P. (2012) · Biochemistry · doi:10.1021/bi3014278 · Cited by 135

Islet amyloid polypeptide demonstrates a persistent capacity to disrupt membrane integrity

Last, N. B., Rhoades, E. R., & Miranker, A. D. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1102356108 · Cited by 132

Full-length Rat Amylin Forms Fibrils Following Substitution of Single Residues from Human Amylin

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Role of Aromatic Interactions in Amyloid Formation by Peptides Derived from Human Amylin

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