Islet amyloid polypeptide toxicity and membrane interactions

Protein Misfolding, Functional Amyloid, and Human Disease

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Calcium Dysregulation and Membrane Disruption as a Ubiquitous Neurotoxic Mechanism of Soluble Amyloid Oligomers*♦

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Islet Amyloid Polypeptide, Islet Amyloid, and Diabetes Mellitus

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Diabetes Mellitus and the β Cell: The Last Ten Years

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Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases

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Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus

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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, increased A-cells, reduced B-cells and exocrine fibrosis: quantitative changes in the pancreas in type 2 diabetes.

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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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Mechanism of fluorescence concentration quenching of carboxyfluorescein in liposomes: Energy transfer to nonfluorescent dimers

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

Lukinius, A., Wilander, E., Westermark, G. T., Engstr�m, U., & Westermark, P. (1989) · Diabetologia · doi:10.1007/bf00285291 · Cited by 371

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

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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

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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

Lipid Membranes Modulate the Structure of Islet Amyloid Polypeptide

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

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

Sparr, E., Engel, M. F. M., Sakharov, D. V., Sprong, M., Jacobs, J., KRUIJFF, B. D., Höppener, J. W. M., & Killian, J. A. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.09.075 · Cited by 257

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

Yan, L., Tatarek‐Nossol, M., Velkova, A., Kazantzis, A., & Kapurniotu, A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507471103 · Cited by 247

Recent Insights in Islet Amyloid Polypeptide‐Induced Membrane Disruption and Its Role in β‐Cell Death in Type 2 Diabetes Mellitus

Khemtémourian, L., Killian, J. A., Höppener, J. W. M., & Engel, M. F. M. (2008) · Journal of Diabetes Research · doi:10.1155/2008/421287 · Cited by 238

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

Brender, J., Lee, E. L., Cavitt, M. A., Gafni, A., Steel, D. G., & Ramamoorthy, A. (2008) · Journal of the American Chemical Society · doi:10.1021/ja710484d · Cited by 229

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

Hebda, J. A., & Miranker, A. D. (2009) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.050708.133622 · Cited by 223

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

Konarkowska, B., Aitken, J. F., Kistler, J., Zhang, S., & Cooper, G. J. S. (2006) · The FEBS Journal · doi:10.1111/j.1742-4658.2006.05367.x · Cited by 219

Preparation and Properties of Asymmetric Vesicles That Mimic Cell Membranes

Cheng, H.-T., Megha, M., & London, E. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m806077200 · Cited by 198

Widespread Amyloid Deposition in Transplanted Human Pancreatic Islets

Westermark, G. T., Westermark, P., Berne, C., & Korsgren, O. (2008) · New England Journal of Medicine · doi:10.1056/nejmc0802893 · Cited by 187

Membrane interaction of islet amyloid polypeptide

Jayasinghe, S. A., & Langen, R. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.01.022 · Cited by 181

Islet amyloid: From fundamental biophysics to mechanisms of cytotoxicity

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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

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

Potter, K. J., Abedini, A., Marek, P., Klimek-Abercrombie, A. M., Butterworth, S. A., Driscoll, M., Baker, R. L., Nilsson, M. R., Warnock, G. L., Oberholzer, J., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0909024107 · Cited by 171

Atomic Force Microscopy Reveals Defects Within Mica Supported Lipid Bilayers Induced by the Amyloidogenic Human Amylin Peptide

Green, J. D., Kreplak, L., Goldsbury, C. S., Li‐Blatter, X., Stolz, M., Cooper, G. J. S., Seelig, A., Kistler, J., & Aebi, U. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.07.052 · Cited by 161

Preparation and properties of asymmetric vesicles that mimic cell membranes. EFFECT UPON LIPID RAFT FORMATION AND TRANSMEMBRANE HELIX ORIENTATION.

Cheng, H.-T., Megha, M., & London, E. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.a111.806077 · Cited by 149

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

Marek, P., Abedini, A., Song, B., Kanungo, M., Johnson, M. E., Gupta, R., Zaman, W., Wong, S. S., & Raleigh, D. P. (2007) · Biochemistry · doi:10.1021/bi0621967 · Cited by 142

Control of energy homeostasis by amylin

Lutz, T. A. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0905-1 · Cited by 139

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

Membrane permeabilization by Islet Amyloid Polypeptide

Engel, M. F. M. (2009) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2009.03.008 · Cited by 129

Low levels of asparagine deamidation can have a dramatic effect on aggregation of amyloidogenic peptides: Implications for the study of amyloid formation

Nilsson, M. R., Driscoll, M., & Raleigh, D. P. (2002) · Protein Science · doi:10.1110/ps.48702 · Cited by 124

Biphasic Effects of Insulin on Islet Amyloid Polypeptide Membrane Disruption

Brender, J., Lee, E. L., Hartman, K. L., Wong, P. T., Ramamoorthy, A., Steel, D. G., & Gafni, A. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2010.09.070 · Cited by 93

Sensitivity of Amyloid Formation by Human Islet Amyloid Polypeptide to Mutations at Residue 20

Cao, P., Tu, L., Abedini, A., Levsh, O., Akter, R., Patsalo, V., Schmidt, A. M., & Raleigh, D. P. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.12.032 · Cited by 85

Amyloidogenic Propensities and Conformational Properties of ProIAPP and IAPP in the Presence of Lipid Bilayer Membranes

Jha, S., Sellin, D., Seidel, R. P., & Winter, R. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.04.077 · Cited by 79

Clustering and Internalization of Toxic Amylin Oligomers in Pancreatic Cells Require Plasma Membrane Cholesterol

Trikha, S., & Jeremic, A. M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.240762 · Cited by 75

Interaction of hIAPP with Model Raft Membranes and Pancreatic β‐Cells: Cytotoxicity of hIAPP Oligomers

Weise, K., Radovan, D., Gohlke, A., Opitz, N., & Winter, R. (2010) · ChemBioChem · doi:10.1002/cbic.201000039 · Cited by 74

Fluorescence microscopy studies on islet amyloid polypeptide fibrillation at heterogeneous and cellular membrane interfaces and its inhibition by resveratrol

Radovan, D., Opitz, N., & Winter, R. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.03.059 · Cited by 66

The Effect of Aβ on IAPP Aggregation in the Presence of an Isolated β-Cell Membrane

Seeliger, J., Weise, K., Opitz, N., & Winter, R. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.01.048 · Cited by 59

Combination of Kinetically Selected Inhibitors in Trans Leads to Highly Effective Inhibition of Amyloid Formation

Meng, F., Raleigh, D. P., & Abedini, A. (2010) · Journal of the American Chemical Society · doi:10.1021/ja1046186 · Cited by 50

A Co(III) complex cleaving soluble oligomers of h-IAPP in the presence of polymeric aggregates of h-IAPP

Lee, T. Y., Chei, W. S., Ju, H., Lee, M., Lee, S. E., & Suh, J. (2012) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2012.06.089 · Cited by 16

Preparation of a protein‐free total brain white matter lipid fraction: Characterization of liposomes

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A flash in the pan: Dissecting dynamic amyloid intermediates using fluorescence

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Type 2 diabetes as a protein misfolding disease

Mukherjee, A., Morales‐Scheihing, D., Butler, P. C., & Soto, C. A. (2015) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2015.04.005 · Cited by 349

Implications of peptide assemblies in amyloid diseases

Ke, P. C., Sani, M., Ding, F., Käkinen, A., Javed, I., Separovic, F., Davis, T. P., & Mezzenga, R. (2017) · Chemical Society Reviews · doi:10.1039/c7cs00372b · Cited by 340

Islet amyloid polypeptide: structure, function, and pathophysiology

Akter, R., Cao, P., Noor, H., Ridgway, Z., Tu, L.-H., Wang, H., Wong, A. G., Zhang, X., Abedini, A., Schmidt, A. M., et al. (2016) · Journal of Diabetes Research · doi:10.1155/2016/2798269 · Cited by 273

Amyloid assembly and disassembly

Chuang, E., Hori, A. M., Hesketh, C. D., & Shorter, J. (2018) · Journal of Cell Science · doi:10.1242/jcs.189928 · Cited by 188

Effects of in vivo conditions on amyloid aggregation

Owen, M. C., Gnutt, D., Gao, M., Wärmländer, S. K. T. S., Jarvet, J., Gräslund, A., Winter, R., Ebbinghaus, S., & Strodel, B. (2019) · Chemical Society Reviews · doi:10.1039/c8cs00034d · Cited by 181

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

Sparr, E., Engel, M. F. M., Sakharov, D. V., Sprong, M., Jacobs, J., KRUIJFF, B. D., Höppener, J. W. M., & Killian, J. A. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.09.075 · Cited by 257

Membrane permeabilization by Islet Amyloid Polypeptide

Engel, M. F. M. (2009) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2009.03.008 · Cited by 129

Islet Amyloid Polypeptide Membrane Interactions: Effects of Membrane Composition

Zhang, X., Clair, J. R. S., London, E., & Raleigh, D. P. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b01016 · Cited by 123

Membrane interaction of islet amyloid polypeptide

Jayasinghe, S. A., & Langen, R. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.01.022 · Cited by 181

In Vitro Studies of Membrane Permeability Induced by Amyloidogenic Polypeptides Using Large Unilamellar Vesicles

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