Cations as switches of amyloid-mediated membrane disruption mechanisms: Calcium and IAPP (608 views)
Biophysical Journal (ISSN: 0006-3495, 1542-0086), 2013 Jan 8; 104(1): 173-184.
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Paper type: Journal Article,
Impact factor: 3.832, 5-year impact factor: 3.976
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Keywords: 1-Palmitoyl-2-Oleoylglycero-3-Phosphoserine, 1-Palmitoyl-2-Oleoylphosphatidylcholine, 2 Oleoyl 1 Palmitoylphosphatidylcholine, 2 Oleoyl 1 Palmitoylphosphatidylserine, Amylin, Amyloid, Calcium, Cation, Coloring Agent, Detergent, Lysomyristoylphosphatidylglycerol, Animal, Article, Atomic Force Microscopy, Cell Membrane, Chemical Phenomena, Chemistry, Drug Effect, Human, Lipid Bilayer, Metabolism, Quartz Crystal Microbalance, Hydrophobic And Hydrophilic Interactions, Islet Amyloid Polypeptide, Quartz Crystal Microbalance Techniques,
Affiliations:
*** IBB - CNR ***
Biophysics, University of Michigan, Ann Arbor, MI, United States
Department of Chemistry, University of Michigan, Ann Arbor, MI, United States
Istituto di Biostrutture e Bioimmagini CNR-UOS, University of Catania, Catania, Italy
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Hebda, J. A., Miranker, A. D., The interplay of catalysis and toxicity by amyloid intermediates on lipid bilayers: Insights from type II diabetes (2009) Annu Rev Biophys, 38, pp. 125-152
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Squier, T. C., Bigelow, D. J., Protein oxidation and age-dependent alterations in calcium homeostasis (2000) Front. Biosci., 5, pp. 504-D526
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Sciacca, M. F. M., Pappalardo, M., La Rosa, C., Calcium-activated membrane interaction of the islet amyloid polypeptide: Implications in the pathogenesis of type II diabetes mellitus (2008) Arch. Biochem. Biophys., 477, pp. 291-298
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Merchant, T. E., Glonek, T., 31P NMR of tissue phospholipids: Competition for Mg2+, Ca2+, Na+ and K+ cations (1992) Lipids, 27, pp. 551-559
Nanga, R. P. R., Brender, J. R., Ramamoorthy, A., Structure and membrane orientation of IAPP in its natively amidated form at physiological pH in a membrane environment (2011) Biochim. Biophys. Acta, 1808, pp. 2337-2342
Boettcher, J. M., Davis-Harrison, R. L., Rienstra, C. M., Atomic view of calcium-induced clustering of phosphatidylserine in mixed lipid bilayers (2011) Biochemistry, 50, pp. 2264-2273
Vernier, P. T., Ziegler, M. J., Dimova, R., Calcium binding and head group dipole angle in phosphatidylserine- phosphatidylcholine bilayers (2009) Langmuir, 25, pp. 1020-1027
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Mart n-Molina, A., Rodr guez-Beas, C., Faraudo, J., Effect of calcium and magnesium on phosphatidylserine membranes: Experiments and all-atomic simulations (2012) Biophys. J., 102, pp. 2095-2103
Brender, J. R., Durr, U. H. N., Heyl, D., Budarapu, M. B., Ramamoorthy, A., Membrane fragmentation by an amyloidogenic fragment of human Islet Amyloid Polypeptide detected by solid-state NMR spectroscopy of membrane nanotubes (2007) Biochimica et Biophysica Acta - Biomembranes, 1768 (9), pp. 2026-2029. , DOI 10. 1016/j. bbamem. 2007. 07. 001, PII S0005273607002477
Feiler, A. A., Sahlholm, A., Sandberg, T., Caldwell, K. D., Adsorption and viscoelastic properties of fractionated mucin (BSM) and bovine serum albumin (BSA) studied with quartz crystal microbalance (QCM-D) (2007) Journal of Colloid and Interface Science, 315 (2), pp. 475-481. , DOI 10. 1016/j. jcis. 2007. 07. 029, PII S0021979707009800
Brender, J. R., Hartman, K., Ramamoorthy, A., A single mutation in the nonamyloidogenic region of islet amyloid polypeptide greatly reduces toxicity (2008) Biochemistry, 47, pp. 12680-12688
Glabe, C. G., Kayed, R., Common structure and toxic function of amyloid oligomers implies a common mechanism of pathogenesis (2006) Neurology, 66 (2 SUPPL. 1), pp. 74-S78
Lashuel, H. A., Hartley, D., Petre, B. M., Walz, T., Lansbury Jr., P. T., Neurodegenerative disease: Amyloid pores from pathogenic mutations (2002) Nature, 418 (6895), p. 291
Patil, S. M., Xu, S. H., Alexandrescu, A. T., Dynamic -helix structure of micelle-bound human amylin (2009) J. Biol. Chem., 284, pp. 11982-11991
Huang, C. J., Gurlo, T., Butler, P. C., Calcium-activated calpain-2 is a mediator of cell dysfunction and apoptosis in type 2 diabetes (2010) J. Biol. Chem., 285, pp. 339-348
Hall, J. E., Cahalan, M. D., Calcium-induced inactivation of alamethicin in asymmetric lipid bilayers (1982) Journal of General Physiology, 79 (3), pp. 387-409
Meratan, A. A., Ghasemi, A., Nemat-Gorgani, M., Membrane integrity and amyloid cytotoxicity: A model study involving mitochondria and lysozyme fibrillation products (2011) J. Mol. Biol., 409, pp. 826-838
Zakharov, S. D., Hulleman, J. D., Dutseva, E. A., Antonenko, Y. N., Rochet, J. -C., Cramer, W. A., Helical -synuclein forms highly conductive ion channels (2007) Biochemistry, 46 (50), pp. 14369-14379. , DOI 10. 1021/bi701275p
Kagan, B. L., Thundimadathil, J., Amyloid peptide pores and the sheet conformation (2010) Adv. Exp. Med. Biol., 677, pp. 150-167
Kagan, B. L., Jang, H., Nussinov, R., Antimicrobial properties of amyloid peptides (2012) Mol. Pharm., 9, pp. 708-717
Reynolds, N. P., Soragni, A., Seeger, S., Mechanism of membrane interaction and disruption by -synuclein (2011) J. Am. Chem. Soc., 133, pp. 19366-19375
Van Rooijen, B. D., Claessens, M. M. A. E., Subramaniam, V., Membrane interactions of oligomeric -synuclein: Potential role in Parkinson's disease (2010) Curr. Protein Pept. Sci., 11, pp. 334-342
Mattson, M. P., Chan, S. L., Calcium orchestrates apoptosis (2003) Nature Cell Biology, 5 (12), pp. 1041-1043. , DOI 10. 1038/ncb1203-1041
Biophysical Journal (ISSN: 0006-3495, 1542-0086), 2013 Jan 8; 104(1): 173-184.
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Paper type: Journal Article,
Impact factor: 3.832, 5-year impact factor: 3.976
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84872166034&partnerID=40&md5=8b2b4c89607e48dbaace634df7273795
Keywords: 1-Palmitoyl-2-Oleoylglycero-3-Phosphoserine, 1-Palmitoyl-2-Oleoylphosphatidylcholine, 2 Oleoyl 1 Palmitoylphosphatidylcholine, 2 Oleoyl 1 Palmitoylphosphatidylserine, Amylin, Amyloid, Calcium, Cation, Coloring Agent, Detergent, Lysomyristoylphosphatidylglycerol, Animal, Article, Atomic Force Microscopy, Cell Membrane, Chemical Phenomena, Chemistry, Drug Effect, Human, Lipid Bilayer, Metabolism, Quartz Crystal Microbalance, Hydrophobic And Hydrophilic Interactions, Islet Amyloid Polypeptide, Quartz Crystal Microbalance Techniques,
Affiliations:
*** IBB - CNR ***
Biophysics, University of Michigan, Ann Arbor, MI, United States
Department of Chemistry, University of Michigan, Ann Arbor, MI, United States
Istituto di Biostrutture e Bioimmagini CNR-UOS, University of Catania, Catania, Italy
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Cations as switches of amyloid-mediated membrane disruption mechanisms: Calcium and IAPP
Disruption of the integrity of the plasma membrane by amyloidogenic proteins is linked to the pathogenesis of a number of common age-related diseases. Although accumulating evidence suggests that adverse environmental stressors such as unbalanced levels of metal ions may trigger amyloid-mediated membrane damage, many features of the molecular mechanisms underlying these events are unknown. Using human islet amyloid polypeptide (hIAPP, aka amylin), an amyloidogenic peptide associated with β-cell death in type 2 diabetes, we demonstrate that the presence of Ca2+ ions inhibits membrane damage occurring immediately after the interaction of freshly dissolved hIAPP with the membrane, but significantly enhances fiber-dependent membrane disruption. In particular, dye leakage, quartz crystal microbalance, atomic force microscopy, and NMR experiments show that Ca2+ ions promote a shallow membrane insertion of hIAPP, which leads to the removal of lipids from the bilayer through a detergent-like mechanism triggered by fiber growth. Because both types of membrane-damage mechanisms are common to amyloid toxicity by most amyloidogenic proteins, it is likely that unregulated ion homeostasis, amyloid aggregation, and membrane disruption are all parts of a self-perpetuating cycle that fuels amyloid cytotoxicity. © 2013 Biophysical Society.
Disruption of the integrity of the plasma membrane by amyloidogenic proteins is linked to the pathogenesis of a number of common age-related diseases. Although accumulating evidence suggests that adverse environmental stressors such as unbalanced levels of metal ions may trigger amyloid-mediated membrane damage, many features of the molecular mechanisms underlying these events are unknown. Using human islet amyloid polypeptide (hIAPP, aka amylin), an amyloidogenic peptide associated with β-cell death in type 2 diabetes, we demonstrate that the presence of Ca2+ ions inhibits membrane damage occurring immediately after the interaction of freshly dissolved hIAPP with the membrane, but significantly enhances fiber-dependent membrane disruption. In particular, dye leakage, quartz crystal microbalance, atomic force microscopy, and NMR experiments show that Ca2+ ions promote a shallow membrane insertion of hIAPP, which leads to the removal of lipids from the bilayer through a detergent-like mechanism triggered by fiber growth. Because both types of membrane-damage mechanisms are common to amyloid toxicity by most amyloidogenic proteins, it is likely that unregulated ion homeostasis, amyloid aggregation, and membrane disruption are all parts of a self-perpetuating cycle that fuels amyloid cytotoxicity. © 2013 Biophysical Society.
Cations as switches of amyloid-mediated membrane disruption mechanisms: Calcium and IAPP
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Cations as switches of amyloid-mediated membrane disruption mechanisms: Calcium and IAPP
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Scalia M, Satriano C, Greca R, Stella AM, Rizzarelli E, Spina-Purrello V
* PARP-1 inhibitors DPQ and PJ-34 negatively modulate proinflammatory commitment of human glioblastoma cells (425 views)
Neurochemical Research (ISSN: 1573-6903, 0364-3190), 2013 Jan; 38(1): 50-58.
Impact Factor: 2.551
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Pannuzzo M, Milardi D, Raudino A, Karttunen M, La Rosa C
* Analytical model and multiscale simulations of Aβ peptide aggregation in lipid membranes: Towards a unifying description of conformational transitions, oligomerization and membrane damage (737 views)
Phys Chem Chem Phys (ISSN: 1463-9076, 1463-3907, 1463-9084electronic), 2013; 15(23): 8940-8951.
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Arnesano F, Scintilla S, Calò V, Bonfrate E, Ingrosso C, Losacco M, Pellegrino T, Rizzarelli E, Natile G
* Copper-triggered aggregation of ubiquitin (534 views)
Plosone (ISSN: 1932-6203, 1932-6203electronic, 1932-6203linking), 2009 Sep 16; 4(9): e7052-e7052.
Impact Factor: 4.351
View Export to BibTeX Export to EndNote
* PARP-1 inhibitors DPQ and PJ-34 negatively modulate proinflammatory commitment of human glioblastoma cells (425 views)
Neurochemical Research (ISSN: 1573-6903, 0364-3190), 2013 Jan; 38(1): 50-58.
Impact Factor: 2.551
View Export to BibTeX Export to EndNote
Pannuzzo M, Milardi D, Raudino A, Karttunen M, La Rosa C
* Analytical model and multiscale simulations of Aβ peptide aggregation in lipid membranes: Towards a unifying description of conformational transitions, oligomerization and membrane damage (737 views)
Phys Chem Chem Phys (ISSN: 1463-9076, 1463-3907, 1463-9084electronic), 2013; 15(23): 8940-8951.
Impact Factor: 4.198
View Export to BibTeX Export to EndNote
Arnesano F, Scintilla S, Calò V, Bonfrate E, Ingrosso C, Losacco M, Pellegrino T, Rizzarelli E, Natile G
* Copper-triggered aggregation of ubiquitin (534 views)
Plosone (ISSN: 1932-6203, 1932-6203electronic, 1932-6203linking), 2009 Sep 16; 4(9): e7052-e7052.
Impact Factor: 4.351
View Export to BibTeX Export to EndNote
3 Records (2 excluding Abstracts).
Total impact factor: 11.1 (6.749 excluding Abstracts).
Total 5 year impact factor: 10.783 (6.4 excluding Abstracts).
Total impact factor: 11.1 (6.749 excluding Abstracts).
Total 5 year impact factor: 10.783 (6.4 excluding Abstracts).
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