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References
Kirschner DA, Abraham C, Selkoe DJ. X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation [erratum]. Proc Natl Acad Sci U S A 1986;83:503–507.
LeVine HD. Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci 1993;2(3):404–410.
Eanes ED, Glenner GG. X-ray diffraction studies on amyloid filaments. J Histochem Cytochem 1968;16:673–677.
Harper JD, Wong SS, Lieber CM, Lansbury PT. Observation of metastable Abeta amyloid protofibrils by atomic force microscopy. Chem Biol 1997;4(2):119–125.
Lashuel HA, Hartley D, Petre BM, et al. Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature 2002;418(6895):291.
Anguiano M, Nowak RJ, Lansbury PT Jr. Protofibrillar islet amyloid polypeptide permeabilizes synthetic vesicles by a pore-like mechanism that may be relevant to type II diabetes. Biochemistry 2002;41(38):11338–11343.
Walsh DM, Lomakin A, Benedek GB, et al. Amyloid beta-protein fibrillogenesis: detection of a protofibrillar intermediate. J Biol Chem 1997;272(35):22364–22372.
Lambert MP, Barlow AK, Chromy BA, et al. Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins. Proc Natl Acad Sci U S A 1998;95(11):6448–6453.
Lomakin A, Teplow DB, Kirschner DA, Benedek GB. Kinetic theory of fibrillogenesis of amyloid beta-protein. Proc Natl Acad Sci U S A 1997;94(15):7942–7947.
Soreghan B, Kosmoski J, Glabe C. Surfactant properties of Alzheimer's A beta peptides and the mechanism of amyloid aggregation. J Biol Chem 1994;269(46):28551–28554.
Terry R. The pathogenesis of Alzheimer disease: an alternative to the amyloid hypothesis. J Neuropathol Exp Neurol 1996;55(10):1023–1025.
Hsia AY, Masliah E, McConlogue L, et al. Plaque-independent disruption of neural circuits in Alzheimer's disease mouse models. Proc Natl Acad Sci U S A 1999;96(6):3228–3233.
Westerman MA, Cooper-Blacketer D, Mariash A, et al. The relationship between Abeta and memory in the Tg2576 mouse model of Alzheimer's disease. J Neurosci 2002;22(5):1858–1867.
Caughey B, Lansbury PT. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu Rev Neurosci 2003;26(1):267–298.
Bucciantini M, Giannoni E, Chiti F, et al. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 2002;416(6880):507–511.
Kayed R, Head E, Thompson JL, et al. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 2003;300(5618):486–489.
Mattson MP, Cheng B, Davis D, et al. Beta-amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. J Neurosci 1992;12:376–389.
Mattson MP. Calcium and neuronal injury in Alzheimer's disease: contributions of beta-amyloid precursor protein mismetabolism, free radicals, and metabolic compromise. Ann N Y Acad Sci 1994;747:50–76.
Arispe N, Pollard HB, Rojas E. Beta-amyloid Ca(2+)-channel hypothesis for neuronal death in Alzheimer disease. Mol Cell Biochem 1994;140:119–125.
Arispe N, Rojas E, Pollard HB. Alzheimer disease amyloid beta protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminum. Proc Natl Acad Sci U S A 1993;90:567–571.
Mirzabekov T, Lin MC, Yuan WL, et al. Channel formation in planar lipid bilayers by a neurotoxic fragment of the beta-amyloid peptide. Biochem Biophys Res Commun 1994;202:1142–1148.
Hirakura Y, Yiu WW, Yamamoto A, Kagan BL. Amyloid peptide channels: blockade by zinc and inhibition by Congo red (amyloid channel block). Amyloid 2000;7(3):194–199.
Mirzabekov TA, Lin M-C, Kagan BL. Pore formation by the cytotoxic islet amyloid peptide amylin. J Biol Chem 1996;271(4):1988–1992.
Kagan BL, Azimov RH, Azimova R. Amyloid peptide channels. J Membr Biol 2004;202:1–10.
Kayed R, Sokolov Y, Edmonds B, et al. Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases. J Biol Chem 2004;279(45):46363–46366.
Green JD, Kreplak L, Goldsbury C, et al. Atomic force microscopy reveals defects within mica supported lipid bilayers induced by the amyloidogenic human amylin peptide. J Mol Biol 2004;342(3):877–887.
Mattson MP. Pathways towards and away from Alzheimer's disease. 2004;430(7000):631–639.
Kawahara M, Kuroda Y, Arispe N, Rojas E. Alzheimer's beta-amyloid, human islet amylin, and prion protein fragment evoke intracellular free calcium elevations by a common mechanism in a hypothalamic GnRH neuronal cell line. J Biol Chem 2000;275(19):14077–14083.
Pierrot N, Ghisdal P, Caumont A-S, Octave J-N. Intraneuronal amyloid-1-42 production triggered by sustained increase of cytosolic calcium concentration induces neuronal death. J Neurochem 2004;88(5):1140–1150.
LaFerla FM. Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease. Nat Rev Neurosci 2002;3(11):862–872.
Bucciantini M, Calloni G, Chiti F, et al. Prefibrillar amyloid protein aggregates share common features of cytotoxicity. J Biol Chem 2004;279(30):31374–31382.
Schubert D, Behl C, Lesley R, et al. Amyloid peptides are toxic via a common oxidative mechanism. Proc Natl Acad Sci U S A 1995;92(6):1989–1993.
Blanchard BJ, Chen A, Rozeboom LM, et al. Inaugural article: efficient reversal of Alzheimer's disease fibril formation and elimination of neurotoxicity by a small molecule. Proc Natl Acad Sci U S A 2004;101(40):14326–14332.
Guo Q, Furukawa K, Sopher BL, et al. Alzheimer's PS-1 mutation perturbs calcium homeostasis and sensitizes PC12 cells to death induced by amyloid beta-peptide. Neuroreport 1996;8(1):379–383.
Kagan BL, Hirakura Y, Azimov R, et al. The channel hypothesis of Alzheimer's disease: current status. Peptides 2002;23(7):1311–1315.
Demuro A, Mina E, Kayed R, et al. Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J Biol Chem 2005;280(17):17294–17300.
Relini A, Torrassa S, Rolandi R, et al. Monitoring the process of HypF fibrillization and liposome permeabilization by protofibrils. J Mol Biol 2004;338(5):943–957.
Janson J, Ashley RH, Harrison D, et al. The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles. Diabetes 1999;48(3):491–498.
Mattson MP. Degenerative and protective signaling mechanisms in the neurofibrillary pathology of AD. Neurobiol Aging 1995;16:447–457; discussion 458–463.
Saitoh T, Horsburgh K, Masliah E. Hyperactivation of signal transduction systems in Alzheimer's disease. Ann N Y Acad Sci 1993;695:34–41.
Shoffner JM. Oxidative phosphorylation defects and Alzheimer's disease. Neurogenetics 1997;1(1):13–19.
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Mina, E.W., Glabe, C.G. (2008). Cellular Membranes as Targets in Amyloid Oligomer Disease Pathogenesis. In: Fisher, A., Memo, M., Stocchi, F., Hanin, I. (eds) Advances in Alzheimer’s and Parkinson’s Disease. Advances in Behavioral Biology, vol 57. Springer, Boston, MA. https://doi.org/10.1007/978-0-387-72076-0_40
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