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International Journal of Alzheimer’s Disease
Volume 2011, Article ID 917629, 13 pages
http://dx.doi.org/10.4061/2011/917629
Research Article

Fluorescent Analysis of the Cell-Selective Alzheimer's Disease Aβ Peptide Surface Membrane Binding: Influence of Membrane Components

Department of Anatomy, Physiology and Genetics, and Institute for Molecular Medicine, Uniformed Services University School of Medicine (USUHS), Bethesda, MD 20814, USA

Received 10 December 2010; Revised 10 February 2011; Accepted 22 March 2011

Academic Editor: Brian Austen

Copyright © 2011 Olga Simakova and Nelson J. Arispe. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. B. A. Yankner, “Mechanisms of neuronal degeneration in Alzheimer's disease,” Neuron, vol. 16, no. 5, pp. 921–932, 1996. View at Publisher · View at Google Scholar · View at Scopus
  2. O. Simakova and N. J. Arispe, “Early and late cytotoxic effects of external application of the Alzheimer's Aβ result from the initial formation and function of Aβ ion channels,” Biochemistry, vol. 45, no. 18, pp. 5907–5915, 2006. View at Publisher · View at Google Scholar
  3. O. Simakova and N. J. Arispe, “The cell-selective neurotoxicity of the Alzheimer's Aβ peptide is determined by surface phosphatidylserine and cytosolic ATP levels. Membrane binding is required for Aβ toxicity,” Journal of Neuroscience, vol. 27, no. 50, pp. 13719–13729, 2007. View at Publisher · View at Google Scholar
  4. V. A. Fadok, D. R. Voelker, P. A. Campbell, J. J. Cohen, D. L. Bratton, and P. M. Henson, “Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages,” Journal of Immunology, vol. 148, no. 7, pp. 2207–2216, 1992. View at Google Scholar · View at Scopus
  5. V. A. Fadok, D. L. Bratton, D. M. Rose, A. Pearson, R. A. B. Ezekewitz, and P. M. Henson, “A receptor for phosphatidylserine-specific clearance of apoptotic cells,” Nature, vol. 405, no. 6782, pp. 85–90, 2000. View at Publisher · View at Google Scholar · View at Scopus
  6. O. C. Martin and R. E. Pagano, “Transbilayer movement of fluorescent analogs of phosphatidylserine and phosphatidylethanolamine at the plasma membrane of cultured cells. Evidence for a protein-mediated and ATP-dependent process(es),” Journal of Biological Chemistry, vol. 262, no. 12, pp. 5890–5898, 1987. View at Google Scholar · View at Scopus
  7. S. J. Martin, C. P. M. Reutelingsperger, A. J. McGahon et al., “Early redistribution of plasma membrane phosphatidylserine is a general feature of apoptosis regardless of the initiating stimulus: inhibition by overexpression of Bcl-2 and Abl,” Journal of Experimental Medicine, vol. 182, no. 5, pp. 1545–1556, 1995. View at Publisher · View at Google Scholar · View at Scopus
  8. R. F. A. Zwaal and A. J. Schroit, “Pathophysiologic implications of membrane phospholipid asymmetry in blood cells,” Blood, vol. 89, no. 4, pp. 1121–1132, 1997. View at Google Scholar · View at Scopus
  9. R. F. A. Zwaal, P. Comfurius, and E. M. Bevers, “Surface exposure of phosphatidylserine in pathological cells,” Cellular and Molecular Life Sciences, vol. 62, no. 9, pp. 971–988, 2005. View at Publisher · View at Google Scholar · View at Scopus
  10. N. Arispe, M. Doh, O. Simakova, B. Kurganov, and A. De Maio, “Hsc70 and Hsp70 interact with phosphatidylserine on the surface of PC12 cells resulting in a decrease of viability,” FASEB Journal, vol. 18, no. 14, pp. 1636–1645, 2004. View at Publisher · View at Google Scholar · View at Scopus
  11. E. Terzi, G. Hölzemann, and J. Seelig, “Interaction of Alzheimer β-amyloid peptide(1-40) with lipid membranes,” Biochemistry, vol. 36, no. 48, pp. 14845–14852, 1997. View at Publisher · View at Google Scholar · View at Scopus
  12. A. Kakio, S. I. Nishimoto, K. Yanagisawa, Y. Kozutsumi, and K. Matsuzaki, “Cholesterol-dependent formation of GM1 ganglioside-bound amyloid β-protein, an endogenous seed for Alzheimer amyloid,” Journal of Biological Chemistry, vol. 276, no. 27, pp. 24985–24990, 2001. View at Publisher · View at Google Scholar · View at Scopus
  13. K. Matsuzaki, “Physicochemical interactions of amyloid β-peptide with lipid bilayers,” Biochimica et Biophysica Acta, vol. 1768, no. 8, pp. 1935–1942, 2007. View at Publisher · View at Google Scholar · View at Scopus
  14. K. Yanagisawa, “Role of gangliosides in Alzheimer's disease,” Biochimica et Biophysica Acta, vol. 1768, no. 8, pp. 1943–1951, 2007. View at Publisher · View at Google Scholar · View at Scopus
  15. K. Matsuzaki, K. Kato, and K. Yanagisawa, “Aβ polymerization through interaction with membrane gangliosides,” Biochimica et Biophysica Acta, vol. 1801, no. 8, pp. 868–877, 2010. View at Publisher · View at Google Scholar · View at Scopus
  16. S.-R. Ji, Y. Wu, and S.-F. Sui, “Cholesterol is an important factor affecting the membrane insertion of β-amyloid peptide (Aβ1-40), which may potentially inhibit the fibril formation,” Journal of Biological Chemistry, vol. 277, no. 8, pp. 6273–6279, 2002. View at Publisher · View at Google Scholar
  17. J. Vargas, J. M. Alarcón, and E. Rojas, “Displacement currents associated with the insertion of Alzheimer disease amyloid β-peptide into planar bilayer membranes,” Biophysical Journal, vol. 79, no. 2, pp. 934–944, 2000. View at Google Scholar · View at Scopus
  18. N. Arispe, J. C. Diaz, and O. Simakova, “Aβ ion channels. Prospects for treating Alzheimer's disease with Aβ channel blockers,” Biochimica et Biophysica Acta, vol. 1768, no. 8, pp. 1952–1965, 2007. View at Publisher · View at Google Scholar · View at Scopus
  19. P. T. Wong, J. A. Schauerte, K. C. Wisser et al., “Amyloid-β membrane binding and permeabilization are distinct processes influenced separated by membrane charge and fluidity,” Journal of Molecular Biology, vol. 386, no. 1, pp. 81–96, 2009. View at Publisher · View at Google Scholar · View at Scopus
  20. A. W. Norman, R. A. Demel, B. de Kruyff, and L. L. van Deenen, “Studies on the biological properties of polyene antibiotics. Evidence for the direct interaction of filipin with cholesterol,” Journal of Biological Chemistry, vol. 247, no. 6, pp. 1918–1929, 1972. View at Google Scholar · View at Scopus
  21. M. Simons, P. Keller, B. De Strooper, K. Beyreuther, C. G. Dotti, and K. Simons, “Cholesterol depletion inhibits the generation of β-amyloid in hippocampal neurons,” Proceedings of the National Academy of Sciences of the United States of America, vol. 95, no. 11, pp. 6460–6464, 1998. View at Publisher · View at Google Scholar · View at Scopus
  22. J. C. Diaz and N. Arispe, “GM1 and PS enrichment of cell membranes assists Aβ membrane binding and ion channel formation,” Biophysical Journal, vol. 94, no. 2, p. p1025, 2008. View at Google Scholar
  23. N. Arispe and O. Simakova, “Alzheimer’s disease Aβ peptide binding to cell membranes is correlated to membrane surface phosphatidylserine levels,” Biophysical Journal, vol. 92, no. 3, p. 612a, 2007. View at Google Scholar
  24. O. Simakova and N. Arispe, “High membrane cholesterol levels characterize cells identified by their Aβ binding affinity,” Biophysical Journal, vol. 94, no. 2, p. p1025, 2008. View at Google Scholar
  25. N. Arispe and M. Doh, “Plasma membrane cholesterol controls the cytotoxicity of Alzheimer's disease AβP (1-40) and (1-42) peptides,” FASEB Journal, vol. 16, no. 12, pp. 1526–1536, 2002. View at Publisher · View at Google Scholar · View at Scopus
  26. T.-L. Lau, E. E. Ambroggio, D. J. Tew et al., “Amyloid-β peptide disruption of lipid membranes and the effect of metal ions,” Journal of Molecular Biology, vol. 356, no. 3, pp. 759–770, 2006. View at Publisher · View at Google Scholar
  27. K. Yanagisawa, “GM1 ganglioside and the seeding of amyloid in Alzheimer's disease: endogenous seed for Alzheimer amyloid,” Neuroscientist, vol. 11, no. 3, pp. 250–260, 2005. View at Publisher · View at Google Scholar · View at Scopus
  28. L. Qiu, A. Lewis, J. Como et al., “Cholesterol modulates the interaction of β-amyloid peptide with lipid bilayers,” Biophysical Journal, vol. 96, no. 10, pp. 4299–4307, 2009. View at Publisher · View at Google Scholar · View at Scopus
  29. W. E. Muller, S. Koch, A. Eckert, H. Hartmann, and K. Scheuer, “β-Amyloid peptide decreases membrane fluidity,” Brain Research, vol. 674, no. 1, pp. 133–136, 1995. View at Publisher · View at Google Scholar · View at Scopus
  30. A. Buchsteiner, T. Hauß, S. Dante, and N. A. Dencher, “Alzheimer's disease amyloid-β peptide analogue alters the ps-dynamics of phospholipid membranes,” Biochimica et Biophysica Acta, vol. 1798, no. 10, pp. 1969–1976, 2010. View at Publisher · View at Google Scholar
  31. S. Dante, T. Hauß, A. Brandt, and N. A. Dencher, “Membrane fusogenic activity of the Alzheimer's peptide Aβ(1-42) demonstrated by small-angle neutron scattering,” Journal of Molecular Biology, vol. 376, no. 2, pp. 393–404, 2008. View at Publisher · View at Google Scholar · View at Scopus
  32. N. Arispe, E. Rojas, and H. B. Pollard, “Alzheimer disease amyloid β protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminum,” Proceedings of the National Academy of Sciences of the United States of America, vol. 90, no. 2, pp. 567–571, 1993. View at Publisher · View at Google Scholar · View at Scopus
  33. G. Lee, H. B. Pollard, and N. Arispe, “Annexin 5 and apolipoprotein E2 protect against Alzheimer's amyloid-β-peptide cytotoxicity by competitive inhibition at a common phosphatidylserine interaction site,” Peptides, vol. 23, no. 7, pp. 1249–1263, 2002. View at Publisher · View at Google Scholar · View at Scopus
  34. M. Bokvist, F. Lindström, A. Watts, and G. Gröbner, “Two types of Alzheimer's β-amyloid (1-40) peptide membrane interactions: aggregation preventing transmembrane anchoring versus accelerated surface fibril formation,” Journal of Molecular Biology, vol. 335, no. 4, pp. 1039–1049, 2004. View at Publisher · View at Google Scholar · View at Scopus
  35. L. P. Choo-Smith and W. K. Surewicz, “The interaction between Alzheimer amyloid β(1-40) peptide and ganglioside G(M1)-containing membranes,” FEBS Letters, vol. 402, no. 2-3, pp. 95–98, 1997. View at Publisher · View at Google Scholar · View at Scopus
  36. T. Ariga, K. Kobayashi, A. Hasegawa, M. Kiso, H. Ishida, and T. Miyatake, “Characterization of high-affinity binding between gangliosides and amyloid β-protein,” Archives of Biochemistry and Biophysics, vol. 388, no. 2, pp. 225–230, 2001. View at Publisher · View at Google Scholar · View at Scopus
  37. C. Cecchi, F. Rosati, A. Pensalfini et al., “Seladin-1/DHCR24 protects neuroblastoma cells against Aβ toxicity by increasing membrane cholesterol content,” Journal of Cellular and Molecular Medicine, vol. 12, no. 5B, pp. 1990–2002, 2008. View at Publisher · View at Google Scholar · View at Scopus
  38. T. Mirzabekov, M. C. Lin, W. L. Yuan et al., “Channel formation in planar lipid bilayers by a neurotoxic fragment of the beta-amyloid peptide,” Biochemical and Biophysical Research Communications, vol. 202, no. 2, pp. 1142–1148, 1994. View at Publisher · View at Google Scholar · View at Scopus
  39. M. Kawahara, Y. Kuroda, N. Arispe, and E. Rojas, “Alzheimer's β-amyloid, human islet amylin, and priori protein fragment evoke intracellular free calcium elevations by a common mechanism in a hypothalamic GnRH neuronal cell line,” Journal of Biological Chemistry, vol. 275, no. 19, pp. 14077–14083, 2000. View at Publisher · View at Google Scholar · View at Scopus
  40. M. Kawahara and Y. Kuroda, “Intracellular calcium changes in neuronal cells induced by Alzheimer's β-amyloid protein are blocked by estradiol and cholesterol,” Cellular and Molecular Neurobiology, vol. 21, no. 1, pp. 1–13, 2001. View at Publisher · View at Google Scholar