Bexarotene blocks calcium-permeable ion channels formed by neurotoxic Alzheimer's β-amyloid peptides

ACS Chemical Neuroscience

Volumn 5, Issue 3, 2014, Pages 216-224

  Fantini, Jacques ^a   Di Scala, Coralie ^a   Yahi, Nouara ^a   Troadec, Jean Denis ^a   Sadelli, Kevin ^a   Chahinian, Henri ^a   Garmy, Nicolas ^a  

^a AIX MARSEILLE UNIVERSITY   (France)

Author keywords

Alzheimer's disease; amyloid; bexarotene; cholesterol; oligomers; therapy

Indexed keywords

AMYLOID BETA PROTEIN; BEXAROTENE; CALCIUM CHANNEL; CHOLESTEROL; ISOLEUCINE; AMYLOID BETA-PROTEIN (1-42); AMYLOID BETA-PROTEIN (25-35); CALCIUM; CALCIUM CHANNEL BLOCKING AGENT; PEPTIDE FRAGMENT; TETRALIN DERIVATIVE; WATER;

ABSORPTION SPECTROSCOPY; ALZHEIMER DISEASE; ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; CONTROLLED STUDY; DRUG ABSORPTION; DRUG BINDING SITE; DRUG MECHANISM; DRUG PURITY; DRUG STRUCTURE; HIGH PERFORMANCE THIN LAYER CHROMATOGRAPHY; HYDROGEN BOND; MOLECULAR DOCKING; MOLECULAR DYNAMICS; NERVE CELL MEMBRANE; NEUROTOXICITY; NONHUMAN; OLIGOMERIZATION; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; ABSORPTION; BINDING COMPETITION; CELL MEMBRANE; CHEMICAL STRUCTURE; CHEMISTRY; DRUG EFFECTS; HUMAN; METABOLISM; PROTEIN MULTIMERIZATION; SPECTROSCOPY; TUMOR CELL LINE;

ABSORPTION, PHYSICOCHEMICAL; AMYLOID BETA-PEPTIDES; BINDING, COMPETITIVE; CALCIUM; CALCIUM CHANNEL BLOCKERS; CALCIUM CHANNELS; CELL LINE, TUMOR; CELL MEMBRANE; CHOLESTEROL; HUMANS; MODELS, MOLECULAR; MOLECULAR DOCKING SIMULATION; MOLECULAR DYNAMICS SIMULATION; PEPTIDE FRAGMENTS; PROTEIN MULTIMERIZATION; SPECTRUM ANALYSIS; TETRAHYDRONAPHTHALENES; WATER;

EID: 84896451184     PISSN: None     EISSN: 19487193     Source Type: Journal    
DOI: 10.1021/cn400183w     Document Type: Article

References (38)

1. Cramer, P. E., Cirrito, J. R., Wesson, D. W., Lee, C. Y., Karlo, J. C., Zinn, A. E., Casali, B. T., Restivo, J. L., Goebel, W. D., James, M. J., Brunden, K. R., Wilson, D. A., and Landreth, G. E. (2012) ApoE-directed therapeutics rapidly clear β-amyloid and reverse deficits in AD mouse models Science 335, 1503-1506
2. LaFerla, F. M. (2012) Preclinical success against Alzheimers disease with an old drug N. Engl. J. Med. 367, 570-572
3. Fitz, N. F., Cronican, A. A., Lefterov, I., and Koldamova, R. (2013) Comment on "ApoE-Directed Therapeutics Rapidly Clear β-Amyloid and Reverse Deficits in AD Mouse Models" Science 340, 924-c
4. Landreth, G. E., Cramer, P. E., Lakner, M. M., Cirrito, J. R., Wesson, D. W., Brunden, K. R., and Wilson, D. A. (2013) Response to Comments on "ApoE-Directed Therapeutics Rapidly Clear β-Amyloid and Reverse Deficits in AD Mouse Models" Science 340, 924-g
5. Price, A. R., Xu, G., Siemienski, Z. B., Smithson, L. A., Borchelt, D. R., Golde, T. E., and Felsenstein, K. M. (2013) Comment on "ApoE-Directed Therapeutics Rapidly Clear β-Amyloid and Reverse Deficits in AD Mouse Models" Science 340, 924-d
6. Tesseur, I., Lo, A. C., Roberfroid, A., Dietvorst, S., Van Broeck, B., Borgers, M., Gijsen, H., Moechars, D., Mercken, M., Kemp, J., DHooge, R., and De Strooper, B. (2013) Comment on "ApoE-Directed Therapeutics Rapidly Clear β-Amyloid and Reverse Deficits in AD Mouse Models" Science 340, 924-e
7. Veeraraghavalu, K., Zhang, C., Miller, S., Hefendehl, J. K., Rajapaksha, T. W., Ulrich, J., Jucker, M., Holtzman, D. M., Tanzi, R. E., Vassar, R., and Sisodia, S. S. (2013) Comment on "ApoE-Directed Therapeutics Rapidly Clear β-Amyloid and Reverse Deficits in AD Mouse Models" Science 340, 924-f
8. LaClair, K. D., Manaye, K. F., Lee, D. L., Allard, J. S., Savonenko, A. V., Troncoso, J. C., and Wong, P. C. (2013) Treatment with bexarotene, a compound that increases apolipoprotein-E, provides no cognitive benefit in mutant APP/PS1 mice Mol. Neurodegener. 8, 18
9. Fantini, J. and Yahi, N. (2010) Molecular insights into amyloid regulation by membrane cholesterol and sphingolipids: common mechanisms in neurodegenerative diseases Expert Rev. Mol. Med. 12, e27
10. Jang, H., Connelly, L., Arce, F. T., Ramachandran, R., Lal, R., Kagan, B. L., and Nussinov, R. (2013) Alzheimers disease: which type of amyloid-preventing drug agents to employ? Phys. Chem. Chem. Phys. 15, 8868-8877
11. Demuro, A., Mina, E., Kayed, R., Milton, S. C., Parker, I., and Glabe, C. G. (2005) Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers J. Biol. Chem. 280, 17294-17300
12. Kayed, R. and Lasagna-Reeves, C. A. (2013) Molecular mechanisms of amyloid oligomers toxicity J. Alzheimer's Dis. 33, S67-S78
13. Esparza, T. J., Zhao, H., Cirrito, J. R., Cairns, N. J., Bateman, R. J., Holtzman, D. M., and Brody, D. L. (2012) Amyloid-beta oligomerization in Alzheimer dementia versus high-pathology controls Ann. Neurol. 73, 104-119
14. Arispe, N. and Doh, M. (2002) Plasma membrane cholesterol controls the cytotoxicity of Alzheimers disease AbetaP (1-40) and (1-42) peptides FASEB J. 16, 1526-1536
15. Abramov, A. Y., Ionov, M., Pavlov, E., and Duchen, M. R. (2011) Membrane cholesterol content plays a key role in the neurotoxicity of β-amyloid: implications for Alzheimers disease Aging Cell 10, 595-603
16. Di Scala, C., Yahi, N., Lelièvre, C., Garmy, N., Chahinian, H., and Fantini, J. (2013) Biochemical identification of a linear cholesterol-binding domain within Alzheimers β amyloid peptide ACS Chem. Neurosci. 4, 509-517
17. Yu, X. and Zheng, J. (2012) Cholesterol promotes the interaction of Alzheimer β-amyloid monomer with lipid bilayer J. Mol. Biol. 421, 561-571
18. Di Scala, C., Troadec, J. D., Lelièvre, C., Garmy, N., Fantini, J., and Chahinian, H. (2014) Mechanism of cholesterol-assisted oligomeric channel formation by a short Alzheimer β-amyloid peptide J. Neurochem. 128, 186-195
19. Mattson, M. P., Cheng, B., Davis, D., Bryant, K., Lieberburg, I., and Rydel, R. E. (1992) Beta-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity J. Neurosci. 12, 376-389
20. Simmons, M. A. and Schneider, C. R. (1993) Amyloid beta peptides act directly on single neurons Neurosci. Lett. 150, 133-136
21. Millucci, L., Ghezzi, L., Bernardini, A., and Santucci, A. (2010) Conformations and biological activities of amyloid beta peptide 25-35 Curr. Protein Pept. Sci. 11, 24-67
22. Kubo, T., Nishimura, S., Kumagae, Y., and Kaneko, I. (2002) In vivo conversion of racemized beta-amyloid ([D-Ser 26]A beta 1-40) to truncated and toxic fragments ([D-Ser 26]A beta 25-35/40) and fragment presence in the brains of Alzheimers patients J. Neurosci. Res. 70, 474-483
23. Thakur, G., Pao, C., Micic, M., Johnson, S., and Leblanc, R. M. (2011) Surface chemistry of lipid raft and amyloid Aβ (1-40) Langmuir monolayer Colloids Surf., B 87, 369-377
24. ONeil, M. J., Ed. (2001) The Merck Index: an encyclopedia of chemicals, drugs, and biologicals, 13 th ed., Merck, Rahway, NJ.
25. Fantini, J., Carlus, D., and Yahi, N. (2011) The fusogenic tilted peptide (67-78) of α-synuclein is a cholesterol binding domain Biochim. Biophys. Acta 1808, 2343-23451
26. Jang, H., Arce, F. T., Ramachandran, S., Capone, R., Azimova, R., Kagan, B. L., Nussinov, R., and Lal, R. (2010) Truncated beta-amyloid peptide channels provide an alternative mechanism for Alzheimers Disease and Down syndrome Proc. Natl. Acad. Sci. U.S.A. 107, 6538-6543
27. Arispe, N., Pollard, H. B., and Rojas, E. (1996) Zn2+ interaction with Alzheimer amyloid beta protein calcium channels Proc. Natl. Acad. Sci. U.S.A. 93, 1710-1715
28. Vallee, B. L. and Auld, D. S. (1993) Cocatalytic zinc motifs in enzyme catalysis Proc. Natl. Acad. Sci. U.S.A. 90, 2715-2718
29. Simons, M., Keller, P., Dichgans, J., and Schulz, J. B. (2001) Cholesterol and Alzheimers disease: is there a link? Neurology 57, 1089-1093
30. Ji, S. R., Wu, Y., and Sui, S. F. (2002) Cholesterol is an important factor affecting the membrane insertion of beta-amyloid peptide (A beta 1-40), which may potentially inhibit the fibril formation J. Biol. Chem. 277, 6273-6279
31. Qiu, L., Lewis, A., Como, J., Vaughn, M. W., Huang, J., Somerharju, P., Virtanen, J., and Cheng, K. H. (2009) Cholesterol modulates the interaction of beta-amyloid peptide with lipid bilayers Biophys. J. 96, 4299-4307
32. Micelli, S., Meleleo, D., Picciarelli, V., and Gallucci, E. (2004) Effect of sterols on beta-amyloid peptide (AbetaP 1-40) channel formation and their properties in planar lipid membranes Biophys. J. 86, 2231-7223
33. McFarland, K., Spalding, T. A., Hubbard, D., Ma, J. N., Olsson, R., and Burstein, E. S. (2013) Low Dose Bexarotene Treatment Rescues Dopamine Neurons and Restores Behavioral Function in Models of Parkinsons Disease ACS Chem. Neurosci. 4, 1430-1438
34. Gandy, S. and DeKosky, S. T. (2013) Toward the treatment and prevention of Alzheimer's disease: rational strategies and recent progress Annu. Rev. Med. 64, 367-383
35. Brooks, B. R., Brooks, C. L., 3rd, Mackerell, A. D., Jr., Nilsson, L., Petrella, R. J., Roux, B., Won, Y., Archontis, G., Bartels, C., Boresch, S., Caflisch, A., Caves, L., Cui, Q., Dinner, A. R., Feig, M., Fischer, S., Gao, J., Hodoscek, M., Im, W., Kuczera, K., Lazaridis, T., Ma, J., Ovchinnikov, V., Paci, E., Pastor, R. W., Post, C. B., Pu, J. Z., Schaefer, M., Tidor, B., Venable, R. M., Woodcock, H. L., Wu, X., Yang, W., York, D. M., and Karplus, M. (2009) CHARMM: the biomolecular simulation program J. Comput. Chem. 30, 1545-614
36. Singh, R. P., Brooks, B. R., and Klauda, J. B. (2009) Binding and release of cholesterol in the Osh4 protein of yeast Proteins 75, 468-477
37. Thomsen, R. and Christensen, M. H. (2006) MolDock: A New Technique for High-Accuracy Molecular Docking J. Med. Chem. 49, 3315-3321
38. Fantini, J. and Yahi, N. (2011) Molecular basis for the glycosphingolipid-binding specificity of α-synuclein: key role of tyrosine 39 in membrane insertion J. Mol. Biol. 408, 654-669