Acetylcholinesterase-amyloid-β-peptide interaction: Effect of Congo Red and the role of the Wnt pathway

Current Alzheimer Research

Volumn 2, Issue 3, 2005, Pages 301-306

  Inestrosa, Nibaldo C ^a   Alvarez, Alejandra ^a   Dinamarca, Margarita C ^a   Pérez Acle, Tomás ^a   Colombres, Marcela ^a  

^a PONTIFICIA UNIVERSIDAD CATÓLICA DE CHILE   (Chile)

Author keywords

Acetylcholinesterase; Alzheimer's disease; Amyloid peptide; Congo Red; Peripheral anionic site

Indexed keywords

ACETYLCHOLINE; ACETYLCHOLINESTERASE; AMYLOID; AMYLOID BETA PROTEIN; AP 2238; BETA CATENIN; CHOLINESTERASE; CHOLINESTERASE INHIBITOR; CONGO RED; DONEPEZIL; EDROPHONIUM; FASCICULIN; GALLAMINE; PROPIDIUM IODIDE; UNCLASSIFIED DRUG; WNT PROTEIN;

ALZHEIMER DISEASE; BINDING SITE; COMPARATIVE STUDY; COMPLEX FORMATION; CONFERENCE PAPER; DEGENERATIVE DISEASE; DISEASE COURSE; HUMAN; NEUROTOXICITY; NONHUMAN; PATHOPHYSIOLOGY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEPLETION; PROTEIN PROTEIN INTERACTION; SIGNAL TRANSDUCTION;

ACETYLCHOLINESTERASE; AMYLOID BETA-PROTEIN; ANIMALS; COLORING AGENTS; CONGO RED; DRUG INTERACTIONS; HUMANS; INTERCELLULAR SIGNALING PEPTIDES AND PROTEINS; WNT PROTEINS;

EID: 22144490779     PISSN: 15672050     EISSN: None     Source Type: Journal    
DOI: 10.2174/1567205054367928     Document Type: Conference Paper

References (31)

1. Colombres M, Sagal JP and Inestrosa NC. An Overview of the Current and Novel Drugs for Alzheimer's disease with Particular Reference to Anti-cholinesterase Compounds. Curr Pharm Des 10: 3121-3130 (2004).
2. Fuentealba RA, Parias G, Scheu J, Bronfman M, Marzolo MP and Inestrosa NC. Signal transduction during amyloid-β-peptide neurotoxicity: role in Alzheimer's Disease. Brain Res Brain Res Rev 47: 275-289 (2004).
3. Inestrosa NC and Perelman A. Distribution and anchoring of molecular forms of acetylcholinesterase. Trends Pharmacol Sci 10: 325-329 (1989).
4. Grisaru D, Sternfeld M, Eldor A, Click D and Soreq H. Structural roles of acetylcholinesterase variants in biology and pathology. Eur J Biochem 264: 672-686 (1999).
5. Muñoz FJ, Aldunate R and Inestrosa NC. Peripheral binding site is involved in the neurotrophic activity of acetylcholinesterase. Neuroreport. 10: 3621-3625 (1999).
6. von Bernhardi R, Ramirez G, De Ferrari GV and Inestrosa NC. Acetylcholinesterase induces the expression of the β-amyloid precursor protein in glia and activates glial cells in culture. Neurobiol Dis 14: 447-457 (2003).
7. Inestrosa NC, Alvarez A, Pèrez CA, Moreno RD, Vicente M, Linker C, et al. Acetylcholinesterase accelerates assembly of amyloid-β-peptides into Alzheimer's fibrils: possible role of the peripheral site of the enzyme. Neuron. 16: 881-891 (1996).
8. Harper JD and Lansbury PT Jr. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu Rev Biochem 66: 385-407 (1997).
9. Geula C and Mesulam M-M. Special properties of cholinesterases in the cerebral cortex of Alzheimer's disease. Brain Res 498: 185-189 (1989).
10. Alvarez A, Alarcón R, Opazo C, Campos EO, Muñoz FJ, Calderón FH et al. Stable complexes involving acetylcholinesterase and amyloid-β peptide change the biochemical properties of the enzyme and increase the neurotoxicity of Alzheimer's fibrils. J Neurosci 18: 3213-3223 (1998).
11. Sussman JL, Harel M, Frolow F, Oefner C, Goldman A, Toker L and Silman I. Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science. 253: 872-879 (1991).
12. De Ferrari GV, Canales MA, Shin I, Weiner LM, Silman I and Inestrosa NC. A structural motif of acetylcholinesterase that promotes amyloid β-peptide fibril formation. Biochemistry 40: 10447-10457 (2001).
13. Shin I, Silman I, Bon C and Weiner L. Liposome-catalyzed unfolding of acetylcholinesterase from Bungarus fasciatus. Biochemistry 37: 4310-4316 (1998).
14. Piazzi L, Rampa A, Bisi A, Gobbi S, Belluti F, Cavalli A, et al. 3-(4-[[Benzyl(methyl)amino]methyl]phenyl)-6, 7-dimethoxy-2H-2-chromenone (AP2238) inhibits both acetylcholinesterase and acetylcholinesterase-induced β-amyloid aggregation: a dual function lead for Alzheimer's disease therapy. J Med Chem 46: 2279-2282 (2003).
15. Savini L, Gaeta A, Fattorusso C, Catalanotti B, Campiani G, Chiasserini L, et al. Specific targeting of acetylcholinesterase and butyrylcholinesterase recognition sites. Rational design of novel, selective, and highly potent cholinesterase inhibitors. J Med Chem 46: 1-4 (2003).
16. Golabek AA, Soto C, Vogel T and Wisniewski T. The interaction between apolipoprotein E and Alzheimer's amyloid β-peptide is dependent on β-peptide conformation. J Biol Chem 271: 10602-10606 (1996).
17. Alvarez A, Alarcón R, Gonzalez A, Pérez-Acle T and Inestrosa C. Congo Red inhibits acetylcholinesterase binding to amyloid-β-peptide but not to the Aβ fibrils. J Mol Biol (In press) (2004).
18. Lorenzo A and Yankner BA. β-amyloid neurotoxicity requires fibril formation and is inhibited by congo red. Proc Natl Acad Sci U S A. 91: 12243-12247 (1994).
19. Alvarez A, Opazo C, Alarcón R, Garrido J and Inestrosa NC. Acetylcholinesterase promotes the aggregation of amyloid-β-peptide fragments by forming a complex with the growing fibrils. J Mol Biol. 272: 348-361 (1997).
20. Reyes AE, Chacón MA, Dinamarca MC, Cerpa W, Morgan C and Inestrosa NC. Acetylcholinesterase-Aβ complexes are more toxic than Aβ fibrils in rat hippocampus: Effect on rat β-amyloid aggregation, laminin expression, reactive astrocytosis and neuronal cell loss. Am J Pathol 164: 2163-2174 (2004).
21. Rees T, Hammond PI, Soreq H, Younkin S and Brimijoin S. Acetylcholinesterase promotes β-amyloid plaques in cerebral cortex. Neurobiol Aging 24: 777-787 (2003).
22. Morgan C, Bugueño MP, Garrido J and Inestrosa NC. Laminin affects polymerization, depolymerization and neurotoxicity of Aβ peptide. Peptides 23:1229-1240 (2002).
23. Bronfman FC, Tesseur I, Hofker MH, Havekens LM and Van Leuven F. No evidence for cholinergic problems in apolipoprotein E knockout and apolipoprotein E4 transgenic mice. Neuroscience 97: 411-418 (2000).
24. De Ferrari GV and Inestrosa NC. Wnt signaling function in Alzheimer's disease. Brain Res Brain Res Rev 33: 1-12 (2000).
25. Moon RT, Kohn AD, De Ferrari GV and Kaykas A. Wnt and β-catenin signaling: Diseases and Therapies. Nature Gen 5: 689-698 (2004).
26. Nelson WJ and Nusse R. Convergence of Wnt, β-Catenin, and Cadherin Pathways. Science 303: 1483-1486 (2004).
27. Inestrosa NC, Alvarez A, Godoy J, Reyes A, DeFerrasi GU. Acetylcholinesterase-amyloid-β-peptide interaction and Wnt signaling involvement in Aβ neurotoxicity. Acta Neurol Scand Suppl 2 176: 53-59 (2000).
28. Inestrosa NC, Urra S and Colombres M. Acetylcholinesterase-amyloid- β-peptide complexes in Alzheimer's Disease. The Wnt signaling pathway. Curr Alzheimer Res 1: 249-254 (2004).
29. De Ferrari GV, Chacón MA, Barría MI, Garrido JL, Godoy JA, Olivares G et al. Activation of Wnt signaling rescues neurodegeneration and behavioral impairments induced by β-amyloid fibrils. Molecular Psychiatry 8: 195-208 (2003).
30. Alvarez AR, Godoy JA, Mullendorff K, Olivares GH, Bronfman M and Inestrosa NC. Wnt-3a overcomes β-amyloid toxicity in rat hippocampal neurons. Exp Cell Res 297: 186-196 (2004).
31. Findeis MA, Musso GM, Arico-Muendel CC, Benjamin HW, Hundal AM, Lee JJ, et al. Modified-peptide inhibitors of amyloid-β-peptide polymerization. Biochemistry 38: 6791-800 (1999).