Cellular basis of Alzheimer's disease

Annals of Indian Academy of Neurology

Volumn 13, Issue SUPPL. 2, 2010, Pages

  Bali, Jitin ^a   Halima, Saoussen Ben ^a   Felmy, Boas ^a   Goodger, Zoe ^a   Zurbriggen, Sebastian ^a   Rajendran, Lawrence ^a  

^a UNIVERSITY OF ZURICH   (Switzerland)

Author keywords

secretase; Alzheimer's disease; amyloid; amyloid precursor protein; endocytosis; exosomes; secretase; trafficking

Indexed keywords

ADAM PROTEIN; ALPHA SECRETASE; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; BETA SECRETASE; BETA SECRETASE 1; BETA SECRETASE INHIBITOR; CALSENILIN; CD147 ANTIGEN; FLOTILLIN 1; GAMMA SECRETASE; MESSENGER RNA; PHOSPHOLIPASE D; PRESENILIN 1; PRESENILIN 2; ROSAPROSTOL; TAU PROTEIN; TUMOR NECROSIS FACTOR ALPHA CONVERTING ENZYME;

ALZHEIMER DISEASE; BRAIN DYSFUNCTION; CELL MIGRATION; COGNITION; CYTOLOGY; DOWN SYNDROME; ENZYME ACTIVITY; HUMAN; IMMUNOTHERAPY; MEMORY DISORDER; MICROTUBULE ASSEMBLY; NERVE DEGENERATION; NEUROFIBRILLARY TANGLE; PH; PRESENILE DEMENTIA; PROTEIN CLEAVAGE; PROTEIN DEGRADATION; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; REVIEW; RNA SPLICING; SENILE PLAQUE;

EID: 78650964118     PISSN: 09722327     EISSN: 19983549     Source Type: Journal    
DOI: 10.4103/0972-2327.74251     Document Type: Review

References (40)

1. Selkoe DJ. Alzheimer's disease: genes, proteins, and therapy. Physiol Rev 2001;81:741-66.
2. Blacker D, Wilcox MA, Laird NM, Rodes L, Horvath SM, Go RC, et al. Alpha-2 macroglobulin is genetically associated with Alzheimer disease. Nat Genet 1998;19:357-60.
3. Harold D, Abraham R, Hollingworth P, Sims R, Gerrish A, Hamshere ML, Pahwa JS, et al. Genome-wide association study identifies variants at CLU and PICALM associated with Alzheimer's disease. Nat Genet 2009;41:1088-93.
4. Kosik KS, Joachim CL, Selkoe DJ. Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease. Proc Natl Acad Sci USA 1986;83:4044-8.
5. Lee VM, Balin BJ, Otvos L Jr, Trojanowski JQ. A68: a major subunit of paired helical filaments and derivatized forms of normal Tau. (Translated from eng) Science 1991;251:675-8.
6. Cross D, Vial C, Maccioni RB. A tau-like protein interacts with stress fibers and microtubules in human and rodent cultured cell lines. (Translated from eng) J Cell Sci 1993;105:51-60.
7. Imahori K, Uchida T. Physiology and pathology of tau protein kinases in relation to Alzheimer's disease. J Biochem 1997;121:179-88.
8. Annaert W, De Strooper B. A cell biological perspective on Alzheimer's disease. Annu Rev Cell Dev Biol 2002;18:25-51.
9. Kang J, Muller-Hill B. Differential splicing of Alzheimer's disease amyloid A4 precursor RNA in rat tissues: PreA4 (695) mRNA is predominantly produced in rat and human brain. (Translated from eng) Biochem Biophys Res Commun 1990;166:1192-200.
10. Zheng H, Koo EH. The amyloid precursor protein: beyond amyloid. Mol Neurodegener 2006;1:5.
11. Lichtenthaler SF, Beher D, Grimm HS, Wang R, Shearman MS, Masters CL, et al. The intramembrane cleavage site of the amyloid precursor protein depends on the length of its transmembrane domain. Proc Natl Acad Sci USA 2002;99:1365-70.
12. Bertram L, Blacker D, Crystal A, Mullin K, Keeney D, Jones J, et al. Candidate genes showing no evidence for association or linkage with Alzheimer's disease using family-based methodologies. Exp Gerontol 2000;35:1353-61.
13. Weskamp G, Kratzschmar J, Reid MS, Blobel CP. MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains. J Cell Biol 1996;132:717-26.
14. Jorissen E, Prox J, Bernreuther C, Weber S, Schwanbeck R, Serneels L, et al. The disintegrin/metalloproteinase ADAM10 is essential for the establishment of the brain cortex. J Neurosci 2010;30:4833-44.
15. Vassar R, Bennett BD, Babu-Khan S, Kahn S, Mendiaz EA, Denis P, et al. Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science 1999;286:735-41.
16. Willem M, Garratt AN, Novak B, Citron M, Kaufmann S, Rittger A, et al. Control of peripheral nerve myelination by the beta-secretase BACE1. Science 2006;314:664-6.
17. Savonenko AV, Melnikova T, Laird FM, Stewart KA, Price DL, Wong PC. et al. Alteration of BACE1-dependent NRG1/ErbB4 signaling and schizophrenia-like phenotypes in BACE1-null mice. Proc Natl Acad Sci USA 2008;105:5585-90.
18. Haass C, Koo EH, Mellon A, Hung AY, Selkoe DJ. Targeting of cell-surface beta-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragments. Nature 1992;357:500-3.
19. Selkoe D, Kopan R. Notch and Presenilin: regulated intramembrane proteolysis links development and degeneration. Annu Rev Neurosci 2003;26:565-97.
20. Rajendran L, Simons K. Lipid rafts and membrane dynamics. J Cell Sci 2005;118:1099-102.
21. Cordy JM, Hussain I, Dingwall C, Hooper NM, Turner AJ. Exclusively targeting beta-secretase to lipid rafts by GPI-anchor addition up-regulates beta-site processing of the amyloid precursor protein. Proc Natl Acad Sci USA 2003;100:11735-40.
22. Ehehalt R, Keller P, Haass C, Thiele C, Simons K. Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts. J Cell Biol 2003;160:113-23.
23. Simons M, Keller P, Dichgans J, Schulz JB. Cholesterol and Alzheimer's disease: is there a link? Neurology 2001;57:1089-93.
24. Kojro E, Gimpl G, Lammich S, Marz W, Fahrenholz F. Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the alpha-secretase ADAM 10. Proc Natl Acad Sci USA 2001;98:5815-20.
25. Kalvodova L, Kahya N, Schwille P, Ehehalt R, Verkade P, Drechsel D, et al. Lipids as modulators of proteolytic activity of BACE: involvement of cholesterol, glycosphingolipids, and anionic phospholipids in vitro. J Biol Chem 2005;280:36815-23.
26. Schneider A, Rajendran L, Honsho M, Gralle M, Donnert G, Wouters F, et al. Flotillin-dependent clustering of the amyloid precursor protein regulates its endocytosis and amyloidogenic processing in neurons. J Neurosci 2008;28:2874-82.
27. Rajendran L. Flotillins are involved in the polarization of primitive and mature hematopoietic cells. PLoS One 2009;4:8290.
28. Rajendran L, Masilamani M, Solomon S, Tikkanen R, Stuermer CA, Plattner H, et al. Asymmetric localization of flotillins/reggies in preassembled platforms confers inherent polarity to hematopoietic cells. Proc Natl Acad Sci USA 2003;100:8241-6.
29. Rajendran L, Honsho M, Zahn TR, Keller P, Geiger KD, Verkade P, et al. Alzheimer's disease beta-amyloid peptides are released in association with exosomes. Proc Natl Acad Sci USA 2006;103:11172-7.
30. Kaether C, Schmitt S, Willem M, Haass C. Amyloid precursor protein and notch intracellular domains are generated after transport of their precursors to the cell surface. Traffic 2006;7:408-15.
31. Rajendran L, Knobloch M, Geiger KD, Dienel S, Nitsch R, Simons K, et al. Increased Abeta production leads to intracellular accumulation of Abeta in flotillin-1-positive endosomes. Neurodegener Dis 2007;4:164-70.
32. Pelchen-Matthews A, Raposo G, Marsh M. Endosomes, exosomes and Trojan viruses. Trends Microbiol 2004;12:310-6.
33. Fevrier B, Vilette D, Archer F, Loew D, Faigle W, Vidal M, et al. Cells release prions in association with exosomes. Proc Natl Acad Sci USA 2004;101:9683-8.
34. Aguzzi A, Rajendran L. The transcellular spread of cytosolic amyloids, prions, and prionoids. Neuron 2009;64:783-90.
35. Schenk D. Treatment of Alzheimer's disease: the beginning of a new era. Curr Alzheimer Res 2006;3:177.
36. Selkoe DJ, Schenk D. Alzheimer's disease: molecular understanding predicts amyloid-based therapeutics. Annu Rev Pharmacol Toxicol 2003;43:545-84.
37. Tung JS, Davis DL, Anderson JP, Walker DE, Mamo S, Jewett N, et al. Design of substrate-based inhibitors of human beta-secretase. J Med Chem 2002;45:259-62.
38. Hong L, Koelsch G, Lin X, Wu S, Terzyan S, Ghosh AK, et al. Structure of the protease domain of memapsin 2 (beta-secretase) complexed with inhibitor. Science 2000;290:150-3.
39. Rajendran L, et al. Efficient inhibition of the Alzheimer's disease beta-secretase by membrane targeting. Science 2008;320:520-3.
40. Adam G, Delbruck M. Reduction of dimensionality in biological diffusion processes. San Francisco: W. H. Freeman and Company; 1968. p. 198-215.