Alzheimer's and prion diseases: Distinct pathologies, common proteolytic denominators

Trends in Neurosciences

Volumn 25, Issue 12, 2002, Pages 616-620

  Checler, Frédéric ^a   Vincent, Bruno ^a  

^a INSTITUT DE PHARMACOLOGIE MOLÉCULAIRE ET CELLULAIRE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; CASPASE; DISINTEGRIN; ISOPROTEIN; PRION PROTEIN; PROTEIN KINASE C; PROTEIN PRECURSOR; PROTEINASE;

ALZHEIMER DISEASE; BIOSYNTHESIS; BRAIN; DEGENERATIVE DISEASE; ENZYME ACTIVITY; NONHUMAN; PATHOGENESIS; PATHOLOGY; PRION DISEASE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DEGRADATION; REVIEW; SOLUBILITY; TOXICITY;

ALZHEIMER DISEASE; AMYLOID BETA-PROTEIN PRECURSOR; ANIMALS; HUMANS; PRION DISEASES; PROTEIN KINASE C; PROTEIN PROCESSING, POST-TRANSLATIONAL; PRPC PROTEINS;

EID: 0036890486     PISSN: 01662236     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-2236(02)02263-4     Document Type: Review

References (80)

1. Ghetti B., et al. Prion protein amyloidosis. Brain Pathol. 6:1996;127-145.
2. Prusiner S.B. Prions. Proc. Natl. Acad. Sci. U. S. A. 95:1998;13363-13383.
3. Chesebro B. Prion protein and the transmissible spongiform encephalopathy diseases. Neuron. 24:1999;503-506.
4. Aguzzi A., et al. Prions: Health scare and biological challenge. Nat. Rev. Mol. Cell Biol. 2:2001;118-126.
5. Martins V.R., Brentani R.R. The biology of the cellular prion protein. Neurochem. Int. 1223:2002;1-3.
6. Tanzi R.E., et al. Molecular genetics of Alzheimer disease amyloid. J. Biol. Chem. 266:1991;20579-20582.
7. Hardy J., Duff K. Heterogeneity in Alzheimer's disease. Ann. Med. 25:1993;437-440.
8. Mullan M., Crawford F. Genetic and molecular advances in Alzheimer's disease. Trends Neurosci. 16:1993;398-403.
9. Schellenberg G.D. Genetic dissection of Alzheimer disease, a heterogeneous disorder. Proc. Natl. Acad. Sci. U. S. A. 92:1995;8552-8559.
10. Kang J., et al. The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature. 325:1987;733-736.
11. Tanzi R.E., et al. Amyloid β protein gene: cDNA, mRNA distribution, and genetic linkage near the Alzheimer locus. Science. 235:1987;880-884.
12. Goldgaber D., et al. Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease. Science. 235:1987;877-880.
13. Sherrington R., et al. Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature. 375:1995;754-760.
14. Levy-Lahad E., et al. Candidate gene for the chromosome 1 familial Alzheimer's disease locus. Science. 269:1995;973-977.
15. Rogaev E.I., et al. Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene. Nature. 376:1995;775-778.
16. Checler F. Processing of the β-amyloid precursor protein and its regulation in Alzheimer's disease. J. Neurochem. 65:1995;1431-1444.
17. Checler F. Presenilins: multifunctional proteins involved in Alzheimer's disease pathology. IUBMB Life. 48:1999;33-39.
18. Glatzel M., Aguzzi A. The shifting biology of prions. Brain Res. Rev. 36:2001;241-248.
19. Chiesa R., Harris D.A. Prion diseases: what is the neurotoxic molecule? Neurobiol. Dis. 8:2001;743-763.
20. Brown D.R. Prion and prejudice: normal protein and the synapse. Trends Neurosci. 24:2001;85-90.
21. Hardy J.A., Higgins G.A. Alzheimer's disease: the amyloid cascade hypothesis. Science. 256:1992;184-185.
22. Haass C., Selkoe D.J. Cellular processing of β-amyloid precursor protein and the genesis of amyloid β-peptide. Cell. 75:1993;1039-1042.
23. Sisodia S.S., Price D.L. Role of the β-amyloid protein in Alzheimer's disease. FASEB J. 9:1995;366-370.
24. Octave J.N. The amyloid peptide and its precursor in Alzheimer's disease. Rev. Neurosci. 6:1995;287-316.
25. Prusiner S. Molecular biology and pathogenesis of prion diseases. Trends Biochem. Sci. 21:1996;482-487.
26. Small D.H., McLean C.A. Alzheimer's disease and the amyloid β protein: what is the role of amyloid? J. Neurochem. 73:1999;443-449.
27. Forloni G., et al. Neurotoxicity of a prion protein fragment. Nature. 362:1993;543-546.
28. Yankner B.A., et al. Neurotoxicity of a fragment of the amyloid precursor associated with Alzheimer's disease. Science. 245:1989;417-420.
29. Frautschy S.A., et al. Effects of injected Alzheimer β-amyloid cores in rat brain. Proc. Natl. Acad. Sci. U. S. A. 88:1991;8362-8366.
30. Pike C.J., et al. In vitro aging of β-amyloid protein causes peptide aggregation and neurotoxicity. Brain Res. 563:1991;311-314.
31. Brown D.R. Prion protein peptides: optimal toxicity and peptide blockade of toxicity. Mol. Cell. Neurosci. 15:2000;66-78.
32. Loo D.T., et al. Apoptosis is induced by β-amyloid in cultured central nervous system neurons. Proc. Natl. Acad. Sci. U. S. A. 90:1993;7951-7955.
33. Burkle A., et al. Poly(ADP-ribose) immunostaining to detect apoptosis induced by a neurotoxic fragment of prion protein. Histochem. J. 3:1999;1711-1716.
34. Ettaiche M., et al. In vivo cytotoxicity of the prion protein fragment 106-126. J. Biol. Chem. 275:2000;36487-36490.
35. Daniels M., et al. Toxicity of novel C-terminal prion protein fragments and peptides harbouring disease-related C-terminal mutations. Eur. J. Biochem. 268:2001;6155-6164.
36. Harada J., Sugimoto M. Activation of caspase in β-amyloid-induced apoptosis of cultured rat cortical neurons. Brain Res. 842:1999;311-323.
37. Sàez-Valero J., et al. Caspase-3 activation by β-amyloid and prion protein peptides is independent from their neurotoxic effect. Neurosci. Lett. 293:2000;207-210.
38. Allen J.W., et al. Multiple caspases are involved in β-amyloid-induced neuronal apoptosis. J. Neurosci. Res. 65:2001;45-53.
39. White A.R., et al. Sublethal concentrations of prion peptide PrP106-126 or the amyloid β peptide of Alzheimer's disease activates expression of proapoptotic markers in primary cortical neurons. Neurobiol. Dis. 8:2001;299-316.
40. Cardoso, S.M. et al. (2001) Functional mitochondria are required for amyloid β-mediated neurotoxicity, FASEB J., 1439-1441.
41. Ivins K.J., et al. Neuronal apoptosis induced by β-amyloid is mediated by caspase-8. Neurobiol. Dis. 6:1999;440-449.
42. Rohn T.T., et al. Activation of caspase 8 in the Alzheimer's disease brain. Neurobiol. Dis. 8:2001;1006-1016.
43. O'Donovan C.N., et al. Prion protein fragment PrP-(106-126) induces apoptosis via mitochondrial disruption in human neuronal SH-SY5Y cells. J. Biol. Chem. 276:2001;43516-43523.
44. Brown D.R., et al. PrP and β-amyloid fragments activate different neurotoxic mechanisms in cultured mouse cells. Eur. J. Neurosci. 9:1997;1162-1169.
45. Zanusso G., et al. Proteasomal degradation and N-terminal protease resistance of the codon 145 mutant prion protein. J. Biol. Chem. 274:1999;23396-23404.
46. Yedidia Y., et al. Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein. EMBO J. 20:2001;5383-5391.
47. Nunan J., et al. The C-terminal fragment of the Alzheimer's disease amyloid protein precursor is degraded by a proteasome-dependent mechanism distinct from gamma-secretase. Eur. J. Biochem. 268:2001;5329-5336.
48. Suh Y-H., Checler F. Amyloid precursor protein, presenilins and α-synuclein: Molecular pathogenesis and pharmacological applications in Alzheimer's disease. Pharmacol. Rev. 54:2002;469-525.
49. Vassar R., Citron M. Aβ-generating enzymes: recent advances in β- and γ-secretases research. Neuron. 27:2000;419-422.
50. Dominguez D.I., et al. Secretases as therapeutic targets for the treatment of Alzheimer's disease. Amyloid: J. Prot. Folding Disord. 8:2000;124-142.
51. Wolfe M.S. Secretase targets for Alzheimer's disease: identification and therapeutic potential. J. Med. Chem. 44:2001;2039-2060.
52. Xia W. Amyloid metabolism and secretases in Alzheimer's disease. Curr. Neurol. Neurosci. LA Rep. 1:2001;422-427.
53. Hooper N.M., Turner A.J. The search for α-secretase and its potential as a therapeutic approach to Alzheimer's disease. Curr. Med. Chem. 9:2002;1107-1119.
54. Selkoe D.J. Normal and abnormal biology of the β-amyloid precursor protein. Annu. Rev. Neurosci. 17:1994;489-517.
55. Mattson M.P. Cellular actions of β-amyloid precursor protein and its soluble and fibrillogenic derivatives. Physiol. Rev. 77:1997;1081-1132.
56. Gandy S., Greengard P. Regulated cleavage of the Alzheimer amyloid precursor protein: Molecular and cellular basis. Biochimie. 76:1994;300-303.
57. Nitsch R.M. From acetylcholine to amyloid: neurotransmitters and the pathology of Alzheimer's diseases. Neurodegeneration. 5:1996;477-482.
58. Greenfield J.P., et al. Cellular and molecular basis of β-amyloid precursor protein metabolism. Front. Biosci. 5:2000;72-83.
59. Turner A.J., Hooper N. Role for ADAM-family proteinases as membrane protein secretases. Biochem. Soc. Trans. 27:1999;255-259.
60. Lammich S., et al. Constitutive and regulated α-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease. Proc. Natl. Acad. Sci. U. S. A. 96:1999;3922-3927.
61. Lopez-Perez E., et al. Constitutive α-secretase cleavage of the β-amyloid precursor protein in the furin-deficient LoVo cell line: involvement of the prohormone convertase 7 (PC7) and the disintegrin metalloprotease ADAM10. J. Neurochem. 76:2001;1532-1539.
62. Anders A., et al. Regulation of the α-secretase ADAM10 by its prodomain and proprotein convertase. FASEB J. 15:2001;1837-1839.
63. Marcinkiewicz M., Seidah N.G. Coordinated expression of β-amyloid precursor protein and the putative β-secretase BACE and α-secretase ADAM10 in mouse and human brain. J. Neurochem. 75:2000;2133-2143.
64. Buxbaum J.D., et al. Evidence that tumor necrosis factor α converting enzyme is involved in regulated α-secretase cleavage of the Alzheimer amyloid protein precursor. J. Biol. Chem. 273:1998;27765-27767.
65. Lopez-Perez E., et al. A proprotein convertase activity contributes to the processing of the Alzheimer's β-amyloid precursor protein in human cells: evidence for a role of the prohormone convertase PC7 in the constitutive α-secretase pathway. J. Neurochem. 73:1999;2056-2062.
66. Harris D.A., et al. Processing of a cellular prion protein: identification of N- and C-terminal cleavage sites. Biochemistry. 32:1993;1009-1016.
67. Chen S.G., et al. Truncated forms of the human prion protein in normal brain and in prion disease. J. Biol. Chem. 270:1995;19173-19180.
68. Jiménez-Huete A., et al. Endogenous proteolytic cleavage of normal and disease-associated isoforms of the human prion protein in neural and non neural tissues. Am. J. Pathol. 153:1998;1561-1572.
69. Vincent B., et al. Phorbol ester-regulated cleavage of normal prion protein in HEK293 human cells and murine neurons. J. Biol. Chem. 275:2000;35612-35616.
70. Parizek P., et al. Similar turnover and shedding of the cellular prion protein in primary lymphoid and neuronal cells. J. Biol. Chem. 276:2001;44627-44632.
71. Vincent B., et al. The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol-esters-regulated normal cleavage of the cellular prion protein. J. Biol. Chem. 276:2001;37743-37746.
72. Sisodia S. b-amyloid precursor protein cleavage by a membrane-bound protease. Proc. Natl. Acad. Sci. U. S. A. 89:1992;6075-6079.
73. Vassar R. The β-secretase, BACE. J. Mol. Neurosci. 17:2001;157-170.
74. Büeler H., et al. Mice devoid of PrP are resistant to scrapie. Cell. 73:1993;1339-1347.
75. Brandner S., et al. Normal host prion protein necessary for scrapie-induced neurotoxicity. Nature. 379:1996;339-343.
76. Borchardt T., et al. Copper inhibits β-amyloid production and stimulates the non-amyloidogenic pathway of amyloid-precursor-protein secretion. Biochem. J. 344:1999;461-467.
77. Cai H., et al. BACE1 is the major β-secretase for generation of Aβ peptides by neurons. Nat. Neurosci. 4:2001;233-234.
78. Price D.L., et al. Alzheimer disease and the prion disorders amyloid β-protein and prion protein amyloidoses. Proc. Natl. Acad. Sci. U. S. A. 90:1993;6381-6384.
79. Bucclantini M., et al. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature. 416:2002;507-511.
80. Bence N.F., et al. Impairment of the ubiquitin-proteasome system by protein aggregation. Science. 292:2001;1552-1555.