Bile acids and apoptosis modulation: an emerging role in experimental Alzheimer's disease

Trends in Molecular Medicine

Volumn 14, Issue 2, 2008, Pages 54-62

  Ramalho, Rita M ^a   Viana, Ricardo J S ^a   Low, Walter C ^b   Steer, Clifford J ^b   Rodrigues, Cecília M P ^a  

^a RESEARCH INSTITUTE FOR MEDICINES IMED ULISBOA   (Portugal)

^b UNIVERSITY OF MINNESOTA MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE; CELL CYCLE PROTEIN; CYTOCHROME C; PROTEIN BAX; TAUROURSODEOXYCHOLIC ACID; URSODEOXYCHOLIC ACID;

ALZHEIMER DISEASE; APOPTOSIS; ARTICLE; BILIARY CIRRHOSIS; DISEASE MODEL; DRUG EFFECT; DRUG MECHANISM; ENZYME ACTIVATION; ENZYME RELEASE; HUMAN; MITOCHONDRIAL MEMBRANE; NONHUMAN; PROTEIN FUNCTION; PROTEIN TRANSPORT; TRANSCRIPTION REGULATION;

ALZHEIMER DISEASE; ANIMALS; APOPTOSIS; BILE ACIDS AND SALTS; CELL CYCLE PROTEINS; HUMANS; MODELS, BIOLOGICAL; TAUROCHENODEOXYCHOLIC ACID; URSODEOXYCHOLIC ACID;

EID: 39149099114     PISSN: 14714914     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molmed.2007.12.001     Document Type: Article

References (65)

1. Ferri C.P., et al. Global prevalence of dementia: a Delphi consensus study. Lancet 366 (2005) 2112-2117
2. Goate A., et al. Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease. Nature 349 (1991) 704-706
3. Vassar R., et al. Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science 286 (1999) 735-741
4. Hardy J., and Selkoe D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297 (2002) 353-356
5. Binder L.I., et al. The distribution of tau in the mammalian central nervous system. J. Cell Biol. 101 (1985) 1371-1378
6. Gamblin T.C., et al. Caspase cleavage of tau: linking amyloid and neurofibrillary tangles in Alzheimer's disease. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 10032-10037
7. Rissman R.A., et al. Caspase-cleavage of tau is an early event in Alzheimer disease tangle pathology. J. Clin. Invest. 114 (2004) 121-130
8. Kerr J.F., et al. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer 26 (1972) 239-257
9. Ricci J.E., et al. Caspase-mediated loss of mitochondrial function and generation of reactive oxygen species during apoptosis. J. Cell Biol. 160 (2003) 65-75
10. Li P., et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91 (1997) 479-489
11. Baud V., and Karin M. Signal transduction by tumor necrosis factor and its relatives. Trends Cell Biol. 11 (2001) 372-377
12. Loo D.T., et al. Apoptosis is induced by beta-amyloid in cultured central nervous system neurons. Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 7951-7955
13. Colurso G.J., et al. Quantitative assessment of DNA fragmentation and beta-amyloid deposition in insular cortex and midfrontal gyrus from patients with Alzheimer's disease. Life Sci. 73 (2003) 1795-1803
14. Martinez-Vicente M., et al. Autophagy and neurodegeneration: when the cleaning crew goes on strike. Lancet Neurol. 6 (2007) 352-361
15. Syntichaki P., and Tavernarakis N. The biochemistry of neuronal necrosis: rogue biology?. Nat. Rev. Neurosci. 4 (2003) 672-684
16. Su J.H., et al. Bax protein expression is increased in Alzheimer's brain: correlations with DNA damage, Bcl-2 expression, and brain pathology. J. Neuropathol. Exp. Neurol. 56 (1997) 86-93
17. Anderson A.J., et al. DNA damage and apoptosis in Alzheimer's disease: colocalization with c-Jun immunoreactivity, relationship to brain area, and effect of postmortem delay. J. Neurosci. 16 (1996) 1710-1719
18. Takuma K., et al. ABAD enhances Aβ-induced cell stress via mitochondrial dysfunction. FASEB J. 19 (2005) 597-598
19. Pereira C., et al. Cell degeneration induced by amyloid-beta peptides: implications for Alzheimer's disease. J. Mol. Neurosci. 23 (2004) 97-104
20. Casley C.S., et al. Beta-amyloid inhibits integrated mitochondrial respiration and key enzyme activities. J. Neurochem. 80 (2002) 91-100
21. Cecarini V., et al. Oxidative inactivation of the proteasome in Alzheimer's disease. Free Radic. Res. 41 (2007) 673-680
22. Parihar M.S., and Brewer G.J. Mitoenergetic failure in Alzheimer disease. Am. J. Physiol. Cell Physiol. 292 (2007) C8-C23
23. Moreira P.I., et al. The key role of mitochondria in Alzheimer's disease. J. Alzheimers Dis. 9 (2006) 101-110
24. Ray S., et al. Classification and prediction of clinical Alzheimer's diagnosis based on plasma signaling proteins. Nat. Med. 13 (2007) 1359-1362
25. Su J.H., et al. Activated caspase-3 expression in Alzheimer's and aged control brain: correlation with Alzheimer pathology. Brain Res. 898 (2001) 350-357
26. Guo H., et al. Active caspase-6 and caspase-6-cleaved tau in neuropil threads, neuritic plaques, and neurofibrillary tangles in Alzheimer's disease. Am. J. Pathol. 165 (2004) 523-531
27. Ramalho R.M., et al. Tauroursodeoxycholic acid modulates p53-mediated apoptosis in Alzheimer's disease mutant neuroblastoma cells. J. Neurochem. 98 (2006) 1610-1618
28. Lu D.C., et al. A second cytotoxic proteolytic peptide derived from amyloid beta-protein precursor. Nat. Med. 6 (2000) 397-404
29. Dumanchin-Njock C., et al. The caspase-derived C-terminal fragment of betaAPP induces caspase-independent toxicity and triggers selective increase of Aβ42 in mammalian cells. J. Neurochem. 78 (2001) 1153-1161
30. Park D.S., et al. Cyclin-dependent kinases participate in death of neurons evoked by DNA-damaging agents. J. Cell Biol. 143 (1998) 457-467
31. Phillips A.C., and Vousden K.H. E2F-1 apoptosis. Apoptosis 6 (2001) 173-182
32. Ramalho R.M., et al. Inhibition of the E2F-1/p53/Bax pathway by tauroursodeoxycholic acid in amyloid beta-peptide-induced apoptosis of PC12 cells. J. Neurochem. 90 (2004) 567-575
33. Morrison R.S., et al. p53-dependent cell death signaling in neurons. Neurochem. Res. 28 (2003) 15-27
34. Ohyagi Y., et al. Intracellular Aβ42 activates p53 promoter: a pathway to neurodegeneration in Alzheimer's disease. FASEB J. 19 (2005) 255-257
35. Culmsee C., et al. A synthetic inhibitor of p53 protects neurons against death induced by ischemic and excitotoxic insults, and amyloid beta-peptide. J. Neurochem. 77 (2001) 220-228
36. Hooper C., et al. p53 is upregulated in Alzheimer's disease and induces tau phosphorylation in HEK293a cells. Neurosci. Lett. 418 (2007) 34-37
37. Alves da Costa C., et al. Presenilin-dependent gamma-secretase-mediated control of p53-associated cell death in Alzheimer's disease. J. Neurosci. 26 (2006) 6377-6385
38. Lazaridis K.N., et al. Ursodeoxycholic acid 'mechanisms of action and clinical use in hepatobiliary disorders'. J. Hepatol. 35 (2001) 134-146
39. Paumgartner G., and Beuers U. Mechanisms of action and therapeutic efficacy of ursodeoxycholic acid in cholestatic liver disease. Clin. Liver Dis. 8 (2004) 67-81
40. Rodrigues C.M.P., and Steer C.J. Mitochondrial membrane perturbations in cholestasis. J. Hepatol. 32 (2000) 135-141
41. Rodrigues C.M.P., et al. Ursodeoxycholic acid may inhibit deoxycholic acid-induced apoptosis by modulating mitochondrial transmembrane potential and reactive oxygen species production. Mol. Med. 4 (1998) 165-178
42. Rodrigues C.M.P., et al. A novel role for ursodeoxycholic acid in inhibiting apoptosis by modulating mitochondrial membrane perturbation. J. Clin. Invest. 101 (1998) 2790-2799
43. Rodrigues C.M.P., et al. Ursodeoxycholic acid prevents cytochrome c release in apoptosis by inhibiting mitochondrial membrane depolarization and channel formation. Cell Death Differ. 6 (1999) 842-854
44. Azzaroli F., et al. Ursodeoxycholic acid diminishes Fas-ligand-induced apoptosis in mouse hepatocytes. Hepatology 36 (2002) 49-54
45. Castro R.E., et al. A distinct microarray gene expression profile in primary rat hepatocytes incubated with ursodeoxycholic acid. J. Hepatol. 42 (2005) 897-906
46. 1-induced apoptosis of rat hepatocytes. J. Biol. Chem. 278 (2003) 48831-48838
47. Castro R.E., et al. Differential regulation of cyclin D1 and cell death by bile acids in primary rat hepatocytes. Am. J. Physiol. Gastrointest. Liver Physiol. 293 (2007) G327-G334
48. 1-induced apoptosis in rat hepatocytes. Hepatology 42 (2005) 925-934
49. Solá S., et al. Functional modulation of nuclear steroid receptors by tauroursodeoxycholic acid reduces amyloid beta-peptide-induced apoptosis. Mol. Endocrinol. 20 (2006) 2292-2303
50. Bradham C.A., et al. Mechanisms of hepatic toxicity. I. TNF-induced liver injury. Am. J. Physiol. 275 (1998) G387-G392
51. Schoemaker M.H., et al. Tauroursodeoxycholic acid protects rat hepatocytes from bile acid-induced apoptosis via activation of survival pathways. Hepatology 39 (2004) 1563-1573
52. Mattson M.P. Neuronal life-and-death signaling, apoptosis, and neurodegenerative disorders. Antioxid. Redox Signal. 8 (2006) 1997-2006
53. Keene C.D., et al. A bile acid protects against motor and cognitive deficits and reduces striatal degeneration in the 3-nitropropionic acid model of Huntington's disease. Exp. Neurol. 171 (2001) 351-360
54. Rodrigues C.M.P., et al. Tauroursodeoxycholic acid partially prevents apoptosis induced by 3-nitropropionic acid: evidence for a mitochondrial pathway independent of the permeability transition. J. Neurochem. 75 (2000) 2368-2379
55. Solá S., et al. Tauroursodeoxycholic acid prevents amyloid-beta peptide-induced neuronal death via a phosphatidylinositol 3-kinase-dependent signaling pathway. Mol. Med. 9 (2003) 226-234
56. Keene C.D., et al. Tauroursodeoxycholic acid, a bile acid, is neuroprotective in a transgenic animal model of Huntington's disease. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 10671-10676
57. Duan W.M., et al. Tauroursodeoxycholic acid improves the survival and function of nigral transplants in a rat model of Parkinson's disease. Cell Transplant. 11 (2002) 195-205
58. Ved R., et al. Similar patterns of mitochondrial vulnerability and rescue induced by genetic modification of alpha-synuclein, parkin, and DJ-1 in Caenorhabditis elegans. J. Biol. Chem. 280 (2005) 42655-42668
59. Rodrigues C.M.P., et al. Neuroprotection by a bile acid in an acute stroke model in the rat. J. Cereb. Blood Flow Metab. 22 (2002) 463-471
60. Rodrigues C.M.P., et al. Tauroursodeoxycholic acid reduces apoptosis and protects against neurological injury after acute hemorrhagic stroke in rats. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 6087-6092
61. Castro R.E., et al. The bile acid tauroursodeoxycholic acid modulates phosphorylation and translocation of bad via phosphatidylinositol 3-kinase in glutamate-induced apoptosis of rat cortical neurons. J. Pharmacol. Exp. Ther. 311 (2004) 845-852
62. Rodrigues C.M.P., et al. Bilirubin and amyloid-beta peptide induce cytochrome c release through mitochondrial membrane permeabilization. Mol. Med. 6 (2000) 936-946
63. Rodrigues C.M.P., et al. Amyloid beta-peptide disrupts mitochondrial membrane lipid and protein structure: protective role of tauroursodeoxycholate. Biochem. Biophys. Res. Commun. 281 (2001) 468-474
64. Amaral J.D., et al. p53 is a key molecular target of ursodeoxycholic acid in regulating apoptosis. J. Biol. Chem. 282 (2007) 34250-34259
65. Troy C.M., et al. Caspase-2 mediates neuronal cell death induced by beta-amyloid. J. Neurosci. 20 (2000) 1386-1392