Mechanisms of cerebrovascular amyloid deposition. Lessons from mouse models

Annals of the New York Academy of Sciences

Volumn 903, Issue , 2000, Pages 307-316

  Burgermeister, Patrick ^a   Calhoun, Michael E ^a   Winkler, David T ^a   Jucker, Mathias ^a  

^a UNIVERSITY OF BASEL   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN;

ALZHEIMER DISEASE; ANIMAL EXPERIMENT; ANIMAL MODEL; BRAIN BLOOD VESSEL; CONFERENCE PAPER; GENE MUTATION; MOUSE; NONHUMAN; TRANSGENIC MOUSE; VASCULAR AMYLOIDOSIS;

ANIMALIA; MUS MUSCULUS;

EID: 0034020399     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2000.tb06381.x     Document Type: Conference Paper

References (65)

1. 1. VINTERS, H.V. 1987. Cerebral amyloid angiopathy. A critical review. Stroke 18: 311-324.
2. 2. YAMADA, M. et al. 1987. Cerebral amyloid angiopathy in the aged. J. Neurol. 234: 371-376.
3. 3. KALARIA, R.N. 1996. Cerebral vessels in ageing and Alzheimer's disease. Pharmacol. Ther. 72: 193-214.
4. 4. VONSATTEL, J.P. et al. 1991. Cerebral amyloid angiopathy without and with cerebral hemorrhages: a comparative histological study. Ann. Neurol. 30: 637-649.
5. 5. ITOH, Y. et al. 1993. Cerebral amyloid angiopathy: a significant cause of cerebellar as well as lobar cerebral hemorrhage in the elderly. J. Neurol. Sci. 116: 135-141.
6. 6. LEVY, E. et al. 1990. Mutation of the Alzheimer's disease amyloid gene in hereditary cerebral hemorrhage, Dutch type. Science 248: 1124-1126.
7. 7. GHISO, J. et al. 1986. Amyloid fibrils in hereditary cerebral hemorrhage with amyloidosis of Icelandic type is a variant of γ-trace basic protein (cystatin C). Proc. Natl. Acad. Sci. USA 83: 2974-2978.
8. 8. ABRAHAMSON, M. et al. 1990. Structure and expression of the human cystatin C gene. Biochem. J. 268: 287-294.
9. 9. VIDAL, R. et al. 1999. A stop-codon mutation in the BRI gene associated with familial British dementia. Nature 399: 776-781.
10. 10. HALTIA, M. et al. 1990. Amyloid in familial amyloidosis, Finnish type, is antigenically and structurally related to gelsolin. Am. J. Pathol. 136: 1223-1228.
11. 11. KIURU, S. et al. 1999. Gelsolin-related spinal and cerebral amyloid angiopathy. Ann. Neurol. 45: 305-311.
12. 12. PETERSEN, R.B. et al. 1997. Transthyretin amyloidosis: a new mutation associated with dementia. Ann. Neurol. 41: 307-313.
13. 13. VIDAL, R. et al. 1996. Meningocerebrovascular amyloidosis associated with a novel transthyretin mis-sense mutation at codon 18 (TTRD186). Am. J. Pathol. 148: 361-366.
14. 14. GHETTI, B. et al. 1996. Vascular variant of prion protein cerebral amyloidosis with tau-positive neurofibrillary tangles: the phenotype of the stop codon 145 mutation in PRNP. Proc. Natl. Acad. Sci. USA 93: 744-748.
15. 15. SELKOE, D.J. 1994. Normal and abnormal biology of the β-amyloid precursor protein. Annu. Rev. Neurosci. 17: 489-517.
16. 16. RAEBER, A.J. et al. 1998. Transgenic and knockout mice in research on prion diseases. Brain Pathol. 8: 715-733.
17. 17. GARDELLA, J.E. et al. 1992. Characterization of Alzheimer amyloid precursor protein transcripts in platelets and megakarocytes. Neurosci. Lett. 138: 229-232.
18. 18. SEUBERT, P. et al. 1992. Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids. Nature 359: 325-327.
19. 19. IDA, N. et al. 1996. Analysis of heterogeneous βA4 peptides in human cerebrospinal fluid and blood by a newly developed sensitive Western blot assay. J. Biol. Chem. 271: 22908-22914.
20. 20. SCHEUNER, D. et al. 1996. Secreted amyloid β-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease. Nature Med. 2: 864-870.
21. 21. THOMAS, T. et al. 1997. In vivo vascular damage, leukocyte activation and inflammatory response induced by β-amyloid. J. Submicrosc. Cytol. Pathol. 29: 293-304.
22. 22. VERBEEK, M.M. et al. 1998. Distribution of A beta-associated proteins in cerebrovascular amyloid of Alzheimer's disease. Acta Neuropathol. (Berl.) 96: 628-636.
23. 1-40 labels amyloid deposits in the aged primate brain in vivo. Neuroreport 7: 2607-2611.
24. 24. MACKIC, J.B. et al. 1998. Cerebrovascular accumulation and increased blood-brain barrier permeability to circulating Alzheimer's amyloid beta peptide in aged squirrel monkey with cerebral amyloid angiopathy. J. Neurochem. 70: 210-215.
25. 25. PODUSLO, J.F. et al. 1997. Permeability and residual plasma volume of human, Dutch variant, and rat amyloid β-protein 1-40 at the blood-brain barrier. Neurobiol. Dis. 4: 27-34.
26. 1-40. J. Clin. Invest. 102: 734-743.
27. 27. SCHRÖDER, R. & R.p. LINKE. 1999. Cerebrovascular involvement in systemic AA and AL amyloidosis: a clear haematogenic pattern. Virchows Arch. 434: 551-560.
28. 28. KUO, Y.M. et al. 1999. High levels of circulating Aβ42 are sequestered by plasma proteins in Alzheimer's disease. Biochem. Biophys. Res. Commun. 257: 787-791.
29. 29. SHAYO, M. et al. 1997. The putative blood-brain barrier transporter for the beta-amyloid binding protein apolipoprotein J is saturated at physiological concentrations. Life Sci. 60: 115-118.
30. 30. YAMAGUCHI, H. et al. 1992. Beta amyloid is focally deposited within the outer basement membrane in the amyloid angiopathy of Alzheimer's disease. An immunoelectron microscopic study. Am. J. Pathol. 141: 249-259.
31. 31. WELLER, R.O. et al. 1998. Cerebral amyloid angiopathy: Amyloid β accumulates in putative interstitial fluid drainage pathways in Alzheimer's disease. Am. J. Pathol. 153: 725-733.
32. 32. TIAN, M. et al. 1996. Dystroglycan in the cerebellum is a laminin α2-chain binding protein at the glial-vascular interface and is expressed in Purkinje cells. Eur. J. Neurosci. 8: 2739-2747.
33. 33. KALARIA, R.N. et al. 1996. Production and increased detection of amyloid β protein and amyloidogenic fragments in brain microvessels, meningeal vessels and choroid plexus in Alzheimer's disease. Brain Res. Mol. Brain Res. 35: 58-68.
34. 34. VERBEEK, M.M. et al. 1997. Rapid degeneration of cultured human brain pericytes by amyloid β protein. J. Neurochem. 68: 1135-1141.
35. 35. WISNIEWSKI, H.M. & J. WEGIEL. 1994. β-amyloid formation by myocytes of leptomeningeal vessels. Acta Neuropathol. 87: 233-241.
36. 36. NATTE, R. et al. 1999. Amyloid β precursor protein-mRNA is expressed throughout cerebral vessel walls. Brain Res. 828: 179-183.
37. 37. KAWAI, M. et al. 1993. Degeneration of vascular muscle cells in cerebral amyloid angiopathy of Alzheimer disease. Brain Res. 623: 142-146.
38. 38. WISNIEWSKI, H.M. et al. 1994. Vascular β-amyloid in Alzheimer's disease angiopathy is produced by proliferating and degenerating smooth muscle cells. Amyloid: Int. J. Exp. Clin. Invest. 1: 8-16.
39. 39. DAVIS-SALINAS, J. et al. 1995. Amyloid β-protein induces its own production in cultured degenerating cerebrovascular smooth muscle cells. J. Neurochem. 65: 931-934.
40. 40. VAN NOSTRAND, W.E. et al. 1998. Pathologic amyloid β-protein cell surface fibril assembly on cultured human cerebrovascular smooth muscle cells. J. Neurochem. 70: 216-223.
41. 41. SHINKAI, Y. et al. 1995. Amyloid β-proteins 1-40 and 1-42(43) in the soluble fraction of extra-and intracranial blood vessels. Ann. Neurol. 38: 421-428.
42. 42. VAN NOSTRAND, W.E. et al. 1994. Amyloid β-protein precursor in cultured leptomeningeal smooth muscle cells. Amyloid: Int. J. Exp. Clin. Invest. 1: 1-7.
43. 43. PRELLI, F. et al. 1988. Differences between vascular and plaque core amyloid in Alzheimer's disease. Neurochemistry 51: 648-651.
44. 44. ROHER, A.E. et al. 1993. β-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer disease. Proc. Natl. Acad. Sci. USA 90: 10836-10840.
45. 45. VERBEEK, M.M. et al. 1997. Differences between the pathogenesis of senile plaques and congophilic angiopathy in Alzheimer disease. J. Neuropathol. Exp. Neurol. 56: 751-761.
46. 46. WALKER, L.C. 1997. Animal models of cerebral β-amyloid angiopathy. Brain Res. Brain Res. Rev. 25: 70-84.
47. 47. WEI, L.H. et al. 1996. Cystatin C: Iceland-like mutation in an animal model of cerebrovascular β-amyloidosis. Stroke 27: 2080-2085.
48. 48. GAMES, D. et al. 1995. Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein. Nature 373: 523-527.
49. 49. ROCKENSTEIN, E.M. et al. 1995. Levels and alternative splicing of amyloid β protein precursor (APP) transcripts in brains of APP transgenic mice and humans with Alzheimer's disease. J. Biol. Chem. 47: 28257-28267.
50. 42 deposition in a transgenic mouse model of Alzheimer disease. Proc. Natl. Acad. Sci. USA 94: 1550-1555.
51. 51. HSIA, A.Y. et al. 1999. Plaque-independent disruption of neural circuits in Alzheimer's disease mouse models. Proc. Natl. Acad. Sci. USA 96: 3228-3233.
52. 52. WYSS-CORAY, T. et al. 1997. Amyloidogenic role of cytokine TGF-β1 in transgenic mice and in Alzheimer's disease. Nature 389: 603-606.
53. 53. SNOW, A.D. et al. 1994. An important role of heparan sulfate proteoglycan (perlecan) in a model system for the deposition and persistence of fibrillar Aβ-amyloid in rat brain. Neuron 12: 219-234.
54. 54. NARINDRASORASAK, S. et al. 1995. An interaction between the basement membrane and Alzheimer precursor proteins suggests a role in the pathogenesis of Alzheimer's disease. Lab. Invest. 72: 272-282.
55. 55. WYSS-CORAY, T. et al. 1995. Increased central nervous system production of extracellular matrix components and development of hydrocephalus in transgenic mice overexpressing transforming growth factor β1. Am. J. Pathol. 147: 53-67.
56. 56. HSIAO, K. et al. 1996. Correlative memory deficits, Aβ elevation, and amyloid plaques in transgenic mice. Science 274: 99-102.
57. 57. STÜRCHLER-PIERRAT, C. et al. 1997. Two amyloid precursor protein transgenic mouse models with Alzheimer disease-like pathology. Proc. Natl. Acad. Sci. USA 94: 13287-13292.
58. 58. WALKER, L.C. et al. 1999. Cerebrovascular amyloidosis: experimental analysis in vitro and in vivo. Histol. Histopathol. 14: 827-837.
59. 59. CALHOUN, M.E. et al. 1999. Neuronal overexpression of mutant amyloid precursor protein results in prominent deposition of cerebrovascular amyloid. Proc. Natl. Acad. Sci. USA 96: 14088-14093.
60. 60. KAWARABAYASHI, T. et al. 1996. Accumulation of beta-amyloid fibrils in pancreas of transgenic mice. Neurobiol. Aging 17: 215-222.
61. 61. FUKUCHI, K. et al. 1996. High levels of circulating β-amyloid peptide do not cause cerebral β-amyloidosis in transgenic mice. Am. J. Pathol. 149: 219-227.
62. 62. NAKAMURA, T. et al. 1994. Amyloid β protein levels in cerebrospinal fluid are elevated in early-onset alzheimer's disease. Ann. Neurol. 36: 903-911.
63. 63. NITSCH, R.M. et al. 1995. Cerebrospinal fluid levels of amyloid β-protein in Alzheimer's disease: inverse correlation with severity of dementia and effect of apolipoprotein E genotype. Ann. Neurol. 37: 512-518.
64. 64. WELLER, R.O. 1998. Pathology of cerebrospinal fluid and interstitial fluid of the CNS: significance for Alzheimer disease, prion disorders and multiple sclerosis. J. Neuropathol. Exp. Neurol. 57: 885-894.
65. 65. URMONEIT, B. et al. 1997. Cerebrovascular smooth muscle cells internalize Alzheimer amyloid beta protein via a lipoprotein pathway: implications for cerebral amyloid angiopathy. Lab. Invest. 77: 157-166.