Intracellular APP processing and Aβ production in Alzheimer disease

Journal of Neuropathology and Experimental Neurology

Volumn 58, Issue 8, 1999, Pages 787-794

  Wilson, Christina A ^a   Doms, Robert W ^a   Lee, Virginia M Y ^a,b  

^a HOSPITAL OF THE UNIVERSITY OF PENNSYLVANIA   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

Endoplasmic reticulum; Insoluble A 42; Intracellular A ; Senile plaques

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; PRESENILIN 1; PRESENILIN 2;

ALZHEIMER DISEASE; ARTICLE; ENDOPLASMIC RETICULUM; GENE MUTATION; PATHOGENESIS; PRIORITY JOURNAL; PROTEIN LOCALIZATION; PROTEIN PROCESSING; PROTEIN SECRETION; PROTEIN SYNTHESIS; SENILE PLAQUE;

EID: 0032800818     PISSN: 00223069     EISSN: None     Source Type: Journal    
DOI: 10.1097/00005072-199908000-00001     Document Type: Article

References (67)

1. Selkoe DJ. Cellular and molecular biology of β-amyloid precursor and Alzheimer's disease. In: Prusiner SB, Rosenberg RN, Mauro SD, et al, eds. The molecular and genetic basis of neurological disease. Boston: Butterworth Heinemann Press, 1997:601-2
2. Golde TE, Estus SC, Usiak M, Younkin LH, Younkin SG. Expression of β amyloid protein precursor mRNAs: Recognition of a novel alternatively spliced form and quantitation in Alzheimer's disease using PCR. Neuron 1990;4:253-67
3. Rang J, Muller-Hill B. Differential splicing of Alzheimer's disease amyloid A4 precursor RNA in rat tissues: PreA4-695 is predominantly produced in rat and human brain. Biochem Biophys Res Commun 1990;166:1192-200
4. Muller U, Cristina N, Li ZW, et al. Behavioral and anatomical deficits in mice homozygous for a modified β-amyloid precursor protein. Cell 1994;79:755-65
5. Sisodia SS, Koo EH, Beyreuther K, Unterbeck A, Price DL. Evidence that β-amyloid protein in Alzheimer's disease is not derived by normal processing. Science 1990;248:492-95
6. Seubert P, Vigo-Pelfry C, Esch F, et al. Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids. Nature 1992;359:325-27
7. Iwatsubo T, Okada A, Suzuki N, Mizusawa H, Nukina N, Ihara Y. Visualization of Aβ42(43) and Aβ40 in senile plaques with specific Aβ monoclonals: Evidence that the initially deposited species is Aβ42(43). Neuron 1994;13:45-53
8. Jarrett JT, Berger EP, Lansbury PT. The carboxy terminus of β-amyloid protein is critical for the seeding of amyloid formation: Implications for pathogenesis of Alzheimer's disease. Biochemistry 1993;32:4693-97
9. Jarrett JT, Lansbury PT Jr. Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie? Cell 1993;73:1055-58
10. Wisniewski KE, Dalton AJ, McLachlan C, Wen GY, Wisniewski HM. Alzheimer's disease in Down's syndrome: Clinicopathologic studies. Neurol 1985;35:957-61
11. Giaccone G, Tagliavini F, Linoli G, et al. Down patients: Extracellular preamyloid deposits precede neuritic degeneration and senile plaques. Neurosci Lett 1989;97:232-38
12. Goate A, Chartier-Harlin MC, Mullan M, et al. Segregation of a missense mutation in the amyloid precursor gene with familial Alzheimer's disease. Nature 1991;349:704-6
13. Citron M, Oltersdorf T, Haass C, et al. Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increases β-protein production. Nature 1992;360:672-74
14. Sherrington R, Rogaev EI, Liang Y, et al. Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature 1995;375:754-60
15. Levy-Lehad E, Wijsman EM, Nemens E, et al. A familial Alzheimer's disease locus on chromosome 1. Science 1995;269:970-73
16. Cai XD, Golde TE, Younkin SG. Release of excess amyloid β-protein from a mutant amyloid β-protein precursor. Science 1993;259:514-46
17. Haass C, Lemere CA, Capell A, et al. The Swedish mutation causes early-onset Alzheimer's disease by β-secretase cleavage within the secretory pathway. Nat Med 1995;1:1291-96
18. Thinakaran G, Teplow DB, Siman R, Greenberg B, Sisodia SS. Metabolism of the "Swedish" amyloid precursor protein variant in neuro2a (N2a) cells. Evidence that cleavage at the "β-secretase" site occurs in the Golgi apparatus. J Biol Chem 1996;271:9390-97
19. Suzuki N, Cheung TT, Cai XD, et al. An increased percentage of long amyloid β protein is secreted by familial amyloid β protein precursor (βAPP 717) mutants. Science 1994;264:1336-40
20. Hsiao K, Chapman P, Nilsen S, et al. Correlative memory deficits, Aβ elevation, and amyloid plaques in transgenic mice. Science 1996;274:99-102
21. Games D, Adams D, Alessandrini R, et al. Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein. Nature 1995;373:523-27
22. Johnson-Wood K, Lee M, Motter R, et al. Amyloid precursor protein processing and Aβ42 deposition in a transgenic mouse model of Alzheimer disease. Proc Natl Acad Sci USA 1997;94:1550-55
23. Hsia AY, Masliah E, McConlogue L, et al. Plaque-independent disruption of neural circuits in Alzheimer's disease mouse models. Proc Natl Acad Sci USA 1999;96:3228-33
24. Chen KS, Masliah E, Grajeda H, et al. Neurodegenerative Alzheimer-like pathology in PDAPP 717V->F transgenic mice. Prog Brain Res 1998;117:327-34
25. Xia W, Zhang J, Perez R, Koo EH, Selkoe DJ. Interactions between amyloid precursor protein and presenilins in mammalian cells: Implications for the pathogenesis of Alzheimer's disease. Proc Natl Acad Sci USA 1997;94:8208-13
26. DeStrooper B, Saftig P, Craessaerts K, et al. Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein. Nature 1998;391:387-90
27. Younkin SG, Tanzi RE, Christen Y. Presenilins and Alzheimer's disease. New York: Springer-Verlag 1998
28. Scheuner D, Eckman C, Jensen M, et al. 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. Nat Med 1996;2:864-70
29. Klafki HW, Abramowski D, Swoboda R, Paganetti PA, Staufenbiel M. The carboxyl termini of β amyloid peptides 1-40 and 1-42 are generated by distinct γ-secretase activities. J Biol Chem 1996;271: 28655-59
30. Skovronsky DM, Doms RW, Lee VM-Y. Evidence that distinct proteases produce intracellular versus secreted Aβ. Unpublished observation.
31. Wertkin AM, Turner RS, Pleasure SJ, et al. Human neurons derived from a teratocarcinoma cell line express solely the 695-amino acid amyloid precursor protein and produce intracellular β-amyloid or A4 peptides. Proc Natl Acad Sci USA 1993;90:9513-17
32. Turner RS, Suzuki N, Chyung ASC, Younkin SG, Lee VM-Y. Amyloid β 40 and β 42 are generated intracellularly in human neurons and their secretion increases with maturation. J Biol Chem 1996;271:8966-70
33. Skovronsky DM, Doms RW, Lee VM-Y. Detection of a novel intraneuronal pool of insoluble amyloid β-protein that accumulates with time in culture. J Cell Bio 1998;141:1031-39
34. Fuller SJ, Storey E, Li QX, Smith AI, Beyreuther K, Masters CL. Intracellular production of βA4 amyloid of Alzheimer's disease: Modulation by phosphoramidon and lack of coupling to the secretion of the amyloid precursor protein. Biochemistry 1995;34:8091-98
35. Kuentzel SL, Ali SM, Altman RA, Greenberg BD, Raub TJ. The Alzheimer β-amyloid protein precursor/protease nexin-II is cleaved by secretase in a trans-Golgi secretory compartment in human neuroglioma cells. Biochem J 1993;295:367-78
36. Cook DG, Forman MS, Sung JC, et al. Alzheimer Aβ (42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells. Nat Med 1997;3:1021-23
37. Wild-Bode C, Yamazaki T, Capell A, et al. Intracellular generation and accumulation of amyloid β-peptide terminating at amino acid 42. J Biol Chem 1997;272:10685-88
38. Chyung ASC, Greenberg BD, Cook DG, Doms RW, Lee VM-Y. Novel β-secretase cleavage of β-amyloid precursor protein in the endoplasmic reticulum/intermediate compartment of NT2N cells. J Cell Bio 1997;138:671-80
39. Forman MS, Cook DG, Leight S, Doms RW, Lee VM-Y. Differential effects of the Swedish mutant amyloid precursor protein on β-amyloid accumulation and secretion in neurons and non-neuronal cells J Biol Chem 1997;272:32247-53
40. Sisodia SS. β-amyloid precursor protein cleavage by a membrane-bound protease. Proc Natl Acad Sci USA 1992;89:6075-79
41. Rossner S, Ueberham U, Schliebs R, Perez-Polo JR, Bigl V. The regulation of amyloid precursor protein metabolism by cholinergic mechanisms and neurotrophin receptor signaling. Prog Neurobiol 1998;56:541-69
42. Buxbaum JD, Liu KN, Luo Y, et al. Evidence that tumor necrosis factor a converting enzyme is involved in regulated α-secretase cleavage of the Alzheimer amyloid protein precursor. J Biol Chem 1998;273:27765-67
43. Haass C, Schlossmacher MG, Hung AY, et al. Amyloid β-peptide is produced by cultured cells during normal metabolism. Nature 1992;359:322-25
44. Seubert P, Oltersdorf T, Lee MG, et al. Secretion of β-amyloid precursor protein cleaved at the amino terminus of the β-amyloid peptide. Nature 1993;361:260-63
45. Weidemann A, Koenig G, Bunke D, et al. Identification, biogenesis, and localization of precursors of Alzheimer disease A4 amyloid protein. Cell 1989;57:115-26
46. Golde TE, Estus S, Younkin LH, Selkoe DJ, Younkin SG. Processing of the amyloid protein precursor to potentially amyloidogenic derivatives. Science 1992;255:728-30
47. Koo EH, Squazzo S. Evidence that production and release of amyloid β-protein involves the endocytic pathway. J Biol Chem 1994;269:17386-89
48. Shoji M, Golde TE, Ghiso J, et al. Production of the Alzheimer amyloid β protein by normal proteolytic processing. Science 1992;258:126-29
49. Haass C, Hung AV, Schlossmacher MG, Teplow DB, Selkoe DJ. β-amyloid peptide and a 3-kDa fragment are derived by distinct cellular mechanisms. J Biol Chem 1993;268:3021-24
50. Tienari PJ, Ida N, Ikonen E, et al. Intracellular and secreted Alzheimer β-amyloid species are generated by distinct mechanisms in cultured hippocampal neurons. Proc Natl Acad Sci USA 1997;94: 4125-30
51. Hartmann T, Bieger SC, Bruhl B, et al. Distinct sites of intracellular production for Alzheimer's disease Aβ40/42 amyloid peptides. Nat Med 1997;3:1016-17
52. Xu H, Sweeney D, Wang R, et al. Generation of Alzheimer's β-amyloid protein in the trans-Golgi in the apparent absence of vesicle formation. Proc Natl Acad Sci USA 1997;94:3748-52
53. Martin BL, Schrader-Fischer G, Busciglio J, Duke M, Paganetti P, Yankner BA. Intracellular accumulation of β-amyloid in cells expressing the swedish mutant amyloid precursor protein. J Biol Chem 1995;270:26727-30
54. Sambamurti K, Shioi J, Anderson JP, Pappolla MA, Robakis NK. Evidence for intracellular cleavage of the Alzheimer's amyloid precursor in PC12 cells. J Neurosci Res 1992;33:319-29
55. Gabudza D, Busciglio J, Chen LB, Masudaira P, Yankner BA. Inhibition of energy metabolism alters the processing of amyloid precursor protein and induces a potentially amyloidogenic derivative. J Biol Chem 1994;249:13623-28
56. Greenfield JP, Tsai J, Gouras GK, et al. Endoplasmic reticulum and trans-Golgi network generate distinct populations of Alzheimer β-amyloid peptides. Proc Natl Acad Sci USA 1999;96:742-47
57. Masliah E, Sisk A, Mallory M, Mucke L, Schenk D, Games D. Comparison of neurodegenerative pathology in transgenic mice overexpressing V717F β-amyloid precursor protein and Alzheimer's disease. J Neurosci 1996;16:5795-811
58. Martin LJ, Pardo CA, Cork LC, Price DL. Synaptic pathology and glial responses to neuronal injury precede the formation of senile plaques and amyloid deposits in the aging cerebral cortex. Am J Pathol 1994;145:1358-81
59. Cotman CW, Su JH. Mechanisms of neuronal death in Alzheimer's disease. Brain Pathol 1996;6:493-506
60. Bahr BA, Hoffman KB, Yang AJ, Hess US, Glabe CG, Lynch G. Amyloid β-protein is internalized selectively by hippocampal field CA1 and causes neurons to accumulate amyloidogenic carboxyterminal fragments of the amyloid precursor protein. J Comp Neurol 1998;397:139-47
61. LaFerla FM, Troncoso JC, Strickland DK, Kawas CH, Jay G. Neuronal cell death in Alzheimer's disease correlates with apoE uptake and intracellular Aβ stabilization. J Clin Invest 1997;100:310-20
62. Ginsberg SD, Crino PB, Hemby SE, et al. Predominance of neuronal mRNAs in individual Alzheimer's disease senile plaques. Ann Neurol 1999;45:174-81
63. Iverson LL, Mortishire-Smith RJ, Pollack SJ, Shearman MS. The toxicity in vitro of β-amyloid protein. Biochem J 1995;311:1-16
64. Grundke-Iqbal I, Iqbal K, George L, Tung YC, Kim KS, Wisniewski HM. Amyloid protein and neurofibrillary tangles coexist in the same neuron in Alzheimer disease. Proc Natl Acad Sci USA 1989;86:2853-57
65. Perry G, Cras P, Siedlak SL, Tabaton M, Kawai M. β-protein immunoreactivity is found in the majority of neurofibrillary tangles of Alzheimer's disease. Am J Pathol 1992;140:283-90
66. Murphy GM, Forno LS, Higgins L, Scardina JM, Eng LF, Cordell B. Development of a monoclonal antibody specific for the COOH-terminal of β-amyloid 1-42 and its immunohistochemical reactivity in Alzheimer's disease and related disorders. Am J Pathol 1994;144:1082-88
67. Schwab C, Akiyama H, McGeer EG, McGeer PL. Extracellular neurofibrillary tangles are immunopositive for the 40 carboxy-terminal sequence of β-amyloid protein. J Neuropathol Exp Neurol 1998;57:1131-37