Publication Cover
Amyloid
The Journal of Protein Folding Disorders
Volume 2, 1995 - Issue 4
40
Views
19
CrossRef citations to date
0
Altmetric
Original Article

Elevated Aβ levels in Alzheimer's disease brain are associated with selective accumulation of Aβ42 in parenchymal amyloid plaques and both Aβ40 and Aβ42 in cerebrovascular deposits

, , , , , & show all
Pages 234-240 | Received 05 May 1995, Published online: 06 Jul 2009

References

  • Miller D L, Papayannopoulos I A, Styles J, Bobin S A, Lin Y Y, Biemann K, Iqbal K. Peptide compositions of the cerebrovascular and senile plaque core amyloid deposits of Alzheimer's disease. Arch Biochem Biophys 1993; 301: 41–52
  • Roher A E, Lowenson J D, Clarke S, Wolkow C, Wang R, Cotter R J, Reardon I M, Zurcher-Neeley H A, Heinrikson R L, Ball M J, Greenberg B D. Structural alterations in the peptide backbone of -amyloid core protein may account for its deposition and stability in Alzheimer's disease. J Biol Chem 1993; 268: 3072–3083
  • Selkoe D J. Normal and abnormal biology of the ß-amyloid precursor protein. Annu Rev Neurosci 1994; 17: 489–517
  • Siman R, Greenberg B D. Alzheimer's disease: pathogenesis and therapy. Emerging Srategies in Neurotherapeutics, J Patel, L Pullan. Humana Press, Clifton, NJ, (in press)
  • Burdick D, Soreghan B, Kwon M, Kosmoski J, Knauer M, Henschen A, Yates J, Cotman C, Glabe C. Assembly and aggregation properties of synthetic Alzheimer's A4/ß amyloid peptide analogs. J Biol Chem 1992; 267: 546–554
  • Jarrett J T, Berger E P, Lansbury P T. The carboxy terminus of the ß-amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease. Biochem 1993; 32: 4693–4697
  • Roher A E, Lowenson J D, Clarke S, Woods A S, Cotter R J, Gowing E, Ball M J. ß-amyloid (1–42) is a major component of cerebrovascular amyloid deposits: Implications for the pathology of Alzheimer's disease. Proc Natl Acad Sci (USA) 1993; 90: 10836–10840
  • Iwatsubo T, Odaka A, Suzuki N, Mizusawa H, Nukina N, Ihara Y. Visualization of Aß42/43 and Aß40 in senile plaques with end-specific Aß monoclonals: Evidence that an initially deposited species is Aß42/43. Neuron 1994; 13: 45–53
  • Suzuki N, Iwatsubo T, Odaka A, Ishibashi Y, Kitada C, Ihara Y. High tissue content of soluble ß1–40 is linked to cerebral amyloid angiopathy. Am J Pathol 1994; 145: 452–460
  • Yamaguchi H, Sugihara S, Ishiguro K, Takashima A, Hirai S. Immunohistochemical analysis of COOH-termini of amyloid beta protein (Aß) using end-specific antisera for Aß40 and Aß42 in Alzheimer's disease and normal aging. Amyloid: Int J Exp Clin Invest 1995; 2: 7–16
  • Kim K S, Wen G Y, Bancher C, Chen C MJ, Sapienza V J, Hong H, Wisniewski H M. Detection and quantitation of amyloid B peptide with 2 monoclonal antibodies. Neurosci Res Comm 1990; 7: 113–122
  • Greenberg B. The COOH-terminus of the Alzheimer amyloid Aß peptide: Differences in length influence the process of amyloid deposition in Alzheimer brain and tell us something about relationships among parenchymal and vessel-associated amyloid deposits. Amyloid: Int J Exp Clin Invest 1995; 2: 195–203
  • Tabaton M, Nunzi M G, Xue R, Usiak M, Autilio-Gambetti L, Gambetti P. Soluble amyloid ß-protein is a marker of Alzheimer amyloid in brain but not cerebrospinal fluid. Biochem Biophys Res Comm 1994; 200: 1592–1603
  • Harigaya Y, Shoji M, Kawarabayashi T, Kanai M, Nakamura T, Iizuka T, Igeta Y, Saido T C, Sahara N, Mori H, Hirai S. Modified amyloid ß protein ending at 42 or 40 with different solubility accumulates in the brain of Alzheimer's disease. Biochem Biophys Res Comm 1995; 211: 1015–1022
  • Mori H, Takio K, Ogawara M, Selkoe D J. Mass spectroscopy of purified amyloid ß protein in Alzheimer's disease. J Biol Chem 1992; 267: 17082–17086

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.