Utilization of a multiple antigenic peptide as a calibration standard in the BAN50 single antibody sandwich ELISA for Aβ oligomers

Biochemical and Biophysical Research Communications

Volumn 422, Issue 3, 2012, Pages 375-380

  Kasai, Takashi ^a,b   Tokuda, Takahiko ^a   Taylor, Mark ^b   Nakagawa, Masanori ^a   Allsop, David ^b  

^a KYOTO PREFECTURAL UNIVERSITY OF MEDICINE   (Japan)

^b LANCASTER UNIVERSITY   (United Kingdom)

Author keywords

Alzheimer's disease; Amyloid ; ELISA; Multiple antigenic peptide; Oligomer

Indexed keywords

AMYLOID BETA PROTEIN; EPITOPE; LYSINE; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY BAN50; MULTIPLE ANTIGENIC PEPTIDE; OLIGOMER; PEPTIDE; POLYMER; SPACER DNA; UNCLASSIFIED DRUG;

ARTICLE; CALIBRATION; CEREBROSPINAL FLUID; CLINICAL ARTICLE; CONTROLLED STUDY; ENZYME LINKED IMMUNOSORBENT ASSAY; FREEZE THAWING; HUMAN; PLASMA; PRIORITY JOURNAL; SERUM; SINGLE ANTIBODY SANDWICH ENZYME LINKED IMMUNOSORBENT ASSAY;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; AMYLOID BETA-PEPTIDES; ANTIBODIES, MONOCLONAL; ANTIGENS; CALIBRATION; ENZYME-LINKED IMMUNOSORBENT ASSAY; HUMANS; LUMINESCENT MEASUREMENTS; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS;

EID: 84861936206     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.04.146     Document Type: Article

References (28)

1. Selkoe D.J. Alzheimer's disease: a central role for amyloid. J. Neuropathol. Exp. Neurol. 1994, 53:438-447.
2. Selkoe D.J. Normal and abnormal biology of the β-amyloid precursor protein. Annu. Rev. Neurosci. 1994, 17:489-517.
3. Goedert M. Tau protein and the neurofibrillary pathology of Alzheimer's disease. Trends Neurosci. 1993, 16:460-465.
4. Jarrett J.T., Berger E.P., Jr Lansbury P.T. The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 1993, 32:4693-4697.
5. Hardy J., Allsop D. Amyloid deposition as the central event in the aetiology of Alzheimer's disease. Trends Pharmacol. Sci. 1991, 12:383-388.
6. Hardy J., Selkoe D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 2002, 297:353-356.
7. Bernstein S.L., Dupuis N.F., Lazo N.D., et al. Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease. Nat. Chem. 2009, 1:326-331.
8. Lambert M.P., Barlow A.K., Chromy B.A., et al. Diffusible, nonfibrillar ligands derived from Aβ 1-42 are potent central nervous system neurotoxins. Proc. Natl. Acad. Sci. USA 1998, 95:6448-6453.
9. Walsh D.M., Klyubin I., Fadeeva J.V., et al. Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo. Nature 2002, 416:535-539.
10. Shankar G.M., Li S., Mehta T.H., et al. Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory. Nat. Med. 2008, 14:837-842.
11. Lesne S., Koh M.T., Kotilinek L., et al. A specific amyloid-β protein assembly in the brain impairs memory. Nature 2006, 440:352-357.
12. Ono K., Condron M.M., Teplow D.B. Structure-neurotoxicity relationships of amyloid β-protein oligomers. Proc. Natl. Acad. Sci. USA 2009, 106:14745-14750.
13. Funke S.A. Detection of soluble amyloid-β oligomers and insoluble high-molecular-weight particles in CSF: development of methods with potential for diagnosis and therapy monitoring of Alzheimer's disease. Int. J. Alzheimers Dis. 2011, 2011:151645.
14. LeVine H. Alzheimer's β-peptide oligomer formation at physiologic concentrations. Anal. Biochem. 2004, 335:81-90.
15. Fukumoto H., Tokuda T., Kasai T., et al. High-molecular-weight β-amyloid oligomers are elevated in cerebrospinal fluid of Alzheimer patients. FASEB. J. 2010, 24:2716-2726.
16. Posnett D.N., McGrath H., Tam J.P. A novel method for producing anti-peptide antibodies. Production of site-specific antibodies to the T cell antigen receptor β-chain. J. Biol. Chem. 1988, 263:1719-1725.
17. Taylor M., Moore S., Mayes J., et al. Development of a proteolytically stable retro-inverso peptide inhibitor of β-amyloid oligomerization as a potential novel treatment for Alzheimer's disease. Biochemistry 2010, 49:3261-3272.
18. El-Agnaf O.M., Salem S.A., Paleologou K.E., et al. Detection of oligomeric forms of α-synuclein protein in human plasma as a potential biomarker for Parkinson's disease. FASEB. J. 2006, 20:419-425.
19. Xia W., Yang T., Shankar G., et al. A specific enzyme-linked immunosorbent assay for measuring β-amyloid protein oligomers in human plasma and brain tissue of patients with Alzheimer disease. Arch. Neurol. 2009, 66:190-199.
20. Klaver A.C., Patrias L.M., Finke J.M., et al. Specificity and sensitivity of the Aβ oligomer ELISA. J. Neurosci. Methods 2011, 195:249-254.
21. Tjernberg L.O., Naslund J., Lindqvist F., et al. Arrest of β-amyloid fibril formation by a pentapeptide ligand. J. Biol. Chem. 1996, 271:8545-8548.
22. Ohnishi S., Kamikubo H., Onitsuka M., et al. Conformational preference of polyglycine in solution to elongated structure. J. Am. Chem. Soc. 2006, 128:16338-16344.
23. Gao C.M., Yam A.Y., Wang X., et al. Aβ40 oligomers identified as a potential biomarker for the diagnosis of Alzheimer's disease. PLoS One 2010, 5:e15725.
24. Urbanc B., Cruz L., Yun S., et al. In silico study of amyloid β-protein folding and oligomerization. Proc. Natl. Acad. Sci. USA 2004, 101:17345-17350.
25. Haass C., Selkoe D.J. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide. Nat. Rev. Mol. Cell. Biol. 2007, 8:101-112.
26. Georganopoulou D.G., Chang L., Nam J.M., et al. Nanoparticle-based detection in cerebral spinal fluid of a soluble pathogenic biomarker for Alzheimer's disease. Proc. Natl. Acad. Sci. USA 2005, 102:2273-2276.
27. Schupf N., Tang M.X., Fukuyama H., et al. Peripheral Aβ subspecies as risk biomarkers of Alzheimer's disease. Proc. Natl. Acad. Sci. USA 2008, 105:14052-14057.
28. Tokuda T., Qureshi M.M., Ardah M.T., et al. Detection of elevated levels of α-synuclein oligomers in CSF from patients with Parkinson disease. Neurology 2010, 75:1766-1772.