Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving antigen-antibody binding – specific binding protein...
Reexamination Certificate
2011-04-19
2011-04-19
Hayes, Robert C (Department: 1649)
Chemistry: molecular biology and microbiology
Measuring or testing process involving enzymes or...
Involving antigen-antibody binding, specific binding protein...
C435S007100
Reexamination Certificate
active
07927824
ABSTRACT:
A chaperone protein Q2 and β-amyloid can form a complex. This complex can be detected in a biological sample, such as, for example, tissues or fluids from a mammal. Q2 levels can also be detected in a biological sample. A method for determining the Q2 level in a biological sample and comparing that level to a normal Q2 level can be used to detect, screen, diagnose, or otherwise determine a person's susceptibility to Alzheimer's disease such as, for example, the presence or absence of Alzheimer's disease, of symptoms of this disease, of factors leading to or associated with this disease, of likelihood of developing this disease, and the like. In one embodiment, a decline in Q2 level correlates to an increased likelihood of developing Alzheimer's disease. In another embodiment, a decline in Q2 level correlates to an increase in β-amyloid aggregation. The method may further include screening for an apolipoprotein E genotype, which is associated with Alzheimer's disease.
REFERENCES:
patent: 5223482 (1993-06-01), Schilling et al.
patent: 5707821 (1998-01-01), Rydel et al.
patent: 5750349 (1998-05-01), Suzuki et al.
patent: 5780587 (1998-07-01), Potter
patent: 0 783 104 (1996-12-01), None
patent: 96/12736 (1996-05-01), None
patent: WO 99/029657 (1999-06-01), None
Ida et al., 1996,The Journal of Biological Chemistry, 271:22908-22914, “Analysis of Heterogeneous βA4 Peptides in Human Cerebrospinal Fluid and Blood by a Newly Developed Sensitive Western Blot Assay”.
Matsubara et al., 1996,Biochemical Journal, 316:671-679, “Apolipoprotein J and Alzheimer's amyloid β solubility”.
Rudinger “Characteristics of the amino acids as components of a peptide hormone sequence” In “Peptide Hormones” (ed J.A. Parsons) University Park Press Baltimore, pp. 1-7 (1976).
Koivunen et al. GenBank Accession No. U75885, dated Jul. 9, 1997.
Elliott et al., “The Thiol-dependent Reductase Erp57 Interacts Specifically withN-Glycosylated Integral Membrane Proteins”, The Journal of Biological Chemistry, 272 (21):13849-13855 (1997).
Frickel et al., “ERp57 Is a Multifunctional Thiol-Disulfide Oxidoreductase”, The Journal of Biological-Chemistry, 279(18):18227-18287 (2004).
Haass et al., β-Amyloid Peptide and a 3-kDa Fragment Are Derived by Distinct Cellular Mechanism: The Journal of Biological Chemistry, vol. 268, No. 5, pp. 3021-3024, 1993.
Hirano et al., “Molecular cloning of the human glucose-regulated protein ERp57/GRP58, a thiol-dependent reductase: Identification of its secretory form and inducible expression by the oncogenic transformation”, Eur J Biochem, 234:336-342 (1995).
Malinchik et al., “Structural Analysis of Alzheimer's β(1-40) Amyloid: Protofilament Assembly of Tubular Fibrils”, Biophysical Journal, 74:537-545 (1998).
Otvos et al., “Human and rodent Alzheimer β-amyloid peptides acquire distinct conformations in membrane-mimicking solvents”, Eur J Biochem, 211:249-257 (1993).
Sehgal, “Plasma membrane rafts and chaperones in cytokine/STAT signaling”, Acta Biochimica Polonica Quarterly,50(Mar. 2003):583-594 (2003).
Sisodia et al., “Role of the β-amyloid protein in Alzheimer's disease”, FASEB J., 9:366-370 (1995).
Jarrett et al., “The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease,”Biochemistry32: 4693-4697 (1993). (ABSTRACT ONLY).
Mori et al., “Mass spectrometry of purified amyloid β protein in Alzheimer's disease,”J. Biol. Chem.267:17082-17086 (1992).
Wiltfang et al., “Improved electrophoretic separation and immunoblotting of beta-amyloid (A beta) peptides 1-40, 1-42, and 1-43,”Electrophoresis18:527-532 (1997). (ABSTRACT ONLY).
Furumoto, H. et al., “Apolipoprotein E is Present in Primary Localized Cutaneous Amyloidosis,”The Journal of Investigative Dermatology, vol. 111, No. 3, pp. 417-421 (Sep. 1998).
Holtzman, J. et al., “A Chaperon Binds to b-Amyloids: Implications for the Etiology of Alzheimer's Disease,”Molecular Biology of the Cell, vol. 9, Supplement, Abstract No. 612, p. 106a (Nov. 1998).
Kudva, Y. et al., “Small heat shock proteins inhibit in vitro Aβ1-42amyloidogenesis,”FEBS Letters, vol. 416, pp. 117-121 (1997).
Lindquist, J. et al., “ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly,”The EMBO Journal, vol. 17, No. 8, pp. 2186-2195 (1998).
Yang, Y. et al., “The Chaperone BiP/GRP78 Binds to Amyloid Precursor Protein and Decreases Aβ40 and Aβ42 Secretion,”The Journal of Biological Chemistry, vol. 273, No. 40, pp. 25552-25555 (Oct. 2, 1998).
Dorn Brian R.
Hayes Robert C
Holtzman Jordan L.
Merchant & Gould P.C.
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