Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or...
Reexamination Certificate
2006-12-12
2006-12-12
Andres, Janet L. (Department: 1649)
Chemistry: molecular biology and microbiology
Measuring or testing process involving enzymes or...
C424S009200
Reexamination Certificate
active
07148001
ABSTRACT:
Co-incubation of an amyloid protein with sulfated macromolecules as a method for the formation of amyloid plaques. The amyloid protein may be the beta-amyloid protein or the prion protein or the like. Amyoid plaque formation in one embodiment proceeds in vitro and desirably produces amyloid plaques that stain with Congo red and demonstrate a maltese-cross pattern when viewed under polarized light. The method also produces amyloid plaques that demonstrate an “amyloid star” appearance when viewed by transmission electron microscopy. An in vivo assay is also presented for selecting a candidate therapeutic agent for inhibiting or disrupting amyloid plaque deposition or persistence.
REFERENCES:
Snow et al. “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, vol. 12, pp. 219-234, Jan. 1994.
Castillo et al. “Perlecan Binds to the β-Amyloid Proteins (Aβ) of Alzheimer's Disease, Acclerates AβFibril Formation, and Maintains AβFibril Stability,” Journal of Neurochemistry, vol. 69, No. 6, pp. 2452-2464, 1997.
Desdouits et al. “Amyloid β Peptide Formation in Cell-free Preparations,” Journal of Biological Chemistry, vol. 271, No. 40, pp. 24670-24674, Oct. 4, 1996.
Jensen et al. “Binding of Aβ to α- and β-Synucleins: Identification of Segments in α-Synuclein/NAC Precursor that Bind Aβand NAC,” Biochem. J., vol. 323, pp. 539-546, 1997.
Bame et al. “Aβ(1-40) Prevents Heparanase-catalyzed Degradation of Heparan Sulfate Glycosaminoglycans and Proteoglycansin Vitro,” Journal of Biological chemistry, vol. 272, No. 27, pp. 17005-17011, Jul. 4, 1997.
Castillo et al. “Novel Purification and Detailed Characterization of Perlecan Isolated from the Engelbreth-Holm-Swarm Tumor for Use in an Animal Model of Fibrillar AB Amyloid Persistence in Brain.” J. Biochem, vol. 120, No. 2, pp. 433-444, 1996.
Verga et al. “Alzheimer Patients and Down Patients; Cerebral Preamyloid Deposits Differ Ultrastructurally and Histochemically from the Amyloid of Senile Plaques.” Neuroscience Letters, vol. 105, pp. 294-298, 1989.
Barcikowsha et al. “About the Presence of Paired Helical Filaments in Dystrophic Neurites Participating in the Plaque Formation.” Neuropathol, vol. 78, pp. 225-231, 1989.
Ikeda et al. “Morphology and Distribution of Plaque and Related Ddeposits in the Brains of Alzheimer's Disease and Control Cases.” Laboratory Investigation, vol. 60, No. 1, p. 113-122, 1989.
Masliah et al. “Re-Evaluation of the Structural Organization of Neuritic Plaques in Alzheimer's Disease.” Journal of Neuropathology and Experimental Neurology, vol. 52, No. 6, pp. 619-632, Nov., 1993.
Wisniewski et al. “Spectrum of Morphological Appearance of Amyloid Deposits in Alzheimer's Disease.” Acta Neuropathol, vol. 78, pp. 337-347, 1989.
Schmidt et al. “Chemical and Immunological Heterogeneity of Fibrillar Amyloid in Plaques of Alzheimer's Disease and Down's Syndrome Brains Revealed by Confocal Microscopy.” American Journal of Pathology, vol. 147, No. 2, pp. 503-515, Aug. 1995.
Dickson. “The Pathogenesis of Senile Plaques.” Journal of Neuropathology and Experimental Neurology, vol. 56, No. 4, pp. 321-339, Apr. 1997.
Selkoe et al. “Isolation of Low-Molecular-Weight Proteins from Amyloid Plaque Fibers in Alzheimer's Disease.” Journal of Neurochemistry, vol. 46, No. 6, pp. 1820-1834, 1986.
Snow et al. “The Presence of Heparin Sulfate Proteoglycans in the Neuritic Plaques and Congophilic Angiopathy in Alzheimer's Disease.” American Journal of Pathology, vol. 133, No. 3, pp. 456-463, Dec. 1988.
Glenner et al. “Alzheimer's Disease: Initial Report of the Purification and Characterization of a Novel Cerebrovascular Amyloid Protein.” Biochemical and Biophysical Research Communications, vol. 120, No. 3, pp. 885-890, May 16, 1984.
Masters et al. “Amyloid Plaque Core Protein in Alzheimer Disease and Down Syndrome.” Medical Sciences, vol. 82, pp. 4245-4249, Jun. 1983.
Who-Iuis Nomenclature Sub-Committee. “Nomenclature of Amyloid and Amyloidosis.” Bulletin of the World Health Organization, vol. 71, No. 1, pp. 105-108, 1993.
Tanzi et al. “Protease Inhibitor Domain Encoded by an Amyloid Protein Precursor Mrna Associated with Alzheimer's Disease.” Nature, vol. 331, pp. 528-532, Feb. 1988.
Kitaguchi et al. “Novel Precursor of Alzheimer's Disease Amyloid Protein Shows Protease Inhibitory Activity.” Nature, vol. 331, pp. 530-532, Feb. 11, 1988.
Ponte et al. “A New A4 Amyloid mRNA Contains a Domain Homologous to Sering Proteinase Inhibitors.” Nature, vol. 311, pp. 525-527, Feb. 11, 1988.
Grundke-Iqbal et al. “Abnormal Phosphorylation of the Microtubule-Associated Protein τ (tau) in Alzheimer Cytosheletal Pathology.” Proc. Natl. Acad. Sci. USA, vol. 83, pp. 4913-4917, Jul. 1986.
Kosik et al. “Microtubule-Associated Protein Tau τ is a Major Antigenic Component of Paired Helical Filaments in Alzheimer Disease.” Proc. Natl. Acad. Sci. USA, vol. 83, pp. 4044-4048, Jun. 1986.
Lee et al. “A68: A Major Subunit of Paired Helical Filaments and Derivatized Forms of Normal Tau.” Science, vol. 25, pp. 675-678, Feb., 1991.
Mandybur. “Cerebral Amyloid Angiopathy: The Vascular Pathology and Complications.” Journal of Neuropathology and Experimental Neurology, vol. 45, No. 1, pp. 79-90, Jan, 1986.
Pardridge et al. “Amyloid Angiopathy of Alzheimer's Disease: Amino Acid Composition and Partial Sequence of a 4,200-Dalton Peptide Isolated from Cortical Microvessels.” Journal of Neurochemistry, vol. 49, No. 5, pp. 1394-1401, 1987.
Pike et al. “In Vitro Aging of β-Amyloid Protein Causes Peptide Aggregation and Neurotoxicity.” Brain Research, vol. 563, pp. 311-314, 1991.
Pike et al. “Structure-Activity Analyses of β-Amyloid Peptides: Contributions of the β25-35 Region to Aggregation and Neurotoxicity.” Journal of Neurochemistry, vol. 64, No. 1, pp. 253-265, 1995.
Harrigan et al. “Beta Amyloid is Neurotoxic in Hippocampal Slice Cultures.” Neurobiology of Aging, vol. 16, No. 5, pp. 779-789, 1995.
Games et al. “Alzheimer-Type Neuropathology in Transgenic Mice Overexpressing V717F β-Amyloid Precursor Protein.” Nature, vol. 373, pp. 523-527, Feb. 9, 1995.
Hsiao et al. “Age-Related CNS Disorder and Early Death in Transgenic FVB/N Mice Overexpressing Alzheimer Amyloid Precursor Proteins.” Neuron, vol. 15, pp. 1203-1218, Nov. 1995.
Flood et al. “Amnestic Effects in Mice of Four Synthetic Peptide Homologous to Amyloid β Protein from Patients with Alzheimer Disease.” Proc. Natl. Acad. Sci. USA, vol. 88, pp. 3363-3366, Apr. 1991.
Flood et al. “An Amyloid β-Protein Fragment, A β[12-28], Equipotently Impairs Post-Training Memory Processing When Injected into Different Limbic System Structures.” Brain Research, vol. 663, pp. 271-276, 1994.
Van Broeckhoven et al. “Amyloid β Protein Precursor Gene and Hereditary Cerebral Hemorrhage with Amyloidosis (Dutch).” Science, vol. 248, pp. 1120-1124, Jun. 1990.
Van Broeckhoven. “Molecular Genetics of Alzheimer Disease: Identification of Genes and Gene Mutations.” Eur Neurol, vol. 35, pp. 8-19, Oct. 1991.
Haass et al. “The Swedish Mutation Causes Early-Onset Alzheimer's Disease by β-Secretase Cleavage within the Secretory Pathway.” Nature Medicine, vol. 1, No. 12, pp. 1291-1296, Dec. 1995.
Murrell et al. “A Mutation in the Amyloid Precursor Protein Associated with Hereditary Alzheimer's Disease.” Science, vol. 254, pp. 97-99, Oct. 1991.
Hardy et al. “Framing β-Amyloid.” Na
Castillo Gerardo
Snow Alan D.
Andres Janet L.
Ballard Kimberly A.
Dwyer Patrick M.
University of Washington
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