Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues – Separation or purification
Reexamination Certificate
2002-08-01
2009-10-06
Lukton, David (Department: 1654)
Chemistry: natural resins or derivatives; peptides or proteins;
Proteins, i.e., more than 100 amino acid residues
Separation or purification
C530S412000, C530S417000, C530S415000, C530S350000
Reexamination Certificate
active
07598355
ABSTRACT:
The present invention discloses characterization of interactions between ligands and Hsp90 proteins, including GRP94, wherein ligand binding to the N-terminal nucleotide binding domain of GRP94 elicits a conformational change that converts the GRP94 from an inactive to an active conformation, and wherein the chaperone and peptide-binding activities of the GRP94 are markedly stimulated. Also disclosed are purification, screening, and therapeutic methods pertaining to the biological activity of GRP94, and in some instances HSP90, based upon the characterization of ligand interactions of Hsp90 peptide-binding proteins, including GRP94.
REFERENCES:
patent: 5571840 (1996-11-01), Mayor et al.
patent: 5747332 (1998-05-01), Wallen et al.
patent: 5801160 (1998-09-01), Sandage et al.
patent: WO98/12208 (1998-03-01), None
patent: WO99/29182 (1999-06-01), None
patent: WO 01/64834 (2001-09-01), None
patent: 01/94629 (2001-12-01), None
Sigma Catalog, p. 1581, 1991 edition.
Hermanson (“Immobilized Affinity Ligand Techniques”, Academic Press, 1992, pp. 53-55).
Peng, J Immunol Meth 204, 13-21, 1997.
Massa et al., The Stress Gene Response in Brain,Cerebrovascular and Brain Metabolism Reviews8:95-158 (1996).
Csermely et al., The 90-kDa Molecular Chaperone Family: Structure, Function, and Clinical Applications. A Comprehensive Review,Pharmacol. Ther. 79, No. 2:129-168 (1998).
Xiao et al., Geldanamycin Provides Posttreatment Protection Against Glutamate-Induced Oxidative Toxicity in a Mouse Hippocampal Cell Line,J. of Neurochemistry72, No. 1:95-101 (1999).
Hearse et al., Experimental Models for the Study of Cardiovascular Function and Disease,Pharmacological Research41, No. 6:598-603 (2000).
Fan et al., Therapeutic approaches for ischemia/reperfusion injury in the liver,J. Mol Med77:577-596 (1999).
Horch et al., Destabilization of Cortical Dendrites and Spines by BDNF,Neuron23:353-364 (Jun. 1999).
McAllister et al., Opposing Roles for Endogenous BDNF and NT-3 in Regulating Cortical Dendritic Growth,Neuron18:767-778 (May 1997).
Chen et al., Stress Proteins and Tolerance to Focal Cerebral Ischemia,J. of Cerebral Blood Flow and Metabolism16:566-577 (1996).
Yagita et al., Molecular Cloning of a Novel Member of the HSP110 Family of Genes, Ischemia-Responsive Protein 94 kDa (irp94), Expressed in Rat Brain After Transient Forebrain Ischemia,J. of Neurochemistry72, No. 4:1544-1551 (1999).
Sciandra et al., Induction of glucose-regulated proteins during anaerobic exposure and of heat-shock proteins after reoxygenation,Proc. Natl. Acad. Sci. USA81:4843-4847 (Aug. 1984).
Kusnetsov et al., Perturbations in maturation of secretory proteins and their association with endoplasmic reticulum chaperones in a cell culture model for epithelial ischemia,Proc. Natl. Acad. Sci. USA93:8584-8589 (Aug. 1999).
International Search Report for PCT/US01/09512.
Obermann et al., In Vivo Function of Hsp90 is Dependent on ATP Binding and ATP Hydrolysis,J. of Cell Biology143, No. 4:901-910 (Nov. 16, 1998).
Pratt, The hsp90-based Chaperone System: Involvement in Signal Transduction from a Variety of Hormone and Growth Factor Receptors,Journal of the Society for Experimental Biology and Medicine127, No. 4:420-434 (Apr. 1998).
Fang et al., Hsp90 Regulates Androgen Receptor Hormone Binding Affinity in Vivo,J. of Biological Chemistry271, No. 45:28697-28702 (1996).
Hutchison et al., Soluble and Membrane-Associated Human Low-Affinity Adenosine Binding Protein (Adenotin): Properties and Homology with Mammalian and Avian Stress Proteins,Biochemistry29:5138-5144 (1990).
Maki et al., Human homologue of murine tumor rejection antigen gp96: 5′-Regulatory and coding regions and relationship to stress-induced proteins,Proc. Natl. Acad. Sci. USA87:5658-5662 (Aug. 1990).
Cala et al., GRP94 Resides within Cardiac Sarcoplasmic Reticulum Vesicles and Is Phosphorylated by Casein Kinase II,J. of Biological Chemistry269(8):5926-5931 (1994).
International Search report for PCT/US02/31014.
Wassenberg et al., Ligand Interactions in the Adenosine Nucleotide-binding Domain of theHsp90 Chaperone, GRP94,J. of Biological Chemistry275(30):22806-22814 (Jul. 28, 2000).
Linderoth et al., Identification of the Peptide-Binding Site in the Heat Shock Chaperone/Tumor Rejection Antigen gp96 (Grp94),J. of Biological Chemistry275(8):5472-5477 (Feb. 25, 2000).
Supplementary Partial European Search Report for 01920734.9-2401-US0109512 dated Jun. 1, 2004.
Argon et al. “GRP94, an ER chaperone with protein and peptide binding properties”,Cell&Developmental Biology10:495-505 (1999).
Grenert et al., “The Amino-terminal Domain of Heat Shock Protein 90 (hsp90) That Binds Geldanamycin Is an ATP/ADP Switch Domain That Regulates hsp90 Conformation”,The J. of Biological Chemistry272(38):23843-23850 (Sep. 19, 1997).
Hutchinson et al., “Soluble and Membrane-Associated Human Low-Affinity Adenosine Binding Protein (Adenotin): Properties and Homology with Mammalian and Avian Stress Proteins”Biochemistry29:5138-5144 (1990).
Srivastava, “Peptide-Binding Heat Shock Proteins in the Endoplasmic Reticulum: Role in Immune Response to Cancer and in Antigen Presentation”Advances in Cancer Research62:153-177 (1993).
Notification of Transmittal of International Preliminary Examination Report for PCT/US02/31014 dated Sep. 28, 2004.
European Office Action corresponding to European patent application No. 1920734.9 dated May 31, 2005.
Communication pursuant to Article 96(2) EPC corresponding to EP Patent Application No. 01920734.9 dated Sep. 12, 2006.
Communication pursuant to Article 96(2) EPC corresponding to European Application No. 01 920 734.9-2401 dated Sep. 14, 2007.
Communication pursuant to Article 94(3) EPC corresponding to European Patent Application No. 01 920 734.9-2401 dated Sep. 11, 2008.
Official Communication corresponding to U.S. Appl. No. 11/821,459 dated Nov. 17, 2008.
Nicchitta Christopher V.
Reed Robyn C.
Rosser Meredith F. N.
Wassenberg James J.
Duke University
Jenkins Wilson Taylor & Hunt, P.A.
Lukton David
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