Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Recombinant dna technique included in method of making a...
Reexamination Certificate
2007-08-28
2009-12-29
Rao, Manjunath N (Department: 1647)
Chemistry: molecular biology and microbiology
Micro-organism, tissue cell culture or enzyme using process...
Recombinant dna technique included in method of making a...
C435S325000, C435S007800, C530S350000, C530S402000
Reexamination Certificate
active
07638301
ABSTRACT:
The presently disclosed subject matter discloses isolated ADAM 10 modulating peptides and related compounds useful for studying the biological functions of ADAM 10 and for the treatment of diseases such as cancer, neurological disorders, asthma, and allergic responses, and disorders characterized at least in part by the presence of one or more of inflammation, excess cell proliferation, angiogenesis, and excess soluble CD23. In one aspect, the presently disclosed subject matter provides isolated mouse and human ADAM 10 prodomain comprising the sequence set forth in SEQ ID NOs 1-8, or a sequence having at least 95% homology to any of SEQ ID NOs 1-8 and having the functionality of modulating ADAM 10 activity.
REFERENCES:
patent: 5922546 (1999-07-01), Mayer et al.
patent: 5935792 (1999-08-01), Rubin et al.
patent: 6319681 (2001-11-01), Dalie et al.
patent: 6319704 (2001-11-01), Rubin et al.
patent: 6399350 (2002-06-01), Rubin et al.
patent: 6531290 (2003-03-01), Dalie et al.
Fahrenholz et al 2000. Ann NY Acad Sci 920:215-222.
Edwards et al. 2008. Molecular Aspects of Med 29:258-289.
Bowie et al, 1990, Science 247:1306-1310.
Wells, 1990, Biochemistry 29:8509-8517.
Ngo et al., 1994, The Protein Folding Problem and Tertiary Structure Prediction, Merz et al., eds, Birkhauser, Boston, pp. 433-506.
Gerhard et al. 2004. Genome Res 14:2121-2127.
Uniprot KB/Swiss-Prot 035598, downloaded Feb. 10, 2009.
Anders et al., “Regulation of the α-Secretase ADAM10 by Its Prodomain and Proprotein Convertases,” The FASEB Journal, Published online (Jun. 27, 2001).
Black et al., “Substrate Specificity and Inducibility of TACE (Tumour Necrosis Factor α-Converting Enzyme) Revisited: the Ala-Val Preference, and Induced Intrinsic Activity,” Biochem. Soc. Symp., vol. 70, pp. 39-52 (2003).
Blobel, “ADAMS: Key Components in EGFR Signalling and Development,” Nature Reviews, Molecular Cell Biology, vol. 6, pp. 32-43 (Jan. 2005).
Budagian et al., “Soluble Axl Is Generated by ADAM10-Dependent Cleavage and Associates with Gas6 in Mouse Serum,” Molecular and Cellular Biology, vol. 25, No. 21, pp. 9324-9339 (Nov. 2005).
Gonzales et al., “Inhibition of the Tumor Necrosis Factor-α-converting Enzyme by Its Pro Domain,” The Journal of Biological Chemistry, vol. 279, No. 30, pp. 31638-31645 (Jul. 23, 2004).
Hart et al., “GPCR-induced migration of breast carcinoma cells depends on both EGFR signal transactivation and EGFR-independent pathways,” Biol. Chem., vol. 386, pp. 845-855 (Sep. 2005).
Janes et al., “Adam Meets Eph: An ADAM Substrate Recognition Module Acts as a Molecular Switch for Ephrin Cleavage in Trans,” Cell, vol. 123, pp. 291-304 (Oct. 21, 2005).
Kassouf et al., “Schedule Dependent Efficacy of Gefitinib and Docetaxel for Bladder Cancer,” The Journal of Urology, vol. 176, pp. 787-792 (Aug. 2006).
Kilmon et al., “Metalloprotease inhibitor-mediated inhibition of mouse immunoglobulin production,” Immunology, vol. 102, pp. 281-288 (2001).
Kyte et al., “A Simple Method for Displaying the Hydropathic Character of a Protein,” J. Mol. Biol., vol. 157, pp. 105-132 (1982).
Lammich et al., “Constitutive and regulated α-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease,” Proc. Natl. Acad. Sci. USA, vol. 96, pp. 3922-3927 (Mar. 1999).
Lemieux et al., “The Low Affinity IgE Receptor (CD23) Is Cleaved by the Metalloproteinase ADAM10,” The Journal of Biological Chemistry, vol. 282, No. 20, pp. 14836-14844 (May 18, 2007).
Ludwig et al., “Metalloproteinase Inhibitors for the Disintegrin-Like Metalloproteinases ADAM10 and ADAM17 that Differentially Block Constitutive and Phorbol Ester-Inducible Shedding of Cell Surface Molecules,” Combinatorial Chemistry & High Throughput Screening, vol. 8, pp. 161-171 (2005).
Maretzky et al., “ADAM10 mediates E-cadherin shedding and regulates epithelial cell—cell adhesion, migration, and β-catenin translocation,” PNAS, vol. 102, Number. 26, pp. 9182-9187 (Jun. 28, 2005).
Milla et al., “Specific Sequence Elements Are Required for the Expression of Functional Tumor Necrosis Factor-α-converting Enzyme (TACE),” The Journal of Biological Chemistry, vol. 274, No. 43, pp. 30563-30570 (Oct. 22, 1999).
Moss et al., “Therapeutic Benefits from Targeting of ADAM Family Members,” Biochemistry, vol. 43, No. 23 (Jun. 15, 2004).
Naus et al. “Identification of Candidate Substrates for Ectodomain Shedding by the Metalloprotease-Disintegrin ADAM8,” Biol. Chem., vol. 387, pp. 337-346 (Mar. 2006).
Pan et al., “Kuzbanian Controls Proteolytic Processing of Notch and Mediates Lateral Inhibition during Drosophila and Vertebrate Neurogenesis,” Cell, vol. 90, pp. 271-280 (Jul. 25, 1997).
Postina et al., “A Disintegrin-Metalloproteinase Prevents Amyloid Plaque Formation and Hippocampal Defects in an Alzheimer Disease Mouse Model,” J. Clin. Invest., vol. 113, pp. 1456-1464 (2004).
Reiss et al., “ADAM10 Cleavage of N-cadherin and Regulation of Cell—Cell Adhesion and β-Catenin Nuclear Signalling,” The EMBO Journal, vol. 24, pp. 742-752 (2005).
Rosenwasser et al., “ Anti-CD23,” Clinical Reviews in Allergy & Immunology, vol. 29, pp. 61-72 (2005).
Sahin et al., “Distinct roles for ADAM10 and ADAM17 in Ectodomain Shedding of Six EGFR Ligands,” Journal of Cell Biology, vol. 164, No. 5, pp. 769-779 (Mar. 1, 2004).
Sanderson et al., “ADAM10 Mediates Ectodomain Shedding of the Betacellulin Precursor Activated by p-Aminophenylmercuric Acetate and Extracellular Calcium Influx,” The Journal of Biological Chemistry, vol. 280, No. 3, pp. 1826-1837 (Jan. 21, 2005).
Wolfsberg et al., “ADAM, a Novel Family of Membrane Proteins Containing A Disintegrin And Metalloprotease Domain: Multipotential Functions in Cell-Cell and Cell-Matrix Interactions,” The Journal of Cell Biology, vol. 131, No. 2, pp. 275-278 (Oct. 1995).
Wolfsberg et al., “Rapid Communication: ADAM, a Widely Distributed and Developmentally Regulated Gene Family Encoding Membrane Proteins with A Disintegrin And Metalloprotease Domain,” Developmental Biology, vol. 169, pp. 378-383 (1995).
Moss Marcia
Zhou Pei
BioZyme, Inc.
Duke University
Jenkins Wilson Taylor & Hunt, P.A.
Rao Manjunath N
Shafer Shulamith H
LandOfFree
Prodomain modulators of ADAM 10 does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Prodomain modulators of ADAM 10, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Prodomain modulators of ADAM 10 will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-4106883