Chemistry: natural resins or derivatives; peptides or proteins; – Peptides of 3 to 100 amino acid residues – 25 or more amino acid residues in defined sequence
Reexamination Certificate
2007-06-19
2007-06-19
Wax, Robert A. (Department: 1653)
Chemistry: natural resins or derivatives; peptides or proteins;
Peptides of 3 to 100 amino acid residues
25 or more amino acid residues in defined sequence
C530S350000
Reexamination Certificate
active
10415398
ABSTRACT:
There is disclosed movel mutant IGFBP-3 polypeptides and fragments thereof that have either no binding, or diminished binding to IGFs, yet retain their ability to bind to the human IGFBP-3 receptor (“P4.33”). The present invention provides novel mutant IGFBP-3 nucleic acid sequences, and expression systems. Additional embodiments provide for screening assays for identifying IGFBP-3 receptor antagonists or agonists, methods for modulating IGF-independent IGFBP-3 responses of cells expressing IGFBP-3 receptors, A methods for inducing or potentiating apoptosis of cells expressing IGFBP-3 receptors, methods for treating solid tumors having cells expressing IGFBP-3 receptors, and compositions comprising polypeptides having either no binding, or diminished binding to IGFs, yet retain their ability to bind to the IGFBP-3 receptor.
REFERENCES:
patent: 2004/0253689 (2004-12-01), Rechler
IGFBP-3 protein (Homo sapien) sequence from GenBank. Accession code: P17936; deposited Nov. 1, 1990.
Christiansen et al. “The role of the MoFe protein alpha-125-Phe and beta-235-Phe residues in Azotobacter vinelandii MoFe protein Fe protein interaction”. Journal of Inorganic Biochemistry. 2000. vol. 80, pp. 195-204.
Sorlie et al. “Mechanistic features and structure of the nitrogenase alpha-Gln-195 MoFe protein”. Biochemistry. 2001. vol. 40, pp. 1540-1549.
Buckway et al., Mutation of Three Critical Amino Acids of the N-Terminal Domain of IGF-Binding Protein-3 Essential for High Affinity IGF Binding, J. Clin. Endocrinology & Metabolism 86(10):4943-4950, 2001.
Imai et al., Substitution for hydrophobic amino acids in the N-terminal domains of IGFBP-3 and -5 markedly reduce IGF-I binding and alter their biologic actions, J. Biol. Chem. 275(24):18188-18194, 2000.
Kalus et al., Structure of the IGF-binding domain of the insulin-like growth factor-binding protein-5 (IGFBP-5): implications for IGF and IGF-1 receptor interactions, Embo J. 17(22):6558-6572, 1998.
Hashimoto et al., Binding Sites and Binding Properties of Binary and Temary Complexes of Insulin-like Growth Factor-II (IGF-II), IGF-binding Protein-3, and Acid-labile Subunit, J. Biol. Chem. 272(44):27936-27942, 1997.
Hwa et al., The Insulin-Like Growth Factor-Binding Protein (IGFBP) Superfamily, Endocrine Reviews 20(6):761-787, 1999.
Baxter, Robert C., Insulin-like growth factor (IGF)-binding proteins: interactions with IGFs and intrinsic bioactivites, Am. J. Physiol. Endocrinol. Metab. 278:E967-E976, 2000.
Buckway Caroline K.
Oh Youngman
Rosenfeld Ron G.
Davis Wright Tremaine
Davison Barry L.
Noakes Suzanne M.
Oregon Health & Science University
Wax Robert A.
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