Binding peptides for carcinoembryonic antigen (CEA)

Drug – bio-affecting and body treating compositions – Radionuclide or intended radionuclide containing; adjuvant... – In an organic compound

Reexamination Certificate

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C424S009100, C424S009340, C436S064000, C514S002600, C514S013800, C514S014800, C514S015800

Reexamination Certificate

active

07438890

ABSTRACT:
The present invention provides binding moieties for CEA, which have a variety of uses wherever detecting, isolating or localizing CEA, and particularly CEA as opposed to cross-reactive antigens such as NCA, is advantageous. Particularly disclosed are synthetic, isolated polypeptides capable of binding CEA, which is overexpressed in adenocarcinomas of endodermally derived digestive system epithelia and fetal colon. Such polypeptides and disclosed derivatives are useful, e.g., as imaging agents for CEA-expressing tumors.

REFERENCES:
patent: 5047507 (1991-09-01), Buchegger et al.
patent: 5223409 (1993-06-01), Ladner et al.
patent: 5872215 (1999-02-01), Osbourne et al.
patent: 5912334 (1999-06-01), Kato et al.
patent: 5977315 (1999-11-01), Chatterjee et al.
patent: 1074617 (2001-02-01), None
patent: 9131191 (1997-05-01), None
patent: 2000191697 (2000-07-01), None
patent: WO 92/21364 (1992-12-01), None
patent: WO 95/06067 (1995-03-01), None
patent: WO 96/41172 (1996-12-01), None
patent: WO 99/26961 (1999-06-01), None
patent: WO 99/54436 (1999-10-01), None
patent: WO 00/44908 (2000-08-01), None
patent: WO 01/18250 (2001-03-01), None
patent: WO 01/25427 (2001-04-01), None
patent: WO 01/36632 (2001-05-01), None
patent: WO 01/51512 (2001-07-01), None
patent: WO 01/57270 (2001-08-01), None
patent: WO 01/57274 (2001-08-01), None
patent: WO 01/57275 (2001-08-01), None
patent: WO 01/75068 (2001-10-01), None
Duffy, Critical Reviews in Clinical Laboratory Sciences, 2001, vol. 38, pp. 225-261.
Schlom (‘Monoclonal Antibodies: They're More and Less Than You Think’, In: Molecular foundations in Oncology, 1991, Broder, Ed., pp. 95-134).
Johnson and Tracey, ‘Peptide and Protein Drug Delivery’, In: Encyclopedia of Controlled Drug Delivery, vol. 2, 1999, pp. 816-833.
Beauchemin et al.,Mol. Cell. Biol., 7:3221-3230 (1987).
Berche et al.,Br. Med. J., 285: 1447-1451 (1982).
Gold and Freedman,J. Exp. Med., 121: 439-462 (1965).
Hengerer et al.,Biotechniques, 26(5): 956-964 (1999).
Mach et al.,Immun. Today, 2: 239-249 (1981).
Merrifield,J. Am. Chem. Soc., 85:2149-2154 (1963).
Inal, J.M., et al., “Schistosoma TOR (Trispanning Orphan Receptor), a Novel, Antigenic Surface Receptor of the Blood-Dwelling,SchistosomaParasite,” Biochem. Biophys. Acta. 1445:283-298 (1999).
Lawler, J. and Hynes, R.O., “The Structure of Human Thrombospondin, an Adhesive Glycoprotein with Multiple Calcium-Binding Sites and Homologies with Several Different Proteins,”J. Cell. Biol. 103:1635-1648 (1986).
Imbach, T., et al., A Mutation in the Human Ortholog of theSaccharomyces cerevisiae ALG6Gene Causes Carbohydrate-Deficient Glycoprotein Syndrome Type-Ic, Proc. Natl. Acad. Sci. USA 96:6982-6987 (1999).
Chatterjee, S.K., et al., “Molecular Mimicry of Carcinoembryonic Antigen by Peptides Derived from the Structure of an Anti-Idiotype Antibody,”Cancer Res. 58:1217-1224 (1998).
Aljinovic, G., and Pohl, T.M., “Sequence and Analysis of 24 kb on Chromosome II ofSaccharomyces cerevisiae,” Yeast, 11(5):475-479 (1995).
Amerik, A.Y., et al., “In vivo Disassembly of Free Polyubiquitin Chains by Yeast Ubp14 Modulates Rates of Protein Degradation by the Proteasome,”EMBO J., 16(16):4826-4838 (1997).
Brown, D.D., et al., “The Thyroid Hormone-induced Tail Resorption Program DuringXenopus IaevisMetamorphosis,”Proc. Natl. Acad. Sci. U.S.A., 93(5):1924-1929 (1996).
Cheret, G., et al., “DNA Sequence Analysis of theVPH1-SNF2Region on Chromosome XV ofSaccharomyces cerevisiae,” Yeast, 12:1059-1064 (1996).
Duharcourt, S., et al., “Homology-Dependent Maternal Inhibition of Developmental Excision of Internal Eliminated Sequences inParamecium tetraurelia,” Mol. Cell Biol., 18(12):7075-7085 (1998).
Hennessy, S.W., et al., “Complete Thrombospondin mRNA Sequence Includes Potential Regulatory in the 3′ Untranslated Region,”J. Cell Biol., 108(2):729-736 (1989).
Hirotomo, K., et al., “Molecular Cloning on Equine Interleukin-1α and -β cDNAs,”Vet. Immunol. Immunopathol., 48:221-231 (1995).
Huang, D., et al., “Structural Organization and Splice Variants of thePOLEIGene Encoding the Catalytic Subunit of Human DNA Polymerase ε,”Biochem. J., 339(3):657-665 (1999).
Huang, D., et al., “cDNA and Structural Organization of the genePolelfor the mouse DNA Polymerase ε Catalytic Subunit,”Biochim. Biophys. Acta, 1445(3):363-371 (1999).
Kato, H., et al., “Identification of an Alternatively Spliced Transcript of Equine Interleukin-1 β,”Gene, 177:11-16 (1996).
Kawano, T., et al., “Structures of Insulin-like Peptides of the NematodeCaenorhabditis elegans,” Peptide Science, 35:117-120 (1998).
Kawano, T., et al., “Molecular Cloning and Characterization of a New Insulin/IGF-like Peptide of the NematodeCaenorhabditis elegans,” Biochem. Biophys. Res. Commun., 273(2):431-436 (2000).
Kesti, T., et al., “Molecular Cloning of the cDNA for the Catalytic Subunit of Human DNA Polymerase ε,”J. Biol. Chem., 268(14):10238-10245 (1993).
Li, Y., et al., “Purification, cDNA Cloning, and Gene Mapping of the Small Subunit of Human DNA Polymerase ε,”J. Biol. Chem., 272(51):32337-32344 (1997).
Nielsen, E., et al., “Cysteine Residue Periodicity is a Conserved Structural Feature of Variable Surface Proteins fromParamecium tetraurelia,” J. Mol. Biol., 222(4):835-841 (1991).
Okinaka, R.T., et al., “Sequence and Organization of pX01, the LargeBacillus anthracisPlasmid Harboring the Anthrax Toxin Genes,”J. Bacteriol., 181(20):6509-6515 (1999).
Prat, A., “Conserved Sequences Flank Variable Tandem Repeats in two Alleles of the G Surface Protein ofParamecium primaurelia,” J. Mol. Biol., 211(3):521-535 (1990).
Prat, A., et al., “Nucleotide Sequence of theParamecium primaureliaG Surface Protein,”J. Mol. Biol., 189(1):47-60 (1986).
Tachikawa, H., et al., “Isolation and Characterization of a Yeast Gene,MPD1, the Overexpress of Which Suppresses Inviability Caused by Protein Disulfide Isomerase Depletion,”FEBS Lett., 369:212-216 (1995).
Theébault, S., et al., “Molecular Cloning of a Novel Human I-mfa Domain-containing Protein That Differently Regualtes Human T-cell Leukemia Virus Type I and HIV-1 Expression,”J. Biol. Chem., 275(7):4848-4857 (2000).
Ueno, A., et al., “cDNA Cloning of Bovine Thrombospondin 1 and its Expression in Odontoblasts and Predentin,”Biochim. Biophys. Acta, 1382(1):17-22 (1998).
Wang, H., et al., “Genetic Diversity of Hantaviruses Isolated in China and Characterization of Novel Hantaviruses Isolated fromNiviventer confucianusandRattus rattus,” Virology, 278(2):332-345 (2000).
Hammarström, S., “The Carcinoembryonic Antigen (CEA) Family: Structures, Suggested Functions and Expression in Normal and Malignant Tissues,”Sem. Cancer Biol., (9):67-81 (1999).

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