Binding peptides for carcinoembryonic antigen (CEA)

Details Binding peptides for carcinoembryonic antigen (CEA) Binding peptides for carcinoembryonic antigen (CEA)

2005-07-19

2005-07-19

Canella, Karen A. (Department: 1642)

Chemistry: natural resins or derivatives; peptides or proteins;

Peptides of 3 to 100 amino acid residues

C530S326000, C530S350000, C530S387100

Reexamination Certificate

active

06919424

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
Inal, J.M., et al., “Schistosoma TOR (Trispanning Orphan Receptor), a Novel, Antigenic Surface Receptor of the Blood-Dwelling,SchistosomaParasite,”Biochim. 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 Mutatuion in the Human Ortholog of theSaccharomyces cerevisiae ALG 6Gene Causes Carbohydrate-Deficient Glycoprotein Syndrome Type-Ic,Proc. Natl. Acad. Sci. USA96:6982-6987 (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).
Hammarström, S., “The Carcinoembryonic Antigen (CEA) Family: Structures, Suggested Functions and Expression in Normal and Malignant Tissues,”Sem. Cancer Biol.,(9):67-81 (1999).
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: 239-349 (1981).
Merrifield,J. Am. Chem. Soc.,85:2149-2154 (1963).
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 vivoDisassembly 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 laevisMetamorphosis,”Proc. Natl. Acad. Sci. U.S.A., 93(5):1924-1929 (1996).
Cheret, G., et al., “DNA Sequence Analysis of theVPHI-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 Sequencc Includes Potential Regulatory in the 3′ Untranslated Region,”J. Cell Biol., 108(2):729-736 (1989).
Hiromoto, K., et al., “Molecular Cloning of Equine Interlukin-1 α and -β cNDAs,”Vet. Immunol. Immunopathol., 48:221-231 (1995).
Huang, D., et al., “Structural Organization and Splice Variants of thePOLE1Gene 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 genePole1for the mouse DNA Polymearse 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).
Thébault, S., et al., “Molecular Cloning of a Novel Human I-mfa Domain-containing Protein That Differently Regulates 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).

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