Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving antigen-antibody binding – specific binding protein...
Reexamination Certificate
2011-02-22
2011-02-22
Aeder, Sean E (Department: 1642)
Chemistry: molecular biology and microbiology
Measuring or testing process involving enzymes or...
Involving antigen-antibody binding, specific binding protein...
Reexamination Certificate
active
07892752
ABSTRACT:
One can identify and quantify one or more glycosylation markers of cancer by utilizing quantitative HPLC analysis of glycans which have been released from unpurified glycoproteins. The unpurified glycoproteins can be total glycoproteins or a selection of the total glycoproteins. The identified glycosylation marker can be a native glycan or a digestion product which has been segregated and amplified by exoglycosidase digestions. One can utilize the identified glycosylation marker, for example, for diagnosing and/or monitoring cancer in a subject. One can also use the glycosylation marker to identify glycoprotein biomarkers that carry the glycosylation marker. Such biomarkers can also be used for monitoring and/or diagnosing cancer. The biomarker may also be a subset of glycoforms of a glycoprotein that are separated in trains of spots on 2D gel.
REFERENCES:
patent: 4659659 (1987-04-01), Dwek et al.
patent: 2004/0147033 (2004-07-01), Shriver et al.
patent: 2004/0253651 (2004-12-01), Saarinen et al.
patent: 2006/0269979 (2006-11-01), Dwek et al.
patent: 2006/0270048 (2006-11-01), Dwek et al.
patent: WO 02/08760 (2002-01-01), None
patent: WO 03/016464 (2003-02-01), None
patent: WO 2004/066808 (2003-12-01), None
patent: WO 2004/019040 (2004-03-01), None
patent: WO 2004/066808 (2004-08-01), None
Tockman et al (Cancer Res., 1992, 52:2711s-2718s).
Fukuda et al (The Journal of Biological Chemistry, Sep. 1986, 261(27): 12796-12806).
Kannicht et al (Glycobiology, 1999, 9(9): 897-906).
Peracaula et al (Glycobiology, 2003, 13(6): 457-470).
Amano, J. et. al., “Quantitative Conversion of Mucin-Type Sugar chains to Radioactive Oligosaccharides,” Methods Enzymol 179: 261-70, 1989.
Amess et al., “Programmed cell death in sympathetic neurons: a study by two-dimensional polyacrylamide gel electrophoresis using computer image analysis,” Electrophoresis 16: 1255-1267, 1995.
Anumula et al., “Characterization of carbohydrates using highly fluorescent 2- aminobenzoic acid tag following gel electrophoresis of glycoproteins.” Analytical Biochemistry, 275: 236-42, (1999).
Anumula, K. R., “Thematic Review: High-sensitivity and high-resolution methods for glycoprotein analysis.” Analytical Biochemistry, 2000, 283: 17-26.
Axford, John S., “Glycosylation and rheumatic disease,” Biochimica et Biophysica Acta, Oct. 8, 1999, vol. 1455, No. 2-3, pp. 219-229.
Bigge, J. C., et. al. “Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid,” Analytical Biochemistry, 230: 229-38, 1995.
Blass, S., “Novel 68 kDa autoantigen detected by rheumatoid arthritis specific antibodies,” Annals of the Rheumatic Diseases, 54:355-360, 1995.
Block et al., “Use of targeted glycoproteomics to identify serum glycoproteins that correlate with liver cancer in woodchucks and humans.” Proc Natl Acad Sci U S A, 2005, 102: 779-84.
Brawer MK, “Prostate- specific antigen: current status,” CA Cancer J Clin, 49, 264-281, 1999.
Burlingame, A. L., “Characterization of protein glycosylation by mass spectrometry.” Curr Opin Biotechnol 7: 4-10, (1996).
Butler, M., et al. “Detailed glycan analysis of serum glycoproteins of patients with congenital disorders of glycosylation indicates the specific defective glycan processing step and provides an insight into pathogenesis.” Glycobiology 13: 601-22, 2003.
Caesar et al., “Femtomole oligosaccharide detection using a reducing-end derivative and chemical ionization mass spectrometry,” Analytical Biochemistry, 191: 247-52 (1990).
Callewaert et al., “Total serum protein N-glycome profiling on a capillary electrophoresis-microfluidics platform,” Electrophoresis, 2004, 25: 3128-31.
Callewaert et al., “Increased fucosylation and reduced branching of serum glycoprotein N-glycans in all known subtypes of congenital disorder of glycosylation I.” Glycobiology, 2003, 13: 367-375.
Chan et al., “Alpha-fetoprotein variants in a case of pancreatoblastoma,”Ann Clin Biochem37 ( Pt 5): 681-5, 2000.
Ciolczyk-Wierzbicka et al., “The structure of the oligosaccharides of N-cadherin from human melanoma cell lines,” Glycoconjugate Journal, 2004, vol. 20, No. 7-8, pp. 483-492.
Costello, C. E., “Bioanalytic applications of mass spectrometry.” Curr Opin Biotechnol 10: 22-8, 1999.
Davies et al., “Comparison of separation modes of high-performance liquid chromatography for the analysis of glycoprotein- and proteoglycan-derived oligosaccharides.” J Chromatogr A 720: 227-33, 1996.
Despres et. al., “The Sa system: a novel antigen-antibody system specific for rheumatoid arthritis,” J Rheumatol 21:1027-33, 1994.
Diamandis E., “Prostate-Specific antigen: Its Usefulness in Clinical Medicine,” TEM, 9:310-316, 1998.
Dlamandis,Clin. Lab. News1996, 22: 235-239.
Duffy, M.J., “CA15.3 and related mucins as circulating markers in breast cancer,” Ann. Clin. Biochem., 36, 579-586, 1999.
Edwards et. al., “Efficacy of B-cell-targeted therapy with rituximab in patients with rheumatoid arthritis,” N Engl J Med, 350:2572, 2004.
El Rassi, Z., “Recent developments in capillary electrophoresis and capillary electrochromatography of carbohydrate species.” Electrophoresis 20: 3134-44, 1999.
Ey et. al. “Isolation of pure IgG1, IgG2aand IgG2bImmunoglobulins from mouse serum using protein A-Sepharose,”Molecular Immunology, vol. 15, pp. 429, 1978.
Görg et al., “Current two-dimensional electrophoresis technology for proteomics,” Proteomics, 4, 3665-3685, 2004.
Görg et al., “Horizontal SDS-PAGE for IGP-Dalt,” Methods Mol. Biol, 112, 235-244, 1999.
Guile et al., “Analytical and preparative separation of anionic oligosaccharides by weak anion-exchange high-performance liquid chromatography on an inert polymer column.” Analytical Biochemistry, 1994, 222: 231-5.
Guile et al., “Identification of highly fucosylated N-linked oligosaccharides from the human parotid gland,” European Journal of Biochemistry, 1998, 258: 623-656.
Guile et. al., “A rapid high-resolution high-performance liquid chromatographic method for separating glycan mixtures and analyzing oligosaccharide profiles,” Anal. Biochem. 240: 210-26, 1996.
Hardy et al., “High-pH anion-exchange chromatography of glycoprotein-derived carbohydrates,” Methods Enzymol, 230: 208-25, 1994.
Harvey et al., “Proteomic analysis of glycosylation: structural determination of N- and O-linked glycans by mass spectrometry,” Expert Review of Proteomics 2005, Apr. 1, 2005, vol. 2, No. 1, pp. 87-101.
Harvey, D. J., “Matrix-assisted laser desorption/ionization mass spectrometry of carbohydrates,” Mass Spectrom Rev, 1999, 18: 349-450.
Harvey, D. J., “Electrospray mass spectrometry and fragmentation of N-linked carbohydrates derivatized at the reducing terminus,” J Am Soc Mass Spectrum, 2000, 11: 900-915.
Harvey, DJ, “Fragmentation of negative ions from carbohydrates: Part 1; Use of nitrate and other anionic adducts for the production of negative ion electrospray spectra from N-linked carbohydrates,” J. Am. Soc. Mass Spectrum., 2005, 16, 622-630.
Harvey, DJ, “Fragmentation of negative ions from carbohydrates: Part 2, Fragmentation of high-mannose N-linked glycans,” J. Am. Soc. Mass Spectrom., 2005, 16, 631-646.
Harvey, DJ, “Fragmentation of negative ions from carbohydrates: Part 3, Fragmentation of hybrid and complex N-linked glycans,” J. Am. Soc. Mass Spectrom., 2005, 16, 647-659.
Hassfeld et al., “Demonstration of a new antinuclear antibody (anti-RA33) that is highly specific for rheumatoid arthritis,” Arthritis Rheum, 32:1515-1520, 1989.
Huang et al., “Microscale nonreductive release of O-linked glycans for subsequent analysis through MALDI mass spectrometry and
de Llorens Rafael
Dwek Raymond A.
Hamid Umi Marshida Abd
Peracaula Rosa
Radcliffe Catherine M.
Aeder Sean E
Foley & Lardner LLP
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