Chemistry: analytical and immunological testing – Involving immune complex formed in liquid phase
Patent
1991-05-31
1994-06-14
Schwartz, Richard A.
Chemistry: analytical and immunological testing
Involving immune complex formed in liquid phase
530323, 530356, 530413, G01N 33536, C07K 1520
Patent
active
053209702
ABSTRACT:
Methods of determining collagen degradation in vivo, by quantitating the concentration of a peptide in a body fluid, the peptide having the following structure: ##STR1## is hydroxylysyl pyridinoline or lysyl pyridinoline, and J is pyroglutamic acid or glutamine and (Leu) are optional leucines, are disclosed.
Compositions useful in quantitating collagen peptides to determine the rate of bone resorption are prepared by treating bone with a protease, such as collagenase, and purifying the compositions so as to enrich them with peptides capable of binding to the monoclonal antibody MAb-1H11.
REFERENCES:
patent: 3600132 (1971-08-01), Goverde
patent: 4094646 (1978-06-01), Stern et al.
patent: 4312853 (1982-01-01), Timpl
patent: 4371374 (1983-02-01), Cerami et al.
patent: 4504587 (1985-04-01), Timpl et al.
Hartmann et al., Clin. Chem., vol. 36, 1990, pp. 421-426.
Black, et al., "Urinary excretion of the hydroxypyridinium cross links of collagen in patients with rheumatoid arthritis," Annals of the Rheumatic Diseases, 48:641-644 (1989).
Seibel, et al., "Urinary Hydroxy-pyridinium Crosslinks Provide Indices of Cartilage and Bone Involvement in Arthritic Diseases," The Journal of Rheumatology, 16:964-970 (1989).
Baldwin, et al., "Structure of cDNA clones coding for human type II procollagen: The .alpha.1(II) chain is more similar to the .alpha.1(I) chain than two other .alpha. chains of fibrillar collagens," Biochemistry Journal, 262:521-528 (1989).
Ala-Kokko, et al., "Structure of cDNA clones coding for the entire prepro.alpha.1(III) chain of human type III procollagen: Differences in protein structure from type I procollagen and conservation of codon preferences," Biochemistry Jouranl, 260:509-516 (1989).
Seibel, "Komponenten der extrazllularen Gewebematrix als potentielle `Marker` des Bindegewebs-, Knorpel-und Knochenmetabolismus bei Erkrankungen des Bewegungsapparates," Zeitschrift fur Rheumatologie, 48:6-18 (1989).
Dodge and Poole, "Immunohistochemical Detection and Immunochemical Analysis of Type II Collagen Degradation in Human Normal, Rheumatoid, and Osteoarthritic Articular Cartilages and in Explants of Bovine Articular Cartilage Cultured with Interleukin 1," Journal of Clinical Investigation, 83:647-661 (1989).
Niemela, "Radioimmunoassays for Type III Procollagen Amino-Terminal Peptides In Humans," Clinical Chemistry, 31:1301-1304 (1985).
Sangiorgi, et al., "Isolation and partial characterization of the entire human pro.alpha.1(II) collagen gene," Nucleic Acids Research, 13:2207-2225 (1985).
Loidl, et al., "Molecular cloning and carboxyl-propeptide analysis of human type III procollagen," Nucleic Acids Research, 12:9383-9394 (1984).
Wu and Eyre, "Identification of Hydroxypyridinium Cross-Linking Sites in Type II Collagen of Bovine Articular Cartilage," Biochemistry, 23:1850-1857 (1984).
Pierard, et al., "Radioimmunoassay for the Amino-Terminal Sequences of Type III Procollagen in Human Body Fluids Measuring Fragmented Precursor Sequences," Analytical Biochemistry, 141:127-136 (1984).
Rohde, et al., "Radioimmunoassay for type III procollagen peptide and its application to human liver disease," European Journal of Clinical Investigation, 9:451-459 (1979).
Russell, R. G. G., et al., "Biochemical Markers of Bone Turnover in Paget's Disease," Metab. Bond Dis. & Rel. Res., 4 & 5:255-262 (1981).
Drinkwater, B. L., et al., "Bone Mineral Density After Resumption of Menses in Amenorrheic Athletes," JAMA, 256:380-382 (1986).
Drinkwater, B. L., et a., "Bone Mineral Content of Amenorrheic and Eumenorrheic Athletes," The New England Jouranl of Medicine, 331:5; 277-281 (1984).
Fujimoto, D., "Evidence for Natural Existence of Pyridinoline Crosslink in Collagen," Biochemical and Biophysical Research Communications, 93:948-953 (1980).
Yamauchi, M. et al., "A Comparative Study of the Distribution of the Stable Crosslink, Pyridinoline, in Bone Collagens, from Normal, Osteoblastoma, and Vitamin D-Deficient Chicks," Biochemical and Biophysical Research Communications, 102:59-65 (1981).
Kuboki, Y., et al., "Location of the Intermolecular Crosslinks in Bovine Dentin Collagen, Solubilization with Trypsin and Isolation of Cross-Link Peptides Containing Dihydroxylysinonorleucine and Pyridinoline," Biochemical and Biophysical Research Communications, 102:119-126 (1981).
Gunja-Smith, Z. and Boucek, R. J., "Collagen cross-linking compounds in human urine," Biochemical Journal, 197:759-762 (1981).
Tsuchikura, O., et al., "Pyridinoline Fluorescence in Cyanogen Bromide Peptides of Collagen," Biochemical and Biophysical Research Communications, 102:1203-1208 (1981).
Tsuda, M., et al., "Pyridinoline is a Real Moiety of Collagen," Biochemical and Biophysical Research Communications, 104:1407-1412 (1982).
Robins, S. P., "An enzyme-linked immunoassay for the collagen cross-link pyridinoline," Biochemical Journal, 207:617-620 (1982).
Banes, A. J., et al., "Nonmineralized and Mineralized Compartments of Bone: The Role of Pyridinoline in Nonmineralized Collagen," Biochemical and Biophysical Research Communications, 113:975-981 (1983).
Fujimoto, D., et al., "Analysis of Pyridinoline, a Cross-Linking Compound of Collagen Fibers, in Human Urine," J. Biochem., 94:1133-1136 (1983).
Eyre, D. R., et al, "Cross-Linking in Collagen and Elastin," Ann. Rev. Biochem., 53:717-748 (1984).
Light, N. and Bailey, A. J., "Collagen crosslinks: Location of pyridinoline in type I collagen," FEBS 2409, 182:503-508 (1985).
Wu, J-J. and Eyre, D. R., "Fine Powdering Exposes the Mineral-Protected Collagen of Bone to Protease Digestion," Calcif. Tissue Int., 42:243-247 (1988).
Fujimoto, D., et al., "Pyridinoline, A Non-Reducible Crosslink of Collagen, Quantitative Determination, Distribution, and Isolation of a Crosslinked Peptide," Chemical Abstracts 89(1):148, (Sep. 11, 1978).
Black, D., et al., "Quantitative Analysis of the Pyridinium Crosslinks of Collagen in Urine Using Ion-Paired Reversed-Phase High-Performance Liquid Chromatography," Chemical Abstracts 108(21):354, (May 23, 1988).
Fujimoto, D., et al., "Analysis of Pyridinoline, A Cross-Linking Compound of Collagen Fibers, in Human Urine," Chemical Abstracts 99(19):446-447, (Nov. 7, 1983).
Macek, J., et al., "Determination of Collagen Degradation Products in Human Urine in Osteoarthrosis," Chemical Abstracts 108(3):299, (Jan. 18, 1988).
Eyre, D. R., et al., "Quantitation of Hydroxypyridinium Crosslinks in Collagen by High-Performance Liquid Chromatography," Analytical Biochemistry, 137:380-388 (1984).
Robins, S. R., et al., "Measurement of the cross linking compound, pyridinoline, in urine as an index of collagen degradation in joint disease," Annals of the Rheumatic Diseases, 45:969-973 (1986).
Bernard, M. P., et al., "Nucleotide Sequences of Complementary Deoxyribonucleic Acids for the Pro.alpha.l Chain of Human Type I Procollagen. Statistical Evaluation of Structures that are Conserved During Evolution," Biochemistry, 22:5213-5223 (1983).
Goldstein, D., et al., "Simulataneous Measurement of DOPA, DOPAC, and Catecholamines in Plasma by Liquid Chromatography with Electrochemical Detection," ESA Review, vol. II, No. 1, 2-11 (1986).
Chu, M.-L., et al., "Human pro.alpha.1(I) collagen gene structure reveals evolutionary conservation of a pattern of introns and exons," Nature 310(26):337-340 (1984).
Robins, S. P., et al., "Measurement of Hydroxypyridinium Crosslinks of Collagen as an Index of Bone Matrix Degradation," An Abstract of a Paper, Lake Garda, Italy (1987).
Kang, A. H. and Gross, J., "Amino Acid Sequence of Cyanogen Bromide Peptides from the Amino-Terminal Region of Chick Skin Collagen," Biochemistry 9:796-804 (1970).
Highberger, J. H., et al., "The Amino Acid Sequence of Chick Skin Collagen .alpha.1-CB7," Biochemistry 14(13):2872-2881 (1975).
Fietzek, P. P. and Kuhn, K., "The Covalent Structure of Collagen: Amino Acid Sequence of the N-Terminal Region of .alpha.2-CB5 from Rat Skin Collagen," FEBS Letters 36(3):289-291 (1973).
Dixit, S. N., et al., "Covalent Structure of Collagen: Amino Acid Sequence of .alpha.2-CB5 of Chick Skin Collagen Containing the Animal Collagenase Cleavag
Ketter James
Schwartz Richard A.
Washington Research Foundation
LandOfFree
Detection of collagen degradation in vivo does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Detection of collagen degradation in vivo, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Detection of collagen degradation in vivo will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-1248792