Methods of detecting collagen degradation in vivo

Chemistry: analytical and immunological testing – Involving an insoluble carrier for immobilizing immunochemicals

Patent

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

5303879, G01N 33538, C07K 1618

Patent

active

055321690

ABSTRACT:
A method of determining collagen degradation in vivo, comprising quantitating the concentration of a peptide in a body fluid, the peptide being a C-terminal type II collagen telopeptide containing a hydroxylysyl pyridinoline cross-link or a type III collagen telopeptide containing a hydroxylysyl pyridinoline cross-link. The method includes immunometric assays, fluorometric assays, and electrochemical titrations for quantitation. The structures of specific peptides having cross-links and kits for quantitating these peptides in a body fluid are described.

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.
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 Journal, 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 Cartilages 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. Bone 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 al., "Bone Mineral Content of Amenorrheic and Eumenorrheic Athletes," The New England Journal 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, 104:1047-1412 (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(11):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.1 Chain of Human Type I Procollagen. Statistical Evaluation of Structures that are Conserved During Evolution," Biochemistry, 22:5213-5223 (1983).
Goldstein, D., et al., "Simultaneous 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 Cleavage Site," Biochemistry, 18:3416-3422 (1979).
Dakkak, et al., "Modifications de l'hydroxyprolin

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Methods of detecting 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 Methods of detecting collagen degradation in vivo, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Methods of detecting collagen degradation in vivo will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-1506032

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.