Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues – Scleroproteins – e.g. – fibroin – elastin – silk – etc.
Reexamination Certificate
2006-05-16
2006-05-16
Patterson, Jr., Charles L. (Department: 1652)
Chemistry: natural resins or derivatives; peptides or proteins;
Proteins, i.e., more than 100 amino acid residues
Scleroproteins, e.g., fibroin, elastin, silk, etc.
C435S189000, C435S068100
Reexamination Certificate
active
07045600
ABSTRACT:
The present invention relates to the gene PLOD2 which codes for telopeptide lysyl hydroxylase (TLH). This enzyme converts telopeptidyl Lys into telopeptidyl Hyl, that can subsequently be converted into hydroxyallysine cross-links. Collagen with hydroxyallysine cross-links shows a higher resistance to degradation by proteinases than collagen with cross-links derived from allysine.In one aspect, the invention provides methods and compositions to prepare collagenous materials with varying biodegradation rates by varying the ratio of hydroxyallysine cross-links over allysine cross-links. In another aspect, the invention provides methods and compositions to lower the ratio of hydroxyallysine cross-links over allysine cross-links in fibrotic processes, in order to obtain a collagenous network that is more easy to degrade. Furthermore, the invention provides methods to diagnose and/or monitor fibrotic processes by measuring mRNA levels of PLOD2, by measuring protein levels of the translated mRNA, and/or by measuring enzymatic activity levels of TLH. The invention also provides the description of a high through-put system facilitating the screening of antagonists of telopeptide lysyl hydroxylase.
REFERENCES:
R.A.Bank et al.; Defective Collagen Crosslinking in Bone, but not in Ligament or Cartilage, in Bruck Syndrome: Indications for a Bone-specific Telopeptide Lysyl Hydroxylase on Chromosome 17; Proc. Natl.Acad.Sci USA vol. 96, Feb. 1999, pp. 1054-1058.
R.A. Bank et al.; The Molecular Defect in/Bruck Syndrome: Evidence for Tissue-Specific Telopeptide Lysyl Hydroxylases; Official Journal of the International Bone and Mineral Society; 1998 Program and Abstracts from Second Joint Meeting; SA066, p. S543.
R.J.Fernandes et al.; Post-Translational Overmodification of Collagen Expressed by SAOS-2-Osteoblast-like Cells; 44th Annual Meeting, Orthopaedic Research Society, Mar. 16-19, 1998, p. 933.
R.A. Banks et al.; The Bruck Syndrome Evidence for Tissue-Specific Telopeptidyl Lysyl Hydroxylases; 44th Annual Meeting, Orthopaedic Research Society, Mar. 16-19, 1998; p. 324.
R.Myllylä et al.; Molecular Cloning of Chick Lysyl Hyydroxylase; The Journal of Biological Chemistry, vol. 266, No. 5, Feb. 15, 1991; pp. 2805-2810.
R. Myllylä et al.; Ascorbate Is Consumed Stoichiometrically in the Uncoupled Reactions Catalyzed by Prolyl 4-Hydroxylase and Lysyl Hydroxylase; The Journal of Biological Chemistry, vol. 259, No. 9, May 10, 1984, pp. 5403-5405.
J.Brinckmann et al.; Ehlers-Danlos Syndrome Type VI: Lysyl Hydroxylase Deficiency Due to a Novel Point Mutation (W612C),Arch Dermatol Res (1998) vol. 290; pp. 181-186.
K. Majamaa et al.; Differences Between Collagen Hydroxylases and 2-oxoglutarate Dehydrogenase in their Inhibition by Structural Analogues of 2-oxoglutarate; Biochem. J. (1985) vol. 229; pp. 127-133.
K. Kivirikko et al; Recent Developments in Posttranslational Modification: Intracellular Processing; Methods in Enzymology, vol. 144, 1987, pp. 96-114.
M.J. Barnes et al.; Hydroxylysine in the N-Terminal Telopeptides of Skin Collagen from Chick Embryo and Newborn Rat; Biochem. J. (1971) vol. 125; pp. 925-928.
M.J. Barnes et al.; Hydroxylysine in the N-Terminal Regions of α1and α2-Chains of Various Collagens; Biochem.J., vol. 125, 1971; pp. 433-437.
R. Myllylä et al.; Modification of Vertebrate and Algal Proly 4-Hydroxylases and Vertebrate Lysyl Hydroxylase by Diethyl Pyrocarbonate; Biochem. J. vol. 286, 1992, pp. 923-927.
P.M.Royce et al.; Failure of Highly Purified Lysyl Hydroxylase to Hydoxylate Lysyl Residues in the Non-Helical Regions of Collagen; Biochem. J. vol. 230, 1985, pp. 475-480.
L.Risteli et al.; Preferential Hydroxylation of Type IV Collagen by Lysyl Hydroxylase from Ehlers-Danlos Syndrome Type VI Fibroblasts; Biochemical and Biophysical Research Communications, vol. 96, No. 4 Oct. 31, 1980, pp. 1778-1784.
A.Ihrne et al.; Ehlers-Danlos Syndrome Type VI: Collagen Type Specificity of Defective Lysyl Hydroxylation in Various Tissues; The Journal of Investigative Dermatology vol. 83, No. 3, 1984, pp. 161-165.
J.Chang et al.; Urinary Pyridinoline Cross-links in Ehlers-Danlos Syndrome Type VI; Am. J. Hurn. Genet. vol. 57, 1995, pp. 1505-1508.
H.N. Yeowell et al.; Sequence Analysis of a cDNA for Lysyl Hydroxylase Isolated from Human Skin Fibroblasts from a Normal Donor: Differences from Human Placental Lysyl Hydroxylase cDNA; The Journal of Investigative Dermatology, Inc.0022-202X/94/S07.00 1994, pp. 382-384.
S. Murad et al.; Structure-Activity Relationship of Minoxidil Analogs as Inhibitors of Lysyl Hydroxylase in Cultured Fibroblasts; Archives of Biochemistry and Biophysics, vol. 292, No. 1, Jan. 1992, pp. 234-238.
J. Hanada et al.; Inhibition of Cultured Human RPE Cell Proliferation and Lysyl Hydroxylase Activity in Hydroxy Derivatives of Minoxidil; Investigative Ophithalmology & Visual Science, vol. 35, No. 2, Feb. 1994, pp. 463-469.
J. Handa et al.; Minoxidil Inhibits Ocular Cell Proliferation and Lysyl Hydroxylase Activity; Investigative Ophithalmology & Visual Science, vol. 34, No. 3 Mar. 1993, pp. 567-575.
T. Hautala et al.; Minoxidil Specifically Decreases the Expression of Lysine Hydroxylase in Cultured Human Skin Fibroblasts; Biochem. J. vol. 283, 1992, pp. 51-54.
K. Passoja et al.; Identification of Arginine-700 as the Residue That Binds the C-5 Carboxyl Group of 2-Oxoglutarate in Human Lysyl Hydroxylase 1; Federation of European Biochemical Societies Letters 434, 1998, pp. 145-148.
T. Hautala et al.; Cloning of Human Lysyl Hydroxylase: Complete cDNA-Derived Amino Acid Sequence and Assignment of the Gene (PLOD) to Chromosome 1p36.6-p36.2; Genomics 13, 1992, pp. 62-69.
K. Passoja et al.; Cloning and Characterization of a Third Human Lysyl Hydroxylase Isoform; Proc. Natl. Acad. Sci, USA, vol. 95, Sep. 1998, pp. 10482-10486.
M. Valtavaara et al.; Cloning and Characterization of a Novel Human Lysyl Hydroxylase Isoform Highly Expressed in Pancreas and Muscle; The Journal of Biological Chemistry, vol. 272, No. 11, Mar. 14, 1997, pp. 6831-6834.
A. Pirskanen et al.; Site-directed Mutagenesis of Human Lysyl Hydroxylase Expressed in Insect Cells; The Journal of Biologifal Chemistry, vol. 271, No. 16, Apr. 19, 1996, pp. 9398-9402.
M. Valtavaara et al.; Primary Structure, Tissue Distribution, and Chromosomal Localization of a Novel Isoform of Lysyl Hydroxylase (Lysyl Hydroxylase 3); The Journal of Biological Chemistry, vol. 273, No. 21, May 22, 1998, pp. 12881-12886.
B. Krol et al.; The Expression of a Functional, Secreted Human Lysyl Hydroxylase in a Baculovirus System; The Journal of Investigative Dermatology, Inc., 0022-202X/96, 1996, pp. 11-16.
J. Gerriets et al.; Tendon Hypertrophy is Associated witH Increased Hydroxylation of Nonhelical Lysine Residues at Two Specific Cross-linking Sites in Type 1 Collagen; The Journal of Biological Chemistry, vol. 268, No. 34, Dec. 5, 1993, pp. 25553-25560.
L. Forrest et al.; A comparison Between the Reducible Intermolecular Crosslinks of the Collagens from Mature Dermis and Young Dermal Scar Tissue of the Guinea Pig; Biochemical and Biophysical Research Communications, vol. 46, No. 5, 1972, pp. 1776-1781.
D. Cannon et al.; Collagen Cross-linking in Corneal Scar Formation; Biochimica et Biophysica Acta. 412 (1975) pp. 18-25.
K. Reiser et al.; A Molecular Marker for Fibrotic Collagen in Lungs of Infants with Respiratory Distress Syndrome; Biochemical Medicine and Metabolic Biology, vol. 37, 1987; pp. 16-21.
J. Last et al.; Hydroxylation of Collagen by Lungs of Rats Administered Bleomycin; American Journal of Respiratory Cell and Molecular Biology, vol. 2, 1990, pp. 543-548.
J. Last et al.; Collagen Cross-linking in Adult Patients with Acute and Chronic Fibrotic Lung Disease; Department of Internal Medicine, School of Medicine and California Primate Research Center, Univeristy of California, et al.; Mar. 14, 1989, pp. 307-313.
T. Morigunchi et al.; Crosslink of Collagen in Hypertrophic Scar; The Journal of Investigative Dermatology, vol. 72, 1979, pp. 143-145.
S. Ricard-Blum et al.; Mechanism of Colllagen Network Sta
Bank Rudolf Antonius
te Koppele Johannes Maria
van der Slot Annemarie Jozefien
Zuurmond Anne-Marie
Nederlandse Organisatie voor Toegepastnatuur-Wetenschappelijk On
Norris McLaughlin & Marcus PA
Patterson Jr. Charles L.
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