WO2004099784A3 - Method for determining a tissue degradation process by detection of fibromodulin neoepitopes - Google Patents

Method for determining a tissue degradation process by detection of fibromodulin neoepitopes Download PDF

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Publication number
WO2004099784A3
WO2004099784A3 PCT/EP2004/004886 EP2004004886W WO2004099784A3 WO 2004099784 A3 WO2004099784 A3 WO 2004099784A3 EP 2004004886 W EP2004004886 W EP 2004004886W WO 2004099784 A3 WO2004099784 A3 WO 2004099784A3
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WO
WIPO (PCT)
Prior art keywords
fibromodulin
neoepitopes
determining
degradation process
tissue degradation
Prior art date
Application number
PCT/EP2004/004886
Other languages
French (fr)
Other versions
WO2004099784A2 (en
Inventor
Dick Heinegaard
Leif Dahlberg
Patrick Oennerfjord
Terrence Heathfield
Original Assignee
Anamar Medical Ab
Dick Heinegaard
Leif Dahlberg
Patrick Oennerfjord
Terrence Heathfield
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Anamar Medical Ab, Dick Heinegaard, Leif Dahlberg, Patrick Oennerfjord, Terrence Heathfield filed Critical Anamar Medical Ab
Publication of WO2004099784A2 publication Critical patent/WO2004099784A2/en
Publication of WO2004099784A3 publication Critical patent/WO2004099784A3/en

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    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
    • C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
    • C07K5/08—Tripeptides
    • C07K5/0819—Tripeptides with the first amino acid being acidic
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
    • C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
    • C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
    • C07K14/4725—Proteoglycans, e.g. aggreccan
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
    • C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
    • C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
    • C07K5/08—Tripeptides
    • C07K5/0802—Tripeptides with the first amino acid being neutral
    • C07K5/0804—Tripeptides with the first amino acid being neutral and aliphatic
    • C07K5/0806—Tripeptides with the first amino acid being neutral and aliphatic the side chain containing 0 or 1 carbon atoms, i.e. Gly, Ala
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
    • C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
    • C07K5/08—Tripeptides
    • C07K5/0802—Tripeptides with the first amino acid being neutral
    • C07K5/0804—Tripeptides with the first amino acid being neutral and aliphatic
    • C07K5/0808—Tripeptides with the first amino acid being neutral and aliphatic the side chain containing 2 to 4 carbon atoms, e.g. Val, Ile, Leu
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
    • C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
    • C07K5/08—Tripeptides
    • C07K5/0802—Tripeptides with the first amino acid being neutral
    • C07K5/0804—Tripeptides with the first amino acid being neutral and aliphatic
    • C07K5/081—Tripeptides with the first amino acid being neutral and aliphatic the side chain containing O or S as heteroatoms, e.g. Cys, Ser
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
    • C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
    • C07K5/08—Tripeptides
    • C07K5/0821—Tripeptides with the first amino acid being heterocyclic, e.g. His, Pro, Trp
    • C07K5/0823—Tripeptides with the first amino acid being heterocyclic, e.g. His, Pro, Trp and Pro-amino acid; Derivatives thereof
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
    • C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
    • C07K5/10—Tetrapeptides
    • C07K5/1002—Tetrapeptides with the first amino acid being neutral
    • C07K5/1005—Tetrapeptides with the first amino acid being neutral and aliphatic
    • C07K5/1008—Tetrapeptides with the first amino acid being neutral and aliphatic the side chain containing 0 or 1 carbon atoms, i.e. Gly, Ala
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
    • C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
    • C07K5/10—Tetrapeptides
    • C07K5/1002—Tetrapeptides with the first amino acid being neutral
    • C07K5/1005—Tetrapeptides with the first amino acid being neutral and aliphatic
    • C07K5/1013—Tetrapeptides with the first amino acid being neutral and aliphatic the side chain containing O or S as heteroatoms, e.g. Cys, Ser
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
    • C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
    • C07K5/10—Tetrapeptides
    • C07K5/1002—Tetrapeptides with the first amino acid being neutral
    • C07K5/1016—Tetrapeptides with the first amino acid being neutral and aromatic or cycloaliphatic
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
    • C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
    • C07K5/10—Tetrapeptides
    • C07K5/1021—Tetrapeptides with the first amino acid being acidic
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
    • G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
    • G01N33/6887—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids from muscle, cartilage or connective tissue
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides

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  • Chemical & Material Sciences (AREA)
  • Organic Chemistry (AREA)
  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Molecular Biology (AREA)
  • Biochemistry (AREA)
  • General Health & Medical Sciences (AREA)
  • Medicinal Chemistry (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Biophysics (AREA)
  • Genetics & Genomics (AREA)
  • Engineering & Computer Science (AREA)
  • Immunology (AREA)
  • Biomedical Technology (AREA)
  • Hematology (AREA)
  • Urology & Nephrology (AREA)
  • Microbiology (AREA)
  • Physics & Mathematics (AREA)
  • Biotechnology (AREA)
  • Toxicology (AREA)
  • Zoology (AREA)
  • Gastroenterology & Hepatology (AREA)
  • Food Science & Technology (AREA)
  • Cell Biology (AREA)
  • Analytical Chemistry (AREA)
  • General Physics & Mathematics (AREA)
  • Pathology (AREA)
  • Peptides Or Proteins (AREA)
  • Investigating Or Analysing Biological Materials (AREA)
  • Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)

Abstract

A method for determining a tissue degradation process by detection of fibromodulin neoepitopes, antibodies against fibromodulin neoepitopes and fragments and peptides containing fibromodulin neoepitopes for generation of such antibodies are described. The method for determining a tissue degradation process comprises detecting in a sample the presence of one or more neoepitopes of mammalian fibromodulin that appear after cleavage of fibromodulin at one or more sites between position 20 and 90. The invention also relates to methods for measuring enzymatic cleavage of fibromodulin and for inhibiting the cleavage of fibromodulin. Furthermore, the invention relates to medical use of compounds inhibiting cleavage of fibromodulin.
PCT/EP2004/004886 2003-05-06 2004-05-05 Method for determining a tissue degradation process by detection of fibromodulin neoepitopes WO2004099784A2 (en)

Applications Claiming Priority (4)

Application Number Priority Date Filing Date Title
US46887903P 2003-05-06 2003-05-06
DKPA200300684 2003-05-06
US60/468,879 2003-05-06
DKPA200300684 2003-05-06

Publications (2)

Publication Number Publication Date
WO2004099784A2 WO2004099784A2 (en) 2004-11-18
WO2004099784A3 true WO2004099784A3 (en) 2005-05-26

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ID=33436000

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Application Number Title Priority Date Filing Date
PCT/EP2004/004886 WO2004099784A2 (en) 2003-05-06 2004-05-05 Method for determining a tissue degradation process by detection of fibromodulin neoepitopes

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Families Citing this family (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
GB0505641D0 (en) * 2005-03-18 2005-04-27 Anamar Medical Ab Treatment of autoimmune and inflamatory diseases
CA2763466C (en) * 2009-05-26 2019-02-26 B. Chia Soo Fibromodulin peptide
GB201318728D0 (en) * 2013-10-23 2013-12-04 Mologic Ltd Detection of cleavage activity of an enzyme
JP7191386B2 (en) * 2017-02-24 2022-12-19 リポトゥルー，エセ．エレ． Peptides and compositions for use in cosmetics
WO2018209178A1 (en) * 2017-05-11 2018-11-15 The Research Foundation For The State University Of New York Method and kit for determining the presence of monosodium urate crystals in joint synovial fluid
CN113087773B (en) * 2021-04-29 2022-02-18 安徽国肽生物科技有限公司 Yak bone peptide with blood sugar reducing and antioxidant functions and preparation method thereof

Citations (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5935796A (en) * 1995-06-30 1999-08-10 The University Of Melbourne Diagnostic methods and compositions relating to the proteoglycan proteins of cartilage breakdown
EP1033401A2 (en) * 1999-02-26 2000-09-06 Genset Expressed sequence tags and encoded human proteins
US6277812B1 (en) * 1988-06-28 2001-08-21 The Burnham Institute Methods for inhibiting TGF-β activity

Patent Citations (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US6277812B1 (en) * 1988-06-28 2001-08-21 The Burnham Institute Methods for inhibiting TGF-β activity
US5935796A (en) * 1995-06-30 1999-08-10 The University Of Melbourne Diagnostic methods and compositions relating to the proteoglycan proteins of cartilage breakdown
EP1033401A2 (en) * 1999-02-26 2000-09-06 Genset Expressed sequence tags and encoded human proteins

Non-Patent Citations (8)

* Cited by examiner, † Cited by third party
Title
ANTONSSON P ET AL: "STRUCTURE AND DEDUCED AMINO ACID SEQUENCE OF THE HUMAN FIBROMODULIN GENE", BIOCHIMICA ET BIOPHYSICA ACTA, AMSTERDAM, NL, vol. 1174, no. 2, 1993, pages 204 - 206, XP001112988, ISSN: 0006-3002 *
GANU VISHWAS ET AL: "Inhibition of interleukin-1alpha-induced cartilage oligomeric matrix protein degradation in bovine articular cartilage by matrix metalloproteinase inhibitors", ARTHRITIS AND RHEUMATISM, vol. 41, no. 12, December 1998 (1998-12-01), pages 2143 - 2151, XP002151898, ISSN: 0004-3591 *
HEATHFIELD TERRENCE F ET AL: "Cleavage of fibromodulin in cartilage explants involves removal of the N-terminal tyrosine sulfate-rich region by proteolysis at a site that is sensitive to matrix metalloproteinase-13.", JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 279, no. 8, 20 February 2004 (2004-02-20), pages 6286 - 6295, XP002300001, ISSN: 0021-9258 *
HUGHES C E ET AL: "MONOCLONAL ANTIBODIES THAT SPECIFICALLY RECOGNIZE NEOEPITOPE SEQUENCES GENERATED BY 'AGGRECANASE' AND MATRIX METALLOPROTEINASE CLEAVAGE OF AGGRECAN: APPLICATION TO CATABOLISM IN SITU AND IN VITRO", BIOCHEMICAL JOURNAL, PORTLAND PRESS, LONDON, GB, vol. 305, 1 February 1995 (1995-02-01), pages 799 - 804, XP000828196, ISSN: 0264-6021 *
ROUGHLEY P J ET AL: "Changes with age in the structure of fibromodulin in human articular cartilage.", OSTEOARTHRITIS AND CARTILAGE / OARS, OSTEOARTHRITIS RESEARCH SOCIETY. ENGLAND SEP 1996, vol. 4, no. 3, September 1996 (1996-09-01), pages 153 - 161, XP008026636, ISSN: 1063-4584 *
SANDY J D ET AL: "ANALYSIS OF THE CATABOLISM OF AGGRECAN IN CARTILAGE EXPLANTS BY QUANTITATION OF PEPTIDES FROM THE THREE GLOBULAR DOMAINS", JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 266, no. 13, 1991, pages 8198 - 8205, XP001205113, ISSN: 0021-9258 *
SANDY J D ET AL: "CATABOLISM OF AGGRECAN IN CARTILAGE EXPLANTS IDENTIFICATION OF A MAJOR CLEAVAGE SITE WITHIN THE INTERGLOBULAR DOMAIN", JOURNAL OF BIOLOGICAL CHEMISTRY, AMERICAN SOCIETY OF BIOLOGICAL CHEMISTS, BALTIMORE, MD, US, vol. 266, no. 14, 15 May 1991 (1991-05-15), pages 8683 - 8685, XP000571607, ISSN: 0021-9258 *
SZTROLOVICS R ET AL: "Resistance of small leucine-rich repeat proteoglycans to proteolytic degradation during interleukin-1-stimulated cartilage catabolism.", THE BIOCHEMICAL JOURNAL. ENGLAND 1 MAY 1999, vol. 339 ( Pt 3), 1 May 1999 (1999-05-01), pages 571 - 577, XP002267840, ISSN: 0264-6021 *

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