124
Views
17
CrossRef citations to date
0
Altmetric
Review

Inhibition of procollagen C-proteinase: fibrosis and beyond

&
Pages 1185-1197 | Published online: 25 Feb 2005

Bibliography

  • SCOTT IC, BLITZ IL, PAPPANO WN et al.: Mammalian BMP-1/tolloid-related metalloproteinases, including novel family member mammalian tolloid-like 2, have differential enzymatic activities and distributions of expression relevant to patterning and skeletogenesis. Dev. Biol. (1999) 213(2):283–300.
  • TAKAHARA K, LYONS GE, GREENSPAN DS: Bone morphogenetic protein-1 and a mammalian tolloid homologue (mT1d) are encoded by alternatively spliced transcripts which are differentially expressed in some tissues. J. Biol. Chem. (1994) 269(51):32572–32578.
  • PROCKOP DJ, SIERON AL, LI 5: Procollagen N-proteinase and procollagen C-proteinase. Two unusual metalloproteinases that are essential for procollagen processing probably have important roles in development and cell signaling. Matrix Biol. (1998) 16:399–408.
  • •Useful review of the discovery and early evaluation of PCP and PNP.
  • LAPIERE CM, LENARERS A, KOHN ID: Procollagen peptidase: an enzyme excising the coordination peptides of procollagen. Proc. Natl. Acad. Sci USA (1971) 68:3054–3058.
  • HOJIMA Y, VAN DER REST M, PROCKOP DJ: Type I procollagen carboxy-terminal proteinase from chick embryo tendons. Purification and characterization: J. Bin/. Chem. (1985) 260:15996–16003.
  • KESSLER E, ADAR R: Type I procollagen C-proteinase from mouse fibroblasts. Purification and demonstration of a 55kD enhancer glycoprotein. Ear: Biochem. (1989) 186:115–121.
  • LI S, SIERON AL, FERTALA A, HOJIMAY, ARNOLD WV: The C-proteinase that processes procollagens to fibrillar collagens is identical to the protein previously identified as bone morphogenic protein-1. Proc. Natl. Acad. Sci. USA (1996) 93:5127–5130.
  • TAKAHARA K, BREVARD R, HOFFMAN GG, SUZUKI N, GREENSPAN DS: Characterization of a novel gene product (mammalian tolloid-like) with high sequence similarity to mammalian tolloid/bone morphogenetic protein-1. Genomics (1996) 34:157–165.
  • WOZNEY JM, ROSEN V, CELESTE AJ et al.: Novel regulators of bone formation: molecular clones and activities. Science (1988) 242:1528–1534.
  • KESSLER E, TAKAHARA K, BINIAMINOV L, BRUSEL M, GREENSPAN DS: Bone morphogenetic protein-1: the Type I procollagen C-proteinase. Science (1996) 271:360–362.
  • WOLFMAN NM, MCPHERRON AC, PAPPANO WN et al.: Activation of the latent myostatin by the BMP/tolloid family of metalloproteinases. Proc. NatL Acad. ScL USA (2003) 100(26):15842–15846.
  • MULLINS MC: Holy tolloido - tolloid cleaves SOG/chordin to free DPP/BMPs. Trends Genet. (1998) 14(4):127–129.
  • HARTIGAN N, GARRIGUE-ANTAR L, KADLER KE: Bone morphogenetic protein-1 (BMP-1) identification of the minimal domain structure for procollagen C-proteinase activity. J. Biol. Chem. (2003) 278(20):18045–18049.
  • GARRIGUE-ANTAR L, BARKER C, KADLER KE: Identification of amino acid residues in bone morphogenetic protein-1 important for procollagen C-proteinase activity. J. Biol. Chem. (2001) 276(28):26237–26242.
  • BOND JS, BEYNON RJ: The astacin family of metalloendopeptidases. Protein Sci. (1995) 4:1247–1261.
  • •Useful review article covering the astacin family of N-proteinase.
  • GOMIS-RUTH FX, STOCKER W, HUBER R, ZWILLING R, BODE W: Refined 1.8 A X-ray crystal structure of Astacin, a zinc-endopeptidase from the crayfish Astacus astacus L.Biol. (1993) 229:945–968.
  • GRAMS F, DIVE V, YIOTAKIS A, YIALLOUROS I, VASSILIOU S, ZWILLING R et al.: Structure of astacin with transition-state analogue inhibitor. Nat. Smart. Biol. (1996) 3:671–675.
  • LEE S, SOLOW-CORDERO DE, KESSLER E, TAKAHARA K, GREENSPAN DS: Transforming growth factor-I3 regulation of bone morphogenetic protein- l/procollagen C-proteinase and related proteins in fibrogenic cells and keratinocytes. Biol. Chem. (1997) 272 (30) : 19059–19066.
  • LEIGHTON M, KADLER KE: Paired basic/furin-like proprotein convertase cleavage of pro-BMP-1 in the trans-Golgi Network. J. Biol. Chem. (2003) 278 (20) :18478–18484.
  • GARRIGUE-ANTAR L, HARTIGAN N, KADLER KE: Post-translational modification of bone morphogenetic protein-1 is required for secretion and stability of the protein. J Biol. Chem. (2002) 277(45):43327–43334.
  • STEIGLITZ BM, KEENE DR, GREENSPAN DS: PCOLCE2 encodes a functional procollagen c-proteinase enhancer (PCPE2) that is. a collagen-binding protein differing in distribution of expression and post-translational modification from the previously described PCPEl. Biol Chem. (2002) 277 (51):49820–49830.
  • RICARD-BLUM S, BERNOCCO S, FONT B et al.: Interaction properties of the procollagen c-proteinase enhancer protein shed light on the mechanism of stimulation of VMP-1. J. Biol. Chem. (2002) 277(37):33864–33869.
  • UZEL MI, SCOTT IC, BABAKHANLOU - CHASEH et al.: Multiple bone morphogenetic protein-1 related mammalian metalloproteinases process pro-lysyl oxidase at the correct physiological site and control lysyl oxidase activation in mouse embryo fibroblast cultures. J. BioL Chem. (2001) 276(25):22537–22543.
  • STEIGLITZ BM, AYALA M, NARAYANAN K, GEORGE A, GREENSPAN DS: Bone Morphogenetic protein- 1/tolloid-like proteinases process dentin matrix protein.' Biol. Chem. (2004) 279(2):980–986.
  • PAPPANO WN, STEIGLITZ BM, SCOTT IC, KEENE DR, GREENSPAN DS: Use of Bmpl/tlIl doubly homozygous null mice and proteomics to identify an validate in vivo substrates of bone morphogenetic protein metalloproteinases. Bio. (2003) 23(13):4428–4438.
  • RATTENHOLL A, PAPPANO WN, KOCH M et al.: Proteinases of the bone morphogenetic protein-1 family convert procollagen VII to mature anchoring fibril collagen. J. Biol. Chem. (2002) 277(29):26372–26378.
  • MEDECK RJ, SOSA S, MORRIS N, OXFORD JT: BMP-1 mediated proteolytic processing of alternatively spliced isoforms of collagen type XI. Biochem J. (2003) 376:361–368.
  • SIERON AL, TRETIAKOVA A, JAMES ON BA et al.: Structure and function of Procollagen C-proteinase (mTolloid) domains determined by protease digestion, circular dichroism, binding to procollagen Type I, and computer modeling. Biochemistry (2000) 39:3231–3239.
  • KESSLER E, FICHARD A, CHANUT -DELALANDE H, BRUSEL M, RUGGIERO F: Bone morphogenetic protein-1 (BMP-1) mediates C-terminal processing of procollagen V homotrimer. " Biol. Chem. (2001) 276(29):27051–27057.
  • UNSOLD C, PAPPANO WN, IMAMURA Y, STEIGLITZ BM, GREENSPAN DS: Biosynthetic processing of the pro-al (V)2pro-a2 (V) collagen heterotrimer by bone morphogenetic protein-1 and furin-like proprotein convertases. J. Biol. Chem. (2002) 277(7):5596–5602.
  • SCOTT IC, IMAMURA Y, PAPPANO WN et al.: Bone morphogenetic protein -1 processes probiglycan. J. Biol. Chem. (2000) 275(39):30504–30511.
  • WADDINGTON RJ, ROBERTS HC, SUGARS RV, SCHONHERR E: Differential roles for small leucine-rich proteoglycans in bone formation. Ear: Cell. Mater (2003) 6:12–21.
  • SVENSSON L, HEINEGARD D, OLDBERG A: Decorin-binding sites for collagen Type I are mainly located in leucine-rich repeats 4-5. J. Biol. Chem. (1995) 270(35): 20712–20716.
  • AMANO S, SCOTT IC, TAKAHARA K et al.: Bone morphogenetic protein 1 is an extracellular processing enzyme of the laminin 572 chain. " Biol. Chem. (2000) 275(30):22728–22735.
  • QIN C, BRUNN JC, COOK RG et al.: Evidence for the proteolytic processing of dentin matrix protein 1.1 Biol. Chem. (2003) 278(36):34700–34708.
  • BLADER P, RASTEGAR S, FISCHER N, STRAHLE U: Cleavage of the BMP4 antagonist chordin by zebrafish tolloid. Science (1997) 278: 1937-1940.
  • ZAVOICO GB: New targets for the treatment of pathological fibrosis, an unmet clinical need. Drug Market Dev (1999) 10(1):2–10.
  • BITTERMAN PB, HENKE CA: Fibroproliferative disorders. Chest (1991) 99(3):815–845.
  • TRANSQUILLO RT, MURRAY JD: Continuum model of fibroblast-driven wound contraction: inflammation-mediation. " Ther. Biol. (1992) 158:135–172.
  • MAST BA, DIEGELMANN R, KRUMMEL TM, COHEN IK: Scarless wound healing in mammalian fetus. Surg. Cynecol Obstet. (1992) 174:441–451.
  • VEITCH DP, NOKELAINEN P, MCGOWAN KA et al: Mammalian tolloid metalloproteinase, and not matrix metalloprotease 2 or membrane Type 1 metalloprotease, process laminin-5 in keratinocytes and skin. " Biol. Chem (2003) 278(18):15661–15668.
  • LOHI J: Laminin-5 in the progression ofcarcinomas. Int.' Cancer. (2001) 94:763–767.
  • •Useful review of the role of laminin 5 in the migration and proliferation of carcinomas.
  • GIANNELLI G, ANTONACI S: Biological and clinical relevance of laminin-5 in cancer. Clin. Exp. Metastasis (2000) 18(6):439–443.
  • GAGNOUX-PALACIOS L, ALLEGRA M,SPIRITO F et al.: The short arm of the laminin 72 chain plays a pivotal role in the incorporation of laminin-5 into the extracellular matrix and in cell adhesion. Cell Biol. (2001) 153(4):835–849.
  • MIZUSHIMA H, HIROSAKI T, MIYATA S, TAKAMURA H, MIYAGI Y, MIYAZAKI K: Expression of laminin-5 enhances tumorgenicity of human fibrosarcoma cells in nude mice. fpn. " Cancer Res. 93(6) :652–659.
  • ANDERSON TD, FELDMAN M, WEBER RS, ZIOBER AF, ZIOBER BL: Tumor deposition of laminin-5 and the relationship with perineural invasion. Laryngoscope (2001) 111:2140–2143.
  • ONO Y, NAKANISHI Y, GOTOH M, SAKAMOTO M, HIROHASHI S: Epidermal growth factor receptor gene amplification is correlated with laminin-5 72 chain expression in oral squamous cell carcinoma cell lines. Cancer Lett. (2002) 175:197–204.
  • SKYLDBERG B, SALO S, ERIKSSON E et al.: Laminin-5 as a marker of invasiveness in cervical lesions. " Natl. Cancer Inst. (1999) 91(21):1882–1887.
  • LENANDER C, HABERMANN JK, OST A et al.: Laminin-5 gamma2 chain expression correlates with unfavorable prognosis in colon carcinomas. Anal. Cell. Pathol (2001) 22(4):201–209.
  • GIANNELLI G, FRANSVEA E, BERGAMINI C, MARINOSCI F, ANTONACI S: Laminin-5 chains are expressed differentially in metastatic and nonmetastatic hepatocellular carcinoma. Clin. Cancer Res. (2003) 9(10):3684–3691.
  • MCGOWAN K, VEITCH D, FINDELL P et al.: BMP-1 processing of laminin-5 controls migration of human epithelial cells. Ann. Meeting Soc. Invest. Dermatol Chicago, USA (2000).
  • •Two hydroxarnic acid inhibitors of BMP-1 were found to completely inhibit the migration of SCC cells.
  • WOLZ RL, ZEGGAF C, STOCKER W, ZWILLING R: Thio containing compounds and amino acid hydroxamates as reversible synthetic inhibitors of astacus proteinase. Arch. Biochem. Biophys. (1990) 281(2):275–281.
  • YIALLOUROS I, VASSILIOU S, YIOTAKIS A, ZWILLING R, STOCKER W, DIVE V: Phosphinic acids, the first potent inhibitors of astacin, behave as extremely slow-binding inhibitors. Biochem. (1998) 331:375–379.
  • DANKWARDT SM, BILLEDEAU RJ, LAWLEY LK, ABBOT, SC, MARTIN RL, CHAN CS et al.: Solid-phase synthesis of di- and tripeptide hydroxamic acids as inhibitors of procollagen C-proteinase. Bioorg. Med. Chem. Lett. (2000) 10:2513–2516.
  • OVENS A, JOULE JA, KADLER KE: Design and synthesis of acidic dipeptide hydroxamate inhibitors of procollagen C-proteinase. Peptide ScL (2000) 6:489–495.
  • ROBINSON LA, WILSON DM, DELAET NGJ, BRADLEY EK, DANKWARDT SM, CAMPBELL JA et al.: Novel inhibitors of procollagen C-proteinase, part 2: Glutamic acid hydroxamates. Bioorg. Med. Chem. Lett. (2003) 13:2381–2384.
  • DANKWARDT SM, ABBOT SC, BROKA CA, MARTIN RL, CHAN CS, SPRINGMAN EB et al.: Amino acid derived sulfonamide hydroxamates as inhibitors of procollagen C-proteinase. Part 2: Solid-phase optimization of side chains. Bioorg. Med. Chem. Lett. (2002) 12:1233–1235.
  • BAILEY S, FISH PV, JAMES K, MCELROY A: Discovery of UK-383,367, a potent and selective non-peptidic inhibitor of procollagen C-proteinase for the treatment of dermal scarring. 227th American Chem. Soc. National Meeting. Anaheim, USA (2004) MEDI 13.
  • NATCHUS MG, BOOKLAND RG, LAUFERSWEILER MJ et al.: Development of new carboxylic acid-based MMP inhibitors derived from functionalized propargylglycines. Med. Chem. (2001) 44:1060–1071.
  • SUZUKI N, LABOSKY PA, FURUTA Y et al.: Failure of ventral body wall closure in mouse embryos lacking a procollagen C-proteinase encoded by BMP1, a mammalian gene related to Drosophila tofloid. Development (1996) 122:3587–3595.
  • HAJDUK PJ, SHUKER SB, NETTESHEIM DG et al.: NMR-based modification of matrix metalloproteinase inhibitors with improved bioavailibility. J. Med. Chem. (2002) 45:5628–5639.
  • MACPHERSON LJ, BAYBURT EK, CAPPARELLI MP et al.: Discovery of CGS-27023A, a non-peptidic, potent, and orally active stromelysin inhibitor that blocks cartilage degradation in rabbits. J. Med. Chem. (1997) 40:2525–2532.
  • SINGH J, CONZENTINO P, CUNDY K et al.: Relationship between structure and bioavailability in a series of hydroxamate based metalloprotease inhibitors. Bioorg. Med. Chem. Lett. (1995) 5:337–342.
  • SKOTNICKI JS, ZASK A, NELSON FC, ALBRIGHT JD, LEVIN JI: Design and synthetic considerations of matrix metalloproteinase inhibitors. Ann. NY Acad. Sci. (1999) 878:61–72.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.