메뉴 건너뛰기




Volumn 55, Issue 2, 2008, Pages 297-305

Specific inhibition of procollagen C-endopeptidase activity by synthetic peptide with conservative sequence found in chordin

Author keywords

Chordin; N endopeptidase; Procollagen C endopeptidase

Indexed keywords

MAMMALIA;

EID: 46749105988     PISSN: 0001527X     EISSN: 1734154X     Source Type: Journal    
DOI: 10.18388/abp.2008_3076     Document Type: Article
Times cited : (5)

References (51)
  • 2
    • 0030931450 scopus 로고    scopus 로고
    • A cDNA cassette system for the synthesis of recombinant procollagens. Variants of procollagen II lacking a D-period are secreted as triplehelical monomers
    • Arnold WV, Sieron AL, Fertala A, Bachinger HP, Mechling D, Prockop DJ (1997) A cDNA cassette system for the synthesis of recombinant procollagens. Variants of procollagen II lacking a D-period are secreted as triplehelical monomers. Matrix Biol 16: 105-116.
    • (1997) Matrix Biol , vol.16 , pp. 105-116
    • Arnold, W.V.1    Sieron, A.L.2    Fertala, A.3    Bachinger, H.P.4    Mechling, D.5    Prockop, D.J.6
  • 3
    • 0033610910 scopus 로고    scopus 로고
    • Recombinant procollagen II: Deletion of D period segments identifies sequences that are required for helix stabilization and generates a temperature-sensitive N-proteinase cleavage site
    • Arnold WV, Fertala A, Sieron AL, Hattori H, Mechling D, Bachinger HP, Prockop DJ (1998) Recombinant procollagen II: Deletion of D period segments identifies sequences that are required for helix stabilization and generates a temperature-sensitive N-proteinase cleavage site. J Biol Chem 273: 31822-31828.
    • (1998) J Biol Chem , vol.273 , pp. 31822-31828
    • Arnold, W.V.1    Fertala, A.2    Sieron, A.L.3    Hattori, H.4    Mechling, D.5    Bachinger, H.P.6    Prockop, D.J.7
  • 4
    • 0031465734 scopus 로고    scopus 로고
    • Cleavage of the BMP-4 antagonist Chordin by zebrafish Tolloid
    • Blader P, Rastegar S, Fisher N, Strähle U (1997) Cleavage of the BMP-4 antagonist Chordin by zebrafish Tolloid. Science 278: 1937-1940.
    • (1997) Science , vol.278 , pp. 1937-1940
    • Blader, P.1    Rastegar, S.2    Fisher, N.3    Strähle, U.4
  • 6
  • 7
    • 0034833983 scopus 로고    scopus 로고
    • Assessment of a simple, non-toxic Alamar blue cell survival assay to monitor tomato cell viability
    • Byth HA, Mchunu BI, Dubery IA, Bornman L (2001) Assessment of a simple, non-toxic Alamar blue cell survival assay to monitor tomato cell viability. Phytochem Anal 12: 340-346.
    • (2001) Phytochem Anal , vol.12 , pp. 340-346
    • Byth, H.A.1    Mchunu, B.I.2    Dubery, I.A.3    Bornman, L.4
  • 9
    • 0030959540 scopus 로고    scopus 로고
    • cDNA cloning and expression of bovine procollagen I N-proteinase: A new member of the superfamily of zinc-metalloproteinases with binding sites for cells and other matrix components
    • Colige A, Li SW, Sieron AL, Nusgens BV,Prockop DJ, Lapiere CM (1997) cDNA cloning and expression of bovine procollagen I N-proteinase: a new member of the superfamily of zinc-metalloproteinases with binding sites for cells and other matrix components. Proc Natl Acad Sci USA 94: 2374-2379.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2374-2379
    • Colige, A.1    Li, S.W.2    Sieron, A.L.3    Nusgens, B.V.4    Prockop, D.J.5    Lapiere, C.M.6
  • 10
    • 0028837996 scopus 로고
    • The proteolytic processing site of the precursor of lysyl oxidase
    • Cronshaw AD, Fothergill-Gilmore LA, Hulmes DJS (1995) The proteolytic processing site of the precursor of lysyl oxidase. Biochem J 308: 279-284.
    • (1995) Biochem J , vol.308 , pp. 279-284
    • Cronshaw, A.D.1    Fothergill-Gilmore, L.A.2    Hulmes, D.J.S.3
  • 11
    • 0029004025 scopus 로고
    • Vascular permeability factor/vascular endothelial growth factor, microvascular hyperpermeability, and angiogenesis
    • Dvorak HF, Brown LF, Detmar M, Dvorak AM (1995) Vascular permeability factor/vascular endothelial growth factor, microvascular hyperpermeability, and angiogenesis. Am J Pathol 146: 1029-1039.
    • (1995) Am J Pathol , vol.146 , pp. 1029-1039
    • Dvorak, H.F.1    Brown, L.F.2    Detmar, M.3    Dvorak, A.M.4
  • 13
    • 0030448814 scopus 로고    scopus 로고
    • Blood vessel formation: What is its molecular basis?
    • Folkman J, D'Amore PA (1996) Blood vessel formation: what is its molecular basis? Cell 87: 1153-1155.
    • (1996) Cell , vol.87 , pp. 1153-1155
    • Folkman, J.1    D'Amore, P.A.2
  • 14
    • 0027990415 scopus 로고
    • Wound repair in the context of extracellular matrix
    • Gailit J, Clark RA (1994) Wound repair in the context of extracellular matrix. Curr Opin Cell Biol 6: 717-725.
    • (1994) Curr Opin Cell Biol , vol.6 , pp. 717-725
    • Gailit, J.1    Clark, R.A.2
  • 15
    • 9644291556 scopus 로고    scopus 로고
    • Deletion of epidermal growth factor-like domains converts mammalian tolloid into a chordinase and effective procollagen C-proteinase
    • Garrigue-Antar L, Francois V, Kalder KE (2004) Deletion of epidermal growth factor-like domains converts mammalian tolloid into a chordinase and effective procollagen C-proteinase. J Biol Chem 279: 49835-49841.
    • (2004) J Biol Chem , vol.279 , pp. 49835-49841
    • Garrigue-Antar, L.1    Francois, V.2    Kalder, K.E.3
  • 16
    • 33749538647 scopus 로고    scopus 로고
    • BMP1 controls TGFβ1 activation via cleavage of latent TGFβ-binding protein
    • Ge G, Greenspan DS (2006) BMP1 controls TGFβ1 activation via cleavage of latent TGFβ-binding protein. J Cell Biol 175: 111-120
    • (2006) J Cell Biol , vol.175 , pp. 111-120
    • Ge, G.1    Greenspan, D.S.2
  • 17
    • 4744352594 scopus 로고    scopus 로고
    • Bone morphogenetic protein-1/Tolloid-related metalloproteinases process osteoglycin and enhance its ability to regulate collagen fibrillogenesis
    • Ge G, Seo NS, Liang X, Hopkins DR, Höök M, Greenspan DS (2004) Bone morphogenetic protein-1/Tolloid-related metalloproteinases process osteoglycin and enhance its ability to regulate collagen fibrillogenesis. J Biol Chem 279: 41626-41633.
    • (2004) J Biol Chem , vol.279 , pp. 41626-41633
    • Ge, G.1    Seo, N.S.2    Liang, X.3    Hopkins, D.R.4    Höök, M.5    Greenspan, D.S.6
  • 19
    • 0037705369 scopus 로고    scopus 로고
    • Bone morphogenetic protein (BMP)-1: Identification of the minimal domain structure for C-proteinase activity
    • Hartigan N, Garrigue-Antar L, Kadler KE (2003) Bone morphogenetic protein (BMP)-1: identification of the minimal domain structure for C-proteinase activity. J Biol Chem 278: 18045-18049.
    • (2003) J Biol Chem , vol.278 , pp. 18045-18049
    • Hartigan, N.1    Garrigue-Antar, L.2    Kadler, K.E.3
  • 20
    • 0022392606 scopus 로고
    • Type I procollagen carboxylterminal proteinase from chick embryo tendons
    • Hojima Y, van der Rest M, Prockop DJ (1985) Type I procollagen carboxylterminal proteinase from chick embryo tendons. J Biol Chem 260: 15996-16003.
    • (1985) J Biol Chem , vol.260 , pp. 15996-16003
    • Hojima, Y.1    van der Rest, M.2    Prockop, D.J.3
  • 21
    • 0024411470 scopus 로고
    • Type I procollagen N-proteinase from chick embryo tendons. Purification of a new 500-kDa form of the enzyme and identification of the catalytically active polypeptides
    • Hojima Y, McKenzie JA, van der Rest M, Prockop DJ (1989) Type I procollagen N-proteinase from chick embryo tendons. Purification of a new 500-kDa form of the enzyme and identification of the catalytically active polypeptides. J Biol Chem 264: 11336-11345.
    • (1989) J Biol Chem , vol.264 , pp. 11336-11345
    • Hojima, Y.1    McKenzie, J.A.2    van der Rest, M.3    Prockop, D.J.4
  • 22
    • 0027996812 scopus 로고
    • Cleavage of type I procollagen by C- and N-proteinases is more rapid if the substrate is aggregated with dextran sulfate or polyethylene glycol
    • Hojima Y, Behta B, Romanic AM, Prockop DJ (1994) Cleavage of type I procollagen by C- and N-proteinases is more rapid if the substrate is aggregated with dextran sulfate or polyethylene glycol. Anal Biochem 223: 173-180.
    • (1994) Anal Biochem , vol.223 , pp. 173-180
    • Hojima, Y.1    Behta, B.2    Romanic, A.M.3    Prockop, D.J.4
  • 23
    • 13444291201 scopus 로고    scopus 로고
    • Inhibition of VEGF receptors significantly impairs mammary cancer growth in C3(1)/Tag transgenic mice through antiangiogenic and nonantiangiogenic mechanisms
    • Huh JI, Calvo A, Stafford J, Cheung M, Kumar R, Philp D, Kleinman HK, Green JE (2005) Inhibition of VEGF receptors significantly impairs mammary cancer growth in C3(1)/Tag transgenic mice through antiangiogenic and nonantiangiogenic mechanisms. Oncogene 24: 790-800.
    • (2005) Oncogene , vol.24 , pp. 790-800
    • Huh, J.I.1    Calvo, A.2    Stafford, J.3    Cheung, M.4    Kumar, R.5    Philp, D.6    Kleinman, H.K.7    Green, J.E.8
  • 24
    • 0032538562 scopus 로고    scopus 로고
    • 2-terminal propeptide, and a furin-like proprotein convertase processes the COOH-terminal propeptide of pro-α1(V) collagen
    • 2-terminal propeptide, and a furin-like proprotein convertase processes the COOH-terminal propeptide of pro-α1(V) collagen. J Biol Chem 273: 27511-27517.
    • (1998) J Biol Chem , vol.273 , pp. 27511-27517
    • Imamura, Y.1    Steiglitz, B.M.2    Greenspan, D.S.3
  • 25
    • 0030593032 scopus 로고    scopus 로고
    • Bone morphogenetic protein-1: The type I procollagen C-proteinase [see comments]
    • Kessler E, Takahara K, Biniaminov L, Brusel M, Greenspan DS (1996) Bone morphogenetic protein-1: the type I procollagen C-proteinase [see comments]. Science 271: 360-362.
    • (1996) Science , vol.271 , pp. 360-362
    • Kessler, E.1    Takahara, K.2    Biniaminov, L.3    Brusel, M.4    Greenspan, D.S.5
  • 26
    • 0015164941 scopus 로고
    • Procollagen peptidase: An enzyme excising the coordination peptides of procollagen
    • Lapiere CM, Lenaers A, Kohn LD (1971) Procollagen peptidase: an enzyme excising the coordination peptides of procollagen. Proc Natl Acad Sci USA 68: 3054-3058.
    • (1971) Proc Natl Acad Sci USA , vol.68 , pp. 3054-3058
    • Lapiere, C.M.1    Lenaers, A.2    Kohn, L.D.3
  • 27
    • 0018786008 scopus 로고
    • Separate amino and carboxyl procollagen peptidases in chick embryo tendon
    • Leung MK, Fessler LI, Greenberg DB, Fessler JH (1979) Separate amino and carboxyl procollagen peptidases in chick embryo tendon. J Biol Chem 254: 224-232.
    • (1979) J Biol Chem , vol.254 , pp. 224-232
    • Leung, M.K.1    Fessler, L.I.2    Greenberg, D.B.3    Fessler, J.H.4
  • 28
    • 0029906315 scopus 로고    scopus 로고
    • The C-proteinase that processes procollagens to collagens is identical to the protein previously identified as bone morphogenic protein-1
    • Li SW, Sieron AL, Fertala A, Hojima Y, Arnold WV, Prockop DJ (1996) The C-proteinase that processes procollagens to collagens is identical to the protein previously identified as bone morphogenic protein-1. Proc Natl Acad Sci USA 93: 4127-5130.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4127-5130
    • Li, S.W.1    Sieron, A.L.2    Fertala, A.3    Hojima, Y.4    Arnold, W.V.5    Prockop, D.J.6
  • 30
    • 0030671306 scopus 로고    scopus 로고
    • Production of a DPP activity gradient in the early Drosophila embryo through the opposing actions of the SOG and TLD proteins
    • Marques G, Musacchio M, Simell MJ, Wunnenberg-Stapleton K, Cho KWY, O'Connor M (1997) Production of a DPP activity gradient in the early Drosophila embryo through the opposing actions of the SOG and TLD proteins. Cell 91: 417-426.
    • (1997) Cell , vol.91 , pp. 417-426
    • Marques, G.1    Musacchio, M.2    Simell, M.J.3    Wunnenberg-Stapleton, K.4    Cho, K.W.Y.5    O'Connor, M.6
  • 31
    • 0025063772 scopus 로고
    • Increased proteolytic activity is responsible for the aberrant morphogenetic behavior of endothelial cells expressing the middle T oncogene
    • Montesano R, Pepper MS, Mohle-Steinlein U, Risau W, Wagner EF, Orci L (1990) Increased proteolytic activity is responsible for the aberrant morphogenetic behavior of endothelial cells expressing the middle T oncogene. Cell 62: 435-445.
    • (1990) Cell , vol.62 , pp. 435-445
    • Montesano, R.1    Pepper, M.S.2    Mohle-Steinlein, U.3    Risau, W.4    Wagner, E.F.5    Orci, L.6
  • 32
    • 0029863235 scopus 로고    scopus 로고
    • Metalloproteinase activity secreted by fibrogenic cells in the processing of prolysyl oxidase. Potential role of procollagen C-proteinase
    • Panchenko MV, Stelter-Stevenson WG, Trupetskoy OV, Gacheru SN, Kagan HM (1996) Metalloproteinase activity secreted by fibrogenic cells in the processing of prolysyl oxidase. Potential role of procollagen C-proteinase. J Biol Chem 271: 7113-7119.
    • (1996) J Biol Chem , vol.271 , pp. 7113-7119
    • Panchenko, M.V.1    Stelter-Stevenson, W.G.2    Trupetskoy, O.V.3    Gacheru, S.N.4    Kagan, H.M.5
  • 33
    • 0030665807 scopus 로고    scopus 로고
    • Cleavage of Chordin by Xolloid metalloprotease suggests a role for proteolytic processing in the regulation of Spemann organizer activity
    • Piccolo S, Agius E, Lu B, Goodman S, Dale L, De Robertis EM (1997) Cleavage of Chordin by Xolloid metalloprotease suggests a role for proteolytic processing in the regulation of Spemann organizer activity. Cell 91: 407-416.
    • (1997) Cell , vol.91 , pp. 407-416
    • Piccolo, S.1    Agius, E.2    Lu, B.3    Goodman, S.4    Dale, L.5    De Robertis, E.M.6
  • 34
    • 0021247323 scopus 로고
    • Heritable diseases of collagen
    • Prockop DJ, Kivirikko KI (1984) Heritable diseases of collagen. N Engl J Med 311: 376-386.
    • (1984) N Engl J Med , vol.311 , pp. 376-386
    • Prockop, D.J.1    Kivirikko, K.I.2
  • 37
    • 0030952289 scopus 로고    scopus 로고
    • Mechanisms of angiogenesis
    • Risau W (1997) Mechanisms of angiogenesis. Nature 386: 671-674.
    • (1997) Nature , vol.386 , pp. 671-674
    • Risau, W.1
  • 39
    • 0030191756 scopus 로고    scopus 로고
    • Molecular framework for angiogenesis: A complex web of interactions between extravasated plasma proteins and endothelial cell proteins induced by angiogenic cytokines
    • Senger DR (1996) Molecular framework for angiogenesis: a complex web of interactions between extravasated plasma proteins and endothelial cell proteins induced by angiogenic cytokines. Am J Pathol 149: 1-7.
    • (1996) Am J Pathol , vol.149 , pp. 1-7
    • Senger, D.R.1
  • 40
    • 0027441145 scopus 로고
    • Deletion of a large domain in recombinant human procollagen II does not alter the thermal stability of the triple helix
    • Sieron AL, Fertala A, Ala-Kokko L, Prockop DJ (1993) Deletion of a large domain in recombinant human procollagen II does not alter the thermal stability of the triple helix. J Biol Chem 268: 21232-21237.
    • (1993) J Biol Chem , vol.268 , pp. 21232-21237
    • Sieron, A.L.1    Fertala, A.2    Ala-Kokko, L.3    Prockop, D.J.4
  • 41
    • 0034724260 scopus 로고    scopus 로고
    • Structure and function of procollagen C-proteinase (mTolloid) domains determined by protease digestion, circular dichroism, binding to procollagen type I, and computer modeling
    • Sieron AL, Tretiakova A, Jameson BA, Segall ML, Lund-Katz S, Khan MT, Li SW, Stöcker W (2000) Structure and function of procollagen C-proteinase (mTolloid) domains determined by protease digestion, circular dichroism, binding to procollagen type I, and computer modeling. Biochemistry 39: 3231-3239.
    • (2000) Biochemistry , vol.39 , pp. 3231-3239
    • Sieron, A.L.1    Tretiakova, A.2    Jameson, B.A.3    Segall, M.L.4    Lund-Katz, S.5    Khan, M.T.6    Li, S.W.7    Stöcker, W.8
  • 42
    • 0347723963 scopus 로고    scopus 로고
    • Bone morphogenetic protein-1/tolloidlike proteinases process dentin matrix protein-1
    • Steiglitz BM, Ayala M, Narayanan K, George A, Greenspan DS (2004) Bone morphogenetic protein-1/tolloidlike proteinases process dentin matrix protein-1. J Biol Chem 279: 980-986.
    • (2004) J Biol Chem , vol.279 , pp. 980-986
    • Steiglitz, B.M.1    Ayala, M.2    Narayanan, K.3    George, A.4    Greenspan, D.S.5
  • 44
    • 10544240364 scopus 로고    scopus 로고
    • Failure of ventral body wall closure in mouse embryos lacking a procollagen C-proteinase encoded by BMP-1, a mammalian gene related to Drosophila tolloid
    • Suzuki N, Labosky PA, Furuta Y, Hargett L, Dunn R, Fogo AB, Takahara K, Peters DM, Greenspan DS, Hogan BL (1996) Failure of ventral body wall closure in mouse embryos lacking a procollagen C-proteinase encoded by BMP-1, a mammalian gene related to Drosophila tolloid. Development 122: 3587-3595.
    • (1996) Development , vol.122 , pp. 3587-3595
    • Suzuki, N.1    Labosky, P.A.2    Furuta, Y.3    Hargett, L.4    Dunn, R.5    Fogo, A.B.6    Takahara, K.7    Peters, D.M.8    Greenspan, D.S.9    Hogan, B.L.10
  • 45
    • 0028608106 scopus 로고
    • Bone morphogenetic protein-1 and a mammalian toloid homologue (mTld) are encoded by alternatively spliced transcripts which are differentially expressed in some tissues
    • Takahara K, Lyons GE, Greenspan DS (1994) Bone morphogenetic protein-1 and a mammalian toloid homologue (mTld) are encoded by alternatively spliced transcripts which are differentially expressed in some tissues. J Biol Chem 269: 32572-32578.
    • (1994) J Biol Chem , vol.269 , pp. 32572-32578
    • Takahara, K.1    Lyons, G.E.2    Greenspan, D.S.3
  • 49
    • 8544273683 scopus 로고    scopus 로고
    • Yeast two-hybrid screening for proteins that interact with α1-adrenergic receptors
    • Zhang T, Xu Q, Chen FR, Han QD, Zhang YY (2004) Yeast two-hybrid screening for proteins that interact with α1-adrenergic receptors. Acta Pharmacol Sin 25: 1471-1478.
    • (2004) Acta Pharmacol Sin , vol.25 , pp. 1471-1478
    • Zhang, T.1    Xu, Q.2    Chen, F.R.3    Han, Q.D.4    Zhang, Y.Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.