메뉴 건너뛰기




Volumn 23, Issue 15, 2004, Pages 3020-3030

Collagenase unwinds triple-helical collagen prior to peptide bond hydrolysis

Author keywords

Collagenase; Enzyme mechanism; Matrix metalloproteinase; Protein unfolding; Triple helix

Indexed keywords

ALANINE; COLLAGEN; COLLAGEN TYPE 1; COLLAGENASE; GLUTAMIC ACID; INTERSTITIAL COLLAGENASE; MATRIX METALLOPROTEINASE;

EID: 4143066015     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.emboj.7600318     Document Type: Article
Times cited : (401)

References (54)
  • 1
    • 0028947020 scopus 로고
    • Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4- and 1/4-length fragments
    • Aimes RT, Quigley JP (1995) Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4- and 1/4-length fragments. J Biol Chem 270: 5872-5876
    • (1995) J Biol Chem , vol.270 , pp. 5872-5876
    • Aimes, R.T.1    Quigley, J.P.2
  • 2
    • 0029644945 scopus 로고
    • A helping hand for collagenases: The haemopexin-like domain
    • Bode W (1995) A helping hand for collagenases: the haemopexin-like domain. Structure 3: 527-530
    • (1995) Structure , vol.3 , pp. 527-530
    • Bode, W.1
  • 3
    • 0036516460 scopus 로고    scopus 로고
    • Matrix metalloproteinases: A tail of a frog that became a prince
    • Brinckerhoff CE, Matrisian LM (2002) Matrix metalloproteinases: a tail of a frog that became a prince. Nat Rev Mol Cell Biol 3: 207-214
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 207-214
    • Brinckerhoff, C.E.1    Matrisian, L.M.2
  • 4
    • 0017581932 scopus 로고
    • Do mammalian collagenases and DNA restriction endonucleases share a similar mechanism for cleavage site recognition?
    • Brown RA, Hukins DW, Weiss JB, Twose TM (1977) Do mammalian collagenases and DNA restriction endonucleases share a similar mechanism for cleavage site recognition? Biochem Biophys Res Commun 74: 1102-1108
    • (1977) Biochem Biophys Res Commun , vol.74 , pp. 1102-1108
    • Brown, R.A.1    Hukins, D.W.2    Weiss, J.B.3    Twose, T.M.4
  • 5
    • 0029766216 scopus 로고    scopus 로고
    • Metalloproteinase inhibitors and the prevention of connective tissue breakdown
    • Cawston TE (1996) Metalloproteinase inhibitors and the prevention of connective tissue breakdown. Pharmacol Therap 70: 163-182
    • (1996) Pharmacol Therap , vol.70 , pp. 163-182
    • Cawston, T.E.1
  • 6
    • 0034703074 scopus 로고    scopus 로고
    • Identification of the (RWTNNFREY191)-R-183 region as a critical segment of matrix metalloproteinase 1 for the expression of collagenolytic activity
    • Chung L, Shimokawa K, Dinakarpandian D, Grams F, Fields GB, Nagase H (2000) Identification of the (RWTNNFREY191)-R-183 region as a critical segment of matrix metalloproteinase 1 for the expression of collagenolytic activity. J Biol Chem 275: 29610-29617
    • (2000) J Biol Chem , vol.275 , pp. 29610-29617
    • Chung, L.1    Shimokawa, K.2    Dinakarpandian, D.3    Grams, F.4    Fields, G.B.5    Nagase, H.6
  • 7
    • 0024461448 scopus 로고
    • Fragments of human flbroblast collagenase. Purification and characterization
    • Clark IM, Cawston TE (1989) Fragments of human flbroblast collagenase. Purification and characterization. Biochem J 263: 201-206
    • (1989) Biochem J , vol.263 , pp. 201-206
    • Clark, I.M.1    Cawston, T.E.2
  • 8
    • 0029967113 scopus 로고    scopus 로고
    • Collagen/collagenase interaction: Does the enzyme mimic the conformation of its own substrate?
    • de Souza SJ, Pereira HM, Jacchieri S, Brentani RR (1996) Collagen/collagenase interaction: does the enzyme mimic the conformation of its own substrate? FASEB J 10: 927-930
    • (1996) FASEB J , vol.10 , pp. 927-930
    • De Souza, S.J.1    Pereira, H.M.2    Jacchieri, S.3    Brentani, R.R.4
  • 9
    • 0026333465 scopus 로고
    • A model for interstitial collagen catabolism by mammalian collagenases
    • Fields GB (1991) A model for interstitial collagen catabolism by mammalian collagenases. J Theor Biol 153: 585-602
    • (1991) J Theor Biol , vol.153 , pp. 585-602
    • Fields, G.B.1
  • 10
    • 0036303549 scopus 로고    scopus 로고
    • Structural properties of a collagenous heterotrimer that mimics the collagenase cleavage site of collagen type I
    • Fiori S, Sacca B, Moroder L (2002) Structural properties of a collagenous heterotrimer that mimics the collagenase cleavage site of collagen type I. J Mol Biol 319: 1235-1242
    • (2002) J Mol Biol , vol.319 , pp. 1235-1242
    • Fiori, S.1    Sacca, B.2    Moroder, L.3
  • 11
    • 0018400235 scopus 로고
    • Chain conformation in the collagen molecule
    • Fraser RD, MacRae TP, Suzuki E (1979) Chain conformation in the collagen molecule. J Mol Biol 129: 463-481
    • (1979) J Mol Biol , vol.129 , pp. 463-481
    • Fraser, R.D.1    MacRae, T.P.2    Suzuki, E.3
  • 14
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg AL (2003) Protein degradation and protection against misfolded or damaged proteins. Nature 426: 895-899
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 15
    • 0040051981 scopus 로고    scopus 로고
    • The helping hand of collagenase-3 (MMP-13): 2.7 Å crystal structure of its C-terminal haemopexin-like domain
    • Gomis-Ruth FX, Gohlke U, Betz M, Knäuper V, Murphy G, López-Otín C, Bode W (1996) The helping hand of collagenase-3 (MMP-13): 2.7 Å crystal structure of its C-terminal haemopexin-like domain. J Mol Biol 264: 556-566
    • (1996) J Mol Biol , vol.264 , pp. 556-566
    • Gomis-Ruth, F.X.1    Gohlke, U.2    Betz, M.3    Knäuper, V.4    Murphy, G.5    López-Otín, C.6    Bode, W.7
  • 16
    • 0026768692 scopus 로고
    • Inhibition of human skin fibroblast collagenase, thermolysin, and Pseudomonas aeruginosa elastase by peptide hydroxamic acids
    • Grobelny D, Poncz L, Galardy RE (1992) Inhibition of human skin fibroblast collagenase, thermolysin, and Pseudomonas aeruginosa elastase by peptide hydroxamic acids. Biochemistry 31: 7152-7154
    • (1992) Biochemistry , vol.31 , pp. 7152-7154
    • Grobelny, D.1    Poncz, L.2    Galardy, R.E.3
  • 17
    • 0013804986 scopus 로고
    • Specific degradation of the collagen molecule by tadpole collagenolytic enzyme
    • Gross J, Nagai Y (1965) Specific degradation of the collagen molecule by tadpole collagenolytic enzyme. Proc Natl Acad Sci USA 54: 1197-1204
    • (1965) Proc Natl Acad Sci USA , vol.54 , pp. 1197-1204
    • Gross, J.1    Nagai, Y.2
  • 18
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex N, Peitsch MC (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18: 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 19
    • 1442264828 scopus 로고    scopus 로고
    • Take five-BACE and the gamma-secretase quartet conduct Alzheimer's amyloid beta-peptide generation
    • Haass C (2004) Take five-BACE and the gamma-secretase quartet conduct Alzheimer's amyloid beta-peptide generation. EMBO J 23: 483-488
    • (2004) EMBO J , vol.23 , pp. 483-488
    • Haass, C.1
  • 21
    • 0019407381 scopus 로고
    • On the attribution and additivity of binding energies
    • Jencks WP (1981) On the attribution and additivity of binding energies. Proc Natl Acad Sci USA 78: 4046-4050
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 4046-4050
    • Jencks, W.P.1
  • 22
    • 0030898796 scopus 로고    scopus 로고
    • The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction
    • Knäuper V, Cowell S, Smith B, Lopéz-Otín C, O'Shea M, Morris H, Zardi L, Murphy G (1997) The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction. J Biol Chem 272: 7608-7616
    • (1997) J Biol Chem , vol.272 , pp. 7608-7616
    • Knäuper, V.1    Cowell, S.2    Smith, B.3    Lopéz-Otín, C.4    O'Shea, M.5    Morris, H.6    Zardi, L.7    Murphy, G.8
  • 24
    • 0035800664 scopus 로고    scopus 로고
    • The crystal and molecular structure of a collagen-like peptide with a biologically relevant sequence
    • Kramer RZ, Bella J, Brodsky B, Berman HM (2001) The crystal and molecular structure of a collagen-like peptide with a biologically relevant sequence. J Mol Biol 311: 131-147
    • (2001) J Mol Biol , vol.311 , pp. 131-147
    • Kramer, R.Z.1    Bella, J.2    Brodsky, B.3    Berman, H.M.4
  • 28
    • 0015856509 scopus 로고
    • Gelatin: A poor substrate for a mammalian collagenase
    • McCroskery PA, Wood Jr S, Harris Jr ED (1973) Gelatin: a poor substrate for a mammalian collagenase. Science 182: 70-71
    • (1973) Science , vol.182 , pp. 70-71
    • McCroskery, P.A.1    Wood Jr., S.2    Harris Jr., E.D.3
  • 29
    • 0036254702 scopus 로고    scopus 로고
    • Proteolytic response to oxidative stress in mammalian cells
    • Mehlhase J, Grune T (2002) Proteolytic response to oxidative stress in mammalian cells. Biol Chem 383: 559-567
    • (2002) Biol Chem , vol.383 , pp. 559-567
    • Mehlhase, J.1    Grune, T.2
  • 30
    • 0022870835 scopus 로고
    • Purification of human collagenases with a hydroxamic acid affinity column
    • Moore WM, Spilburg CA (1986) Purification of human collagenases with a hydroxamic acid affinity column. Biochemistry 25: 5189-5195
    • (1986) Biochemistry , vol.25 , pp. 5189-5195
    • Moore, W.M.1    Spilburg, C.A.2
  • 31
    • 0040182518 scopus 로고    scopus 로고
    • Heterotrimeric collagen peptides as fluorogenic collagenase substrates: Synthesis, conformational properties, and enzymatic digestion
    • Muller JCD, Ottl J, Moroder L (2000) Heterotrimeric collagen peptides as fluorogenic collagenase substrates: synthesis, conformational properties, and enzymatic digestion. Biochemistry 39: 5111-5116
    • (2000) Biochemistry , vol.39 , pp. 5111-5116
    • Muller, J.C.D.1    Ottl, J.2    Moroder, L.3
  • 33
    • 0022231146 scopus 로고
    • Purification and characterization of a bone metalloproteinase that degrades gelatin and types IV and V collagen
    • Murphy G, McAlpine CG, Poll CT, Reynolds JJ (1985) Purification and characterization of a bone metalloproteinase that degrades gelatin and types IV and V collagen. Biochim Biophys Acta 831: 49-58
    • (1985) Biochim Biophys Acta , vol.831 , pp. 49-58
    • Murphy, G.1    McAlpine, C.G.2    Poll, C.T.3    Reynolds, J.J.4
  • 34
    • 0025335183 scopus 로고
    • Stepwise activation mechanisms of the precursor of matrix metalloproteinase 3 (stromelysin) by proteinases and (4-aminophenyl)mercuric acetate
    • Nagase H, Enghild JJ, Suzuki K, Salvesen G (1990) Stepwise activation mechanisms of the precursor of matrix metalloproteinase 3 (stromelysin) by proteinases and (4-aminophenyl)mercuric acetate. Biochemistry 29: 5783-5789
    • (1990) Biochemistry , vol.29 , pp. 5783-5789
    • Nagase, H.1    Enghild, J.J.2    Suzuki, K.3    Salvesen, G.4
  • 35
    • 0029758751 scopus 로고    scopus 로고
    • Human matrix metalloproteinase specificity studies using collagen sequence-based synthetic peptides
    • Nagase H, Fields GB (1996) Human matrix metalloproteinase specificity studies using collagen sequence-based synthetic peptides. Biopolymers 40: 399-416
    • (1996) Biopolymers , vol.40 , pp. 399-416
    • Nagase, H.1    Fields, G.B.2
  • 36
    • 0031025218 scopus 로고    scopus 로고
    • Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules
    • Ohuchi E, Imai K, Fujii Y, Sato H, Seiki M, Okada Y (1997) Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules. J Biol Chem 272: 2446-2451
    • (1997) J Biol Chem , vol.272 , pp. 2446-2451
    • Ohuchi, E.1    Imai, K.2    Fujii, Y.3    Sato, H.4    Seiki, M.5    Okada, Y.6
  • 38
    • 0036741135 scopus 로고    scopus 로고
    • Molecular determinants of metalloproteinase substrate specificity: Matrix metalloproteinase substrate binding domains, modules, and exosites
    • Overall CM (2002) Molecular determinants of metalloproteinase substrate specificity: matrix metalloproteinase substrate binding domains, modules, and exosites. Mol Biotechnol 22: 51-86
    • (2002) Mol Biotechnol , vol.22 , pp. 51-86
    • Overall, C.M.1
  • 39
    • 0035903020 scopus 로고    scopus 로고
    • Specific collagenolysis by gelatinase A, MMP-2, is determined by the hemopexin domain and not the fibronectin-like domain
    • Patterson ML, Atkinson SJ, Knäuper V, Murphy G (2001) Specific collagenolysis by gelatinase A, MMP-2, is determined by the hemopexin domain and not the fibronectin-like domain. FEBS Lett 503: 158-162
    • (2001) FEBS Lett , vol.503 , pp. 158-162
    • Patterson, M.L.1    Atkinson, S.J.2    Knäuper, V.3    Murphy, G.4
  • 40
    • 0030949650 scopus 로고    scopus 로고
    • The activity of collagenase-1 is required for keratinocyte migration on a type I collagen matrix
    • Pilcher BK, Dumin JA, Sudbeck BD, Krane SM, Welgus HG, Parks WC (1997) The activity of collagenase-1 is required for keratinocyte migration on a type I collagen matrix. J Cell Biol 137: 1445-1457
    • (1997) J Cell Biol , vol.137 , pp. 1445-1457
    • Pilcher, B.K.1    Dumin, J.A.2    Sudbeck, B.D.3    Krane, S.M.4    Welgus, H.G.5    Parks, W.C.6
  • 41
    • 0000523565 scopus 로고
    • Structure of collagen
    • Ramachandran GN, Kartha G (1955) Structure of collagen. Nature 176: 593-595
    • (1955) Nature , vol.176 , pp. 593-595
    • Ramachandran, G.N.1    Kartha, G.2
  • 42
    • 1542390392 scopus 로고    scopus 로고
    • Control of lipid metabolism by regulated intramembrane proteolysis of sterol regulatory element binding proteins (SREBPs)
    • Rawson RB (2003) Control of lipid metabolism by regulated intramembrane proteolysis of sterol regulatory element binding proteins (SREBPs). Biochem Soc Symp 70: 221-231
    • (2003) Biochem Soc Symp , vol.70 , pp. 221-231
    • Rawson, R.B.1
  • 43
    • 32444451050 scopus 로고
    • The molecular structure of collagen
    • Rich A, Crick FH (1961) The molecular structure of collagen. J Mol Biol 3: 483-506
    • (1961) J Mol Biol , vol.3 , pp. 483-506
    • Rich, A.1    Crick, F.H.2
  • 44
    • 0035188727 scopus 로고    scopus 로고
    • How matrix metalloproteinases regulate cell behavior
    • Sternlicht MD, Werb Z (2001) How matrix metalloproteinases regulate cell behavior. Annu Rev Cell Dev Biol 17: 463-516
    • (2001) Annu Rev Cell Dev Biol , vol.17 , pp. 463-516
    • Sternlicht, M.D.1    Werb, Z.2
  • 45
    • 0020557945 scopus 로고
    • Mechanism of collagen degradation by collagenase: A transition process of the collagen molecular from collagenase-substrate to gelatinase-substrate
    • Sunada H, Nagai Y (1983) Mechanism of collagen degradation by collagenase:a transition process of the collagen molecular from collagenase-substrate to gelatinase-substrate. Biomed Res 4: 61-70
    • (1983) Biomed Res , vol.4 , pp. 61-70
    • Sunada, H.1    Nagai, Y.2
  • 46
    • 0017657009 scopus 로고
    • Autoimmunity to type II collagen an experimental model of arthritis
    • Trentham DE, Townes AS, Kang AH (1977) Autoimmunity to type II collagen an experimental model of arthritis. J Exp Med 146: 857-868
    • (1977) J Exp Med , vol.146 , pp. 857-868
    • Trentham, D.E.1    Townes, A.S.2    Kang, A.H.3
  • 47
    • 0037693895 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tissue inhibitors of metalloproteinases: Structure, function, and biochemistry
    • Visse R, Nagase H (2003) Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry. Circ Res 92: 827-839
    • (2003) Circ Res , vol.92 , pp. 827-839
    • Visse, R.1    Nagase, H.2
  • 48
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • Voges D, Zwickl P, Baumeister W (1999) The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu Rev Biochem 68: 1015-1068
    • (1999) Annu Rev Biochem , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 50
    • 0019857661 scopus 로고
    • The collagen substrate specificity of human skin fibroblast collagenase
    • Welgus HG, Jeffrey JJ, Eisen AZ (1981) The collagen substrate specificity of human skin fibroblast collagenase. J Biol Chem 256: 9511-9515
    • (1981) J Biol Chem , vol.256 , pp. 9511-9515
    • Welgus, H.G.1    Jeffrey, J.J.2    Eisen, A.Z.3
  • 51
    • 0001796893 scopus 로고    scopus 로고
    • The matrix metalloproteinase family
    • Parks WC, Mecham RP (eds). San Diego: Academic Press
    • Woessner Jr JF (1998) The matrix metalloproteinase family. In Matrix Metalloproteinases, Parks WC, Mecham RP (eds), pp 1-14. San Diego: Academic Press
    • (1998) Matrix Metalloproteinases , pp. 1-14
    • Woessner Jr., J.F.1
  • 54
    • 0033557316 scopus 로고    scopus 로고
    • Bone resorption induced by parathyroid hormone is strikingly diminished in collagenase-resistant mutant mice
    • Zhao WG, Byrne MH, Boyce BF, Krane SM (1999) Bone resorption induced by parathyroid hormone is strikingly diminished in collagenase-resistant mutant mice. J Clin Invest 103: 517-524
    • (1999) J Clin Invest , vol.103 , pp. 517-524
    • Zhao, W.G.1    Byrne, M.H.2    Boyce, B.F.3    Krane, S.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.