메뉴 건너뛰기




Volumn 382, Issue 1, 2008, Pages 246-256

Differential Unfolding of α1 and α2 Chains in Type I Collagen and Collagenolysis

Author keywords

collagen; collagen degradation; collagenolysis; free energy simulations; protein unfolding

Indexed keywords

COLLAGEN TYPE 1; COLLAGENASE; PROLINE; MUTANT PROTEIN;

EID: 49349102751     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.07.009     Document Type: Article
Times cited : (33)

References (43)
  • 1
    • 0242710145 scopus 로고    scopus 로고
    • Collagens - structure, function, and biosynthesis
    • Gelse K., Pöschl E., and Aigner T. Collagens - structure, function, and biosynthesis. Adv. Drug Deliv. Rev. 55 (2003) 1531-1546
    • (2003) Adv. Drug Deliv. Rev. , vol.55 , pp. 1531-1546
    • Gelse, K.1    Pöschl, E.2    Aigner, T.3
  • 2
    • 0032884147 scopus 로고    scopus 로고
    • Role of matrix metalloproteinases in normal and disease processes
    • McDonnell S., Morgan M., and Lynch C. Role of matrix metalloproteinases in normal and disease processes. Biochem. Soc. Trans. 27 (1999) 734-740
    • (1999) Biochem. Soc. Trans. , vol.27 , pp. 734-740
    • McDonnell, S.1    Morgan, M.2    Lynch, C.3
  • 3
    • 0036516460 scopus 로고    scopus 로고
    • Matrix metalloproteinases: a tail of a frog that became a prince
    • Brinckerhoff C.E., and Matrisian L.M. Matrix metalloproteinases: a tail of a frog that became a prince. Nature Rev. Mol. Cell. Biol. 3 (2002) 207-214
    • (2002) Nature Rev. Mol. Cell. Biol. , vol.3 , pp. 207-214
    • Brinckerhoff, C.E.1    Matrisian, L.M.2
  • 4
    • 0028073883 scopus 로고
    • The role of matrix metalloproteases and their inhibitors in tumour invasion, metastasis and angiogenesis
    • Ray J.M., and Stetler-Stevenson W.G. The role of matrix metalloproteases and their inhibitors in tumour invasion, metastasis and angiogenesis. Eur. Respir. J. 7 (1994) 2062-2072
    • (1994) Eur. Respir. J. , vol.7 , pp. 2062-2072
    • Ray, J.M.1    Stetler-Stevenson, W.G.2
  • 5
    • 0030806173 scopus 로고    scopus 로고
    • Changing views of the role of matrix metalloproteinases in metastasis
    • Chambers A.F., and Matrisian L.M. Changing views of the role of matrix metalloproteinases in metastasis. J. Nat. Cancer Inst. 89 (1997) 1260-1270
    • (1997) J. Nat. Cancer Inst. , vol.89 , pp. 1260-1270
    • Chambers, A.F.1    Matrisian, L.M.2
  • 7
    • 1642390201 scopus 로고    scopus 로고
    • Matrix metalloproteinases: a review of their structure and role in acute coronary syndrome
    • Jones C.B., Sane D.C., and Herrington D.M. Matrix metalloproteinases: a review of their structure and role in acute coronary syndrome. Cardiovasc. Res. 59 (2003) 812-823
    • (2003) Cardiovasc. Res. , vol.59 , pp. 812-823
    • Jones, C.B.1    Sane, D.C.2    Herrington, D.M.3
  • 8
    • 0036741135 scopus 로고    scopus 로고
    • Molecular determinants of metalloproteinase substrate specificity
    • Overall C.M. Molecular determinants of metalloproteinase substrate specificity. Mol. Biotechnol. 22 (2002) 51-86
    • (2002) Mol. Biotechnol. , vol.22 , pp. 51-86
    • Overall, C.M.1
  • 9
    • 0026333465 scopus 로고
    • A model for interstitial collagen catabolism by mammalian collagenases
    • Fields G.B. A model for interstitial collagen catabolism by mammalian collagenases. J. Theor. Biol. 153 (1991) 585-602
    • (1991) J. Theor. Biol. , vol.153 , pp. 585-602
    • Fields, G.B.1
  • 10
    • 0035800664 scopus 로고    scopus 로고
    • The crystal and molecular structure of a collagen-like peptide with a biologically relevant sequence
    • Kramer R.Z., Bella J., Brodsky B., and Berman H.M. The crystal and molecular structure of a collagen-like peptide with a biologically relevant sequence. J. Mol. Biol. 311 (2001) 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
  • 12
    • 5744251586 scopus 로고    scopus 로고
    • Characterization of the distinct collagen binding, helicase and cleavage mechanisms of matrix metalloproteinase 2 and 14 (gelatinase A and MT1-MMP): the differential roles of the MMP hemopexin c domains and the MMP-2 fibronectin type II modules in collagen triple helicase activities
    • Tam E.M., Moore T.R., Butler G.S., and Overall C.M. Characterization of the distinct collagen binding, helicase and cleavage mechanisms of matrix metalloproteinase 2 and 14 (gelatinase A and MT1-MMP): the differential roles of the MMP hemopexin c domains and the MMP-2 fibronectin type II modules in collagen triple helicase activities. J. Biol. Chem. 279 (2004) 43336-43344
    • (2004) J. Biol. Chem. , vol.279 , pp. 43336-43344
    • Tam, E.M.1    Moore, T.R.2    Butler, G.S.3    Overall, C.M.4
  • 13
    • 0036300984 scopus 로고    scopus 로고
    • Localized unfolding of collagen explains collagenase cleavage at imino-poor sites
    • Stultz C.M. Localized unfolding of collagen explains collagenase cleavage at imino-poor sites. J. Mol. Biol. 319 (2002) 997-1003
    • (2002) J. Mol. Biol. , vol.319 , pp. 997-1003
    • Stultz, C.M.1
  • 14
    • 0027731043 scopus 로고
    • 15N NMR relaxation and hydrogen-exchange measurements
    • 15N NMR relaxation and hydrogen-exchange measurements. Biochemistry 32 (1993) 13299-13309
    • (1993) Biochemistry , vol.32 , pp. 13299-13309
    • Fan, P.1    Li, M.2    Brodsky, B.3    Baum, J.4
  • 15
    • 0036303549 scopus 로고    scopus 로고
    • Structural properties of a collagenous heterotrimer that mimics the collagenase cleavage site of collagen type I
    • Fiori S., Saccá B., and Moroder L. Structural properties of a collagenous heterotrimer that mimics the collagenase cleavage site of collagen type I. J. Mol. Biol. 319 (2002) 1235-1242
    • (2002) J. Mol. Biol. , vol.319 , pp. 1235-1242
    • Fiori, S.1    Saccá, B.2    Moroder, L.3
  • 17
  • 18
    • 39749119235 scopus 로고    scopus 로고
    • Do collagenases unwind triple-helical collagen before peptide bond hydrolysis? Reinterpreting experimental observations with mathematical models
    • Nerenberg P.S., Salsas-Escat R., and Stultz C.M. Do collagenases unwind triple-helical collagen before peptide bond hydrolysis? Reinterpreting experimental observations with mathematical models. Proteins: Struct. Funct. Genet. 70 (2008) 1154-1161
    • (2008) Proteins: Struct. Funct. Genet. , vol.70 , pp. 1154-1161
    • Nerenberg, P.S.1    Salsas-Escat, R.2    Stultz, C.M.3
  • 19
    • 0029782362 scopus 로고    scopus 로고
    • Perspectives on the synthesis and application of triple-helical, collagen-model peptides
    • Fields G.B., and Prockop D.J. Perspectives on the synthesis and application of triple-helical, collagen-model peptides. Biopolymers 40 (1996) 345-357
    • (1996) Biopolymers , vol.40 , pp. 345-357
    • Fields, G.B.1    Prockop, D.J.2
  • 20
    • 17444415358 scopus 로고    scopus 로고
    • Molecular structure of the collagen triple helix
    • Brodsky B., and Persikov A.V. Molecular structure of the collagen triple helix. Adv. Protein Chem. 70 (2005) 301-339
    • (2005) Adv. Protein Chem. , vol.70 , pp. 301-339
    • Brodsky, B.1    Persikov, A.V.2
  • 21
    • 0141754092 scopus 로고    scopus 로고
    • A structural model that explains the effects of hyperglycemia on collagenolysis
    • Stultz C.M., and Edelman E.R. A structural model that explains the effects of hyperglycemia on collagenolysis. Biophys. J. 85 (2003) 2198-2204
    • (2003) Biophys. J. , vol.85 , pp. 2198-2204
    • Stultz, C.M.1    Edelman, E.R.2
  • 22
    • 0030602223 scopus 로고    scopus 로고
    • Design and synthesis of heterotrimeric collagen peptides with a built-in cystine-knot. Models for collagen catabolism by matrix-metalloproteases
    • Ottl J., Battistuta R., Pieper M., Tschesche H., Bode W., Kühn K., and Moroder L. Design and synthesis of heterotrimeric collagen peptides with a built-in cystine-knot. Models for collagen catabolism by matrix-metalloproteases. FEBS Lett. 398 (1996) 31-36
    • (1996) FEBS Lett. , vol.398 , pp. 31-36
    • Ottl, J.1    Battistuta, R.2    Pieper, M.3    Tschesche, H.4    Bode, W.5    Kühn, K.6    Moroder, L.7
  • 24
    • 38549097071 scopus 로고    scopus 로고
    • The universal protein resource (UniProt)
    • The UniProt Consortium. The universal protein resource (UniProt). Nucleic Acids Res. 36 (2008) D190-D195
    • (2008) Nucleic Acids Res. , vol.36
    • The UniProt Consortium1
  • 25
    • 0003080378 scopus 로고
    • The chemistry and biology of collagen
    • Neurath H., and Hill R.L. (Eds), Academic Press, New York
    • Bornstein P., and Traub W. The chemistry and biology of collagen. In: Neurath H., and Hill R.L. (Eds). The Proteins. 3rd edit. vol. 4 (1979), Academic Press, New York 411-632
    • (1979) The Proteins. 3rd edit. , vol.4 , pp. 411-632
    • Bornstein, P.1    Traub, W.2
  • 26
    • 0018598695 scopus 로고
    • Covalent structure of collagen: amino acid sequence of α2-CB5 of chick skin collagen containing the animal collagenase cleavage site
    • Dixit S.N., Mainardi C.L., Seyer J.M., and Kang A.H. Covalent structure of collagen: amino acid sequence of α2-CB5 of chick skin collagen containing the animal collagenase cleavage site. Biochemistry 18 (1979) 5416-5422
    • (1979) Biochemistry , vol.18 , pp. 5416-5422
    • Dixit, S.N.1    Mainardi, C.L.2    Seyer, J.M.3    Kang, A.H.4
  • 27
    • 0020634259 scopus 로고
    • Completion of the amino acid sequence of the alpha 1 chain from type I calf skin collagen. Amino acid sequence of α1(I)B8
    • Glanville R.W., Breitkreutz D., Meitinger M., and Fietzek P.P. Completion of the amino acid sequence of the alpha 1 chain from type I calf skin collagen. Amino acid sequence of α1(I)B8. Biochem. J. 215 (1983) 183-189
    • (1983) Biochem. J. , vol.215 , pp. 183-189
    • Glanville, R.W.1    Breitkreutz, D.2    Meitinger, M.3    Fietzek, P.P.4
  • 28
    • 0020492218 scopus 로고
    • Amino acid sequence of chick skin collagen α1(I)-CB8 and the complete primary structure of the helical portion of the chick skin collagen α1(I) chain
    • Highberger J.H., Corbett C., Dixit S.N., Yu W., Seyer J.M., Kang A.H., and Gross J. Amino acid sequence of chick skin collagen α1(I)-CB8 and the complete primary structure of the helical portion of the chick skin collagen α1(I) chain. Biochemistry 21 (1982) 2048-2055
    • (1982) Biochemistry , vol.21 , pp. 2048-2055
    • Highberger, J.H.1    Corbett, C.2    Dixit, S.N.3    Yu, W.4    Seyer, J.M.5    Kang, A.H.6    Gross, J.7
  • 29
    • 0036007873 scopus 로고    scopus 로고
    • Insights on the conformational stability of collagen
    • Jenkins C.L., and Raines R.T. Insights on the conformational stability of collagen. Nature Prod. Rep. 19 (2002) 49-59
    • (2002) Nature Prod. Rep. , vol.19 , pp. 49-59
    • Jenkins, C.L.1    Raines, R.T.2
  • 30
    • 25444463441 scopus 로고    scopus 로고
    • Structure, stability and folding of the collagen triple helix
    • Engel J., and Bächinger H.P. Structure, stability and folding of the collagen triple helix. Top. Curr. Chem. 247 (2005) 7-33
    • (2005) Top. Curr. Chem. , vol.247 , pp. 7-33
    • Engel, J.1    Bächinger, H.P.2
  • 32
    • 43049098250 scopus 로고    scopus 로고
    • Contributions of dipole-dipole interactions to the stability of the collagen triple helix
    • Improta R., Berisio R., and Vitagliano L. Contributions of dipole-dipole interactions to the stability of the collagen triple helix. Protein Sci. 17 (2008) 955-961
    • (2008) Protein Sci. , vol.17 , pp. 955-961
    • Improta, R.1    Berisio, R.2    Vitagliano, L.3
  • 33
    • 42949135530 scopus 로고    scopus 로고
    • Collagen fibril architecture, domain organization, and triple-helical conformation govern its proteolysis
    • Perumal S., Antipova O., and Orgel J.P. Collagen fibril architecture, domain organization, and triple-helical conformation govern its proteolysis. Proc. Natl Acad. Sci. USA 105 (2008) 2824-2829
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 2824-2829
    • Perumal, S.1    Antipova, O.2    Orgel, J.P.3
  • 35
    • 34147150065 scopus 로고    scopus 로고
    • Characterization of the mechanisms by which gelatinase A, neutrophil collagenase, and membrane-type metalloproteinase MMP-14 recognize collagen I and enzymatically process the two α-chains
    • Gioia M., Monaco S., Fasciglione G.F., Coletti A., Modesti A., Marini S., and Coletta M. Characterization of the mechanisms by which gelatinase A, neutrophil collagenase, and membrane-type metalloproteinase MMP-14 recognize collagen I and enzymatically process the two α-chains. J. Mol. Biol. 368 (2007) 1101-1113
    • (2007) J. Mol. Biol. , vol.368 , pp. 1101-1113
    • Gioia, M.1    Monaco, S.2    Fasciglione, G.F.3    Coletti, A.4    Modesti, A.5    Marini, S.6    Coletta, M.7
  • 36
    • 7244253096 scopus 로고    scopus 로고
    • An interactive triple-helical collagen builder
    • Rainey J.K., and Goh M.C. An interactive triple-helical collagen builder. Bioinformatics 20 (2004) 2458-2459
    • (2004) Bioinformatics , vol.20 , pp. 2458-2459
    • Rainey, J.K.1    Goh, M.C.2
  • 38
    • 0000036869 scopus 로고    scopus 로고
    • Simulation of activation free energies in molecular systems
    • Neria E., Fischer S., and Karplus M. Simulation of activation free energies in molecular systems. J. Chem. Phys. 105 (1996) 1902-1921
    • (1996) J. Chem. Phys. , vol.105 , pp. 1902-1921
    • Neria, E.1    Fischer, S.2    Karplus, M.3
  • 40
    • 0001538909 scopus 로고
    • Canonical dynamics: equilibrium phase-space distributions
    • Hoover W.G. Canonical dynamics: equilibrium phase-space distributions. Phys. Rev. A 31 (1985) 1695-1697
    • (1985) Phys. Rev. A , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 41
    • 0041878923 scopus 로고    scopus 로고
    • Modeling induced polarization with classical Drude oscillators: Theory and molecular dynamics simulation algorithm
    • Lamoureux J., and Roux B. Modeling induced polarization with classical Drude oscillators: Theory and molecular dynamics simulation algorithm. J. Chem. Phys. 119 (2003) 3025-3039
    • (2003) J. Chem. Phys. , vol.119 , pp. 3025-3039
    • Lamoureux, J.1    Roux, B.2
  • 42
    • 84986519238 scopus 로고
    • The weighted histogram analysis method for free-energy calculations on biomolecules
    • Kumar S., Rosenberg J.M., Bouzida D., Swendsen R.H., and Kollman P.A. The weighted histogram analysis method for free-energy calculations on biomolecules. J. Comput. Chem. 13 (1992) 1011-1021
    • (1992) J. Comput. Chem. , vol.13 , pp. 1011-1021
    • Kumar, S.1    Rosenberg, J.M.2    Bouzida, D.3    Swendsen, R.H.4    Kollman, P.A.5
  • 43
    • 0035277126 scopus 로고    scopus 로고
    • Extension to the weighted histogram analysis method: combining umbrella sampling with free energy calculations
    • Souaille M., and Roux B. Extension to the weighted histogram analysis method: combining umbrella sampling with free energy calculations. Comput. Phys. Commun. 135 (2001) 40-57
    • (2001) Comput. Phys. Commun. , vol.135 , pp. 40-57
    • Souaille, M.1    Roux, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.