메뉴 건너뛰기




Volumn 4, Issue 8, 2004, Pages 617-629

Matrix metalloproteinases as modulators of inflammation and innate immunity

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLSALICYLIC ACID; AE 941; ALPHA 2 MACROGLOBULIN; BISPHOSPHONIC ACID DERIVATIVE; CATECHIN; CHEMOKINE; COLLAGENASE 3; DOXYCYCLINE; DOXYCYCLINE HYCLATE; GELATINASE A; GELATINASE B; HYDROXAMIC ACID DERIVATIVE; INTERLEUKIN 13; INTERSTITIAL COLLAGENASE; MACROPHAGE ELASTASE; MATRILYSIN; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE 14; NATURAL PRODUCT; NEUTROPHIL COLLAGENASE; PRINOMASTAT; STROMELYSIN; TANOMASTAT; TETRACYCLINE DERIVATIVE; TISSUE INHIBITOR OF METALLOPROTEINASE; TISSUE INHIBITOR OF METALLOPROTEINASE 1; TISSUE INHIBITOR OF METALLOPROTEINASE 2; TISSUE INHIBITOR OF METALLOPROTEINASE 3; TISSUE INHIBITOR OF METALLOPROTEINASE 4; TUMOR NECROSIS FACTOR;

EID: 3543134126     PISSN: 14741733     EISSN: None     Source Type: Journal    
DOI: 10.1038/nri1418     Document Type: Review
Times cited : (1581)

References (144)
  • 1
    • 0033582513 scopus 로고    scopus 로고
    • Cloning and characterization of human MMP-23, a new matrix metalloproteinase predominantly expressed in reproductive tissues and lacking conserved domains in other family members
    • Velasco, G. et al. Cloning and characterization of human MMP-23, a new matrix metalloproteinase predominantly expressed in reproductive tissues and lacking conserved domains in other family members. J. Biol. Chem. 274, 4570-4576 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 4570-4576
    • Velasco, G.1
  • 2
    • 0027515396 scopus 로고
    • Astacins, serralysins, snake venom and matrix metalloproteinases, exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'
    • Bode, W., Gomis-Ruth, F. X. & Stockler, W. Astacins, serralysins, snake venom and matrix metalloproteinases, exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'. FEBS Lett. 331, 134-140 (1993).
    • (1993) FEBS Lett. , vol.331 , pp. 134-140
    • Bode, W.1    Gomis-Ruth, F.X.2    Stockler, W.3
  • 3
    • 0031656460 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Structures, evolution, and diversification
    • Massova, I., Kotra, L. P., Fridman, R. & Mobashery, S. Matrix metalloproteinases: structures, evolution, and diversification. FASEB J. 12, 1075-1095 (1998).
    • (1998) FASEB J. , vol.12 , pp. 1075-1095
    • Massova, I.1    Kotra, L.P.2    Fridman, R.3    Mobashery, S.4
  • 4
    • 0031671855 scopus 로고    scopus 로고
    • Matrix metalloproteinase degradation of extracellular matrix: Biological consequences
    • Shapiro, S. D. Matrix metalloproteinase degradation of extracellular matrix: biological consequences. Curr. Opin. Cell Biol. 10, 602-608 (1998).
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 602-608
    • Shapiro, S.D.1
  • 5
    • 0025025442 scopus 로고
    • The cysteine switch: A principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family
    • Van Wart, H. E. & Birkedal-Hansen, H. The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc. Natl. Acad. Sci. USA 87, 5578-5582 (1990).
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5578-5582
    • Van Wart, H.E.1    Birkedal-Hansen, H.2
  • 6
    • 0028907318 scopus 로고
    • Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease
    • Strongin, A. Y. et al. Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease. J. Biol. Chem. 270, 5331-5338 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 5331-5338
    • Strongin, A.Y.1
  • 7
    • 0034697144 scopus 로고    scopus 로고
    • Binding of active (57 kDa) membrane type 1-matrix metalloproteinase (MT1-MMP) to tissue inhibitor of metalloproteinase (TIMP)-2 regulates MT1-MMP processing and pro-MMP-2 activation
    • Hernandez-Barrantes, S. et al. Binding of active (57 kDa) membrane type 1-matrix metalloproteinase (MT1-MMP) to tissue inhibitor of metalloproteinase (TIMP)-2 regulates MT1-MMP processing and pro-MMP-2 activation. J. Biol. Chem. 275, 12080-12089 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 12080-12089
    • Hernandez-Barrantes, S.1
  • 8
    • 0034714202 scopus 로고    scopus 로고
    • TIMP-2 is required for efficient activation of proMMP-2 in vivo
    • Wang, Z., Juttermann, R. & Soloway, P. D. TIMP-2 is required for efficient activation of proMMP-2 in vivo. J. Biol. Chem. 275, 26411-26415 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 26411-26415
    • Wang, Z.1    Juttermann, R.2    Soloway, P.D.3
  • 9
    • 0034714348 scopus 로고    scopus 로고
    • Inactivating mutation of the mouse tissue inhibitor of metalloproteineses-2 (Timp-2) gene alters proMMP-2 activation
    • Caterina, J. J. et al, Inactivating mutation of the mouse tissue inhibitor of metalloproteineses-2 (Timp-2) gene alters proMMP-2 activation. J. Biol. Chem. 275, 26416-26422 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 26416-26422
    • Caterina, J.J.1
  • 10
    • 0035896646 scopus 로고    scopus 로고
    • Extracellular matrix metalloproteinase 2 levels are regulated by the low density lipoprotein-related scavenger receptor and thrombospondin 2
    • Yang, Z., Strickland, D. K. & Bornstein, P. Extracellular matrix metalloproteinase 2 levels are regulated by the low density lipoprotein-related scavenger receptor and thrombospondin 2. J. Biol. Chem. 276, 8403-8408 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 8403-8408
    • Yang, Z.1    Strickland, D.K.2    Bornstein, P.3
  • 11
    • 0033569725 scopus 로고    scopus 로고
    • Collagenase-3 binds to a specific receptor and requires the low density lipoprotein receptor-related protein for internalization
    • Barmina, O. Y. et al. Collagenase-3 binds to a specific receptor and requires the low density lipoprotein receptor-related protein for internalization. J. Biol. Chem. 274, 30087-30093 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 30087-30093
    • Barmina, O.Y.1
  • 12
    • 0021961153 scopus 로고
    • Oxidative autoactivation of latent collagenase by human neutrophils
    • Weiss, S. J., Peppin, G., Ortiz, X., Ragsdale, C. & Test, S. T. Oxidative autoactivation of latent collagenase by human neutrophils. Science 227, 747-749 (1985).
    • (1985) Science , vol.227 , pp. 747-749
    • Weiss, S.J.1    Peppin, G.2    Ortiz, X.3    Ragsdale, C.4    Test, S.T.5
  • 13
    • 0011489860 scopus 로고
    • Activation of the endogenous metalloproteinase, gelatinase, by triggered human neutrophils
    • Peppin, G. J. & Weiss, S. J. Activation of the endogenous metalloproteinase, gelatinase, by triggered human neutrophils. Proc. Natl. Acad. Sci. USA 83, 4322-4326 (1986).
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4322-4326
    • Peppin, G.J.1    Weiss, S.J.2
  • 14
    • 0035798684 scopus 로고    scopus 로고
    • Hypochlorous acid oxygenates the cysteine switch domain of pro-matrilysin (MMP-7). A mechanism for matrix metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase
    • Fu, X., Kassim, S. Y., Parks, W. C. & Heinecke, J. W. Hypochlorous acid oxygenates the cysteine switch domain of pro-matrilysin (MMP-7). A mechanism for matrix metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase. J. Biol. Chem. 276, 41279-41287 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 41279-41287
    • Fu, X.1    Kassim, S.Y.2    Parks, W.C.3    Heinecke, J.W.4
  • 15
    • 0037119624 scopus 로고    scopus 로고
    • S-nitrosylation of matrix metalloproteinases: Signaling pathway to neuronal cell death
    • Gu, Z. et al. S-nitrosylation of matrix metalloproteinases: signaling pathway to neuronal cell death. Science 297, 1186-1190 (2002).
    • (2002) Science , vol.297 , pp. 1186-1190
    • Gu, Z.1
  • 16
    • 0042093741 scopus 로고    scopus 로고
    • Hypochlorous acid generated by myeloperoxidase modifies adjacent tryptophan and glycine residues in the catalytic domain of matrix metalloproteinase-7 (matrilsin): An oxidative mechanism for restraining proteolytic activity during inflammation
    • Fu, X., Kassim, S. Y., Parks, W. C. & Heinecke, J. W. Hypochlorous acid generated by myeloperoxidase modifies adjacent tryptophan and glycine residues in the catalytic domain of matrix metalloproteinase-7 (matrilsin): an oxidative mechanism for restraining proteolytic activity during inflammation. J. Biol. Chem. 278, 28403-28409 (2003). References 12-16 show that reactive metabolites, often leukocyte-generated oxidants, can both activate and inactivate the catalytic activity of MMPs. Although these mechanisms have not yet been shown in vivo, they are probably important for the regulation of MMPs in inflammation.
    • (2003) J. Biol. Chem. , vol.278 , pp. 28403-28409
    • Fu, X.1    Kassim, S.Y.2    Parks, W.C.3    Heinecke, J.W.4
  • 17
    • 0035188727 scopus 로고    scopus 로고
    • How matrix metalloproteinases regulate cell behavior
    • Sternlicht, M. D. & Werb, Z. How matrix metalloproteinases regulate cell behavior. Annu. Rev. Cell Dev. Biol. 17, 463-516 (2001).
    • (2001) Annu. Rev. Cell Dev. Biol. , vol.17 , pp. 463-516
    • Sternlicht, M.D.1    Werb, Z.2
  • 18
    • 0025651681 scopus 로고
    • Studies on the ability of 65-kDa and 92-kDa tumor cell gelatinases to degrade type IV collagen
    • Mackay, A. R., Hartzler, J. L., Palina, M. D. & Thorgeirsson, U. P. Studies on the ability of 65-kDa and 92-kDa tumor cell gelatinases to degrade type IV collagen. J. Biol. Chem. 265, 21929-21934 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 21929-21934
    • Mackay, A.R.1    Hartzler, J.L.2    Palina, M.D.3    Thorgeirsson, U.P.4
  • 19
    • 0029817688 scopus 로고    scopus 로고
    • Matrilysin is expressed by lipid-laden macrophages at sites of potential rupture in atherosclerotic lesions and localizes to areas of versican deposition, a proteoglycan substrate for the enzyme
    • Halpert, I. et al. Matrilysin is expressed by lipid-laden macrophages at sites of potential rupture in atherosclerotic lesions and localizes to areas of versican deposition, a proteoglycan substrate for the enzyme. Proc. Natl. Acad. Sci. USA 93, 9748-9753 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9748-9753
    • Halpert, I.1
  • 20
    • 15844420283 scopus 로고    scopus 로고
    • 3
    • 3. Cell 85, 683-693 (1996).
    • (1996) Cell , vol.85 , pp. 683-693
    • Brooks, P.C.1
  • 21
    • 0035800766 scopus 로고    scopus 로고
    • 1 upon release from keratinocytes migrating on type I collagen
    • 1 upon release from keratinocytes migrating on type I collagen. J. Biol. Chem. 276, 29368-29374 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 29368-29374
    • Dumin, J.A.1
  • 22
    • 0035800834 scopus 로고    scopus 로고
    • 2 integrin I domain/procollagenase-1 (matrix metalloproteinase-1) interaction
    • 2 integrin I domain/procollagenase-1 (matrix metalloproteinase-1) interaction, J. Biol. Chem. 276, 29375-29381 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 29375-29381
    • Stricker, T.P.1
  • 23
    • 0034650486 scopus 로고    scopus 로고
    • Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-β and promotes tumor invasion and angiogenesis
    • Yu, Q. & Stamenkovic, I. Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-β and promotes tumor invasion and angiogenesis. Genes Dev. 14, 163-176 (2000).
    • (2000) Genes Dev. , vol.14 , pp. 163-176
    • Yu, Q.1    Stamenkovic, I.2
  • 24
    • 0034635483 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans as extracellular docking molecules for matrilysin (matrix metalloproteinase 7)
    • Yu, W. H. & Woessner, J. F. Jr. Heparan sulfate proteoglycans as extracellular docking molecules for matrilysin (matrix metalloproteinase 7). J. Biol. Chem. 275, 4183-4191 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 4183-4191
    • Yu, W.H.1    Woessner Jr., J.F.2
  • 25
    • 0036468005 scopus 로고    scopus 로고
    • CD44 anchors the assembly of matrilysin/MMP-7 with heparin-binding epidermal growth factor precursor and ErbB4 and regulates female reproductive organ remodeling
    • Yu, W. H., Woessner, J. F. Jr, McNeish, J. D. & Stamenkovic, I. CD44 anchors the assembly of matrilysin/MMP-7 with heparin-binding epidermal growth factor precursor and ErbB4 and regulates female reproductive organ remodeling. Genes Dev. 16, 307-323 (2002). This paper provides a good example of how a 'secreted' MMP is bound to and compartmentalized by a cell-surface molecule.
    • (2002) Genes Dev. , vol.16 , pp. 307-323
    • Yu, W.H.1    Woessner Jr., J.F.2    McNeish, J.D.3    Stamenkovic, I.4
  • 26
    • 0345935809 scopus 로고
    • Collagenolytic activity in amphipian tissues: A tissue culture assay
    • Gross, J. & Lapiere, C. M. Collagenolytic activity in amphipian tissues: a tissue culture assay. Proc. Natl Acad. Sci. USA 48, 1014-1022 (1962).
    • (1962) Proc. Natl Acad. Sci. USA , vol.48 , pp. 1014-1022
    • Gross, J.1    Lapiere, C.M.2
  • 27
    • 0034682885 scopus 로고    scopus 로고
    • Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3
    • McQuibban, G.A. et al. Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3. Science 289, 1202-1206 (2000). This paper shows how exosite scanning and yeast two-hybrid techniques can be used to identify novel MMP substrates: in this case, chemokines. Together with other studies by these investigators (references 54 and 55), this study provides evidence that MMP proteolysis directly regulates chemokine activity.
    • (2000) Science , vol.289 , pp. 1202-1206
    • McQuibban, G.A.1
  • 28
    • 0036052092 scopus 로고    scopus 로고
    • A proteomic approach for the identification of cell-surface proteins shed by metalloproteases
    • Guo, L. et al. A proteomic approach for the identification of cell-surface proteins shed by metalloproteases. Mol. Cell Proteomics 1, 30-36 (2002).
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 30-36
    • Guo, L.1
  • 29
    • 2342460878 scopus 로고    scopus 로고
    • Membrane protease proteomics: Isotopecoded affinity tag MS identification of undescribed MT1-matrix metalloproteinase substrates
    • Tam, E. M., Morrison, C. J., Wu, Y. I., Stack, M. S. & Overall, C. M. Membrane protease proteomics: isotopecoded affinity tag MS identification of undescribed MT1-matrix metalloproteinase substrates. Proc. Natl Acad. Sci. USA 101, 6917-6922 (2004). This paper describes a proteomics study using state-of-the-art technology to identify MMP substrates. This knowledge is essential for understanding the function of these enzymes in vivo.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 6917-6922
    • Tam, E.M.1    Morrison, C.J.2    Wu, Y.I.3    Stack, M.S.4    Overall, C.M.5
  • 30
    • 0035479845 scopus 로고    scopus 로고
    • Matrix metalloproteinases: They're not just for matrix anymore!
    • McCawley, L. J. & Matrisian, L. M. Matrix metalloproteinases: they're not just for matrix anymore! Curr. Opin. Cell Biol. 13, 534-540 (2001).
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 534-540
    • McCawley, L.J.1    Matrisian, L.M.2
  • 31
    • 2142784516 scopus 로고    scopus 로고
    • MT1-MMP-deficient mice develop dwarfism, osteopenia, arthritis, and connective tissue disease due to inadequate collagen turnover
    • Holmbeck, K. et al. MT1-MMP-deficient mice develop dwarfism, osteopenia, arthritis, and connective tissue disease due to inadequate collagen turnover. Cell 99, 81-92 (1999).
    • (1999) Cell , vol.99 , pp. 81-92
    • Holmbeck, K.1
  • 32
    • 0034635966 scopus 로고    scopus 로고
    • Impaired endochondral ossification and angiogenesis in mice deficient in membrane-type matrix metalloproteinase I
    • Zhou, Z. et al. Impaired endochondral ossification and angiogenesis in mice deficient in membrane-type matrix metalloproteinase I. Proc. Natl Acad. Sci. USA 97, 4052-4057 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 4052-4057
    • Zhou, Z.1
  • 33
    • 0034641107 scopus 로고    scopus 로고
    • Regulation of cell invasion and morphogenesis in a three-dimensional type I collagen matrix by membrane-type matrix metalloproteinases 1, 2, and 3
    • Hotary, K., Allen, E., Punturieri, A., Yana, I. & Weiss, S. J. Regulation of cell invasion and morphogenesis in a three-dimensional type I collagen matrix by membrane-type matrix metalloproteinases 1, 2, and 3. J. Cell Biol. 149. 1309-1323 (2000).
    • (2000) J. Cell Biol. , vol.149 , pp. 1309-1323
    • Hotary, K.1    Allen, E.2    Punturieri, A.3    Yana, I.4    Weiss, S.J.5
  • 34
    • 0037017385 scopus 로고    scopus 로고
    • Matrix metalloproteinases (MMPs) regulate fibrin-invasive activity via MT1-MMP-dependent and -independent processes
    • Hotary K. B. et al. Matrix metalloproteinases (MMPs) regulate fibrin-invasive activity via MT1-MMP-dependent and -independent processes. J. Exp. Med. 195, 295-308 (2002).
    • (2002) J. Exp. Med. , vol.195 , pp. 295-308
    • Hotary, K.B.1
  • 35
    • 0141449964 scopus 로고    scopus 로고
    • Matrilysin-dependent elastolysis by human macrophages
    • Filippov, S. et al. Matrilysin-dependent elastolysis by human macrophages. J. Exp. Med. 198, 925-935 (2003).
    • (2003) J. Exp. Med. , vol.198 , pp. 925-935
    • Filippov, S.1
  • 36
  • 37
    • 0037180812 scopus 로고    scopus 로고
    • Points of control in inflammation
    • Nathan, C. Points of control in inflammation. Nature 420, 846-852 (2002).
    • (2002) Nature , vol.420 , pp. 846-852
    • Nathan, C.1
  • 38
    • 1842738493 scopus 로고    scopus 로고
    • Subantimicrobial dose doxycycline efficacy as a matrix metalloproteinase inhibitor in chronic periodontits patients is enhanced when combined with a non-steroidal anti-inflammatory drug
    • Lee, H. M. et al. Subantimicrobial dose doxycycline efficacy as a matrix metalloproteinase inhibitor in chronic periodontits patients is enhanced when combined with a non-steroidal anti-inflammatory drug. J. Periodontol. 75, 453-463 (2004).
    • (2004) J. Periodontol. , vol.75 , pp. 453-463
    • Lee, H.M.1
  • 39
    • 3343006385 scopus 로고    scopus 로고
    • Metalloprotease inhibitors as anti-inflammatory agents: An evolving target?
    • Whelan, C. J. Metalloprotease inhibitors as anti-inflammatory agents: an evolving target? Curr. Opin. Investig. Drugs 5, 511-516 (2004).
    • (2004) Curr. Opin. Investig. Drugs , vol.5 , pp. 511-516
    • Whelan, C.J.1
  • 40
    • 0037261987 scopus 로고    scopus 로고
    • Matrix metalloproteinases: A therapeutic target in cardiovascular disease
    • Sierevogel, M. J., Pasterkamp, G., de Kleijn, D. P. & Strauss, B. H. Matrix metalloproteinases: a therapeutic target in cardiovascular disease. Curr. Pharm. Des. 9, 1033-1040 (2003).
    • (2003) Curr. Pharm. Des. , vol.9 , pp. 1033-1040
    • Sierevogel, M.J.1    Pasterkamp, G.2    De Kleijn, D.P.3    Strauss, B.H.4
  • 41
    • 0036721806 scopus 로고    scopus 로고
    • The role of matrix metalloproteinase-2 and matrix metalloproteinase-9 in antibody-induced arthritis
    • Itoh, T. et al. The role of matrix metalloproteinase-2 and matrix metalloproteinase-9 in antibody-induced arthritis. J. Immunol. 169, 2643-2647 (2002).
    • (2002) J. Immunol. , vol.169 , pp. 2643-2647
    • Itoh, T.1
  • 42
    • 14444285039 scopus 로고    scopus 로고
    • Susceptibility of stromelysin 1-deficient mice to collagen-induced arthritis and cartilage destruction
    • Mudgett, J. S. et al. Susceptibility of stromelysin 1-deficient mice to collagen-induced arthritis and cartilage destruction. Arthritis Rheum. 41, 110-121 (1998).
    • (1998) Arthritis Rheum. , vol.41 , pp. 110-121
    • Mudgett, J.S.1
  • 43
    • 0033380154 scopus 로고    scopus 로고
    • Matrix metalloproteinases in repair
    • Parks, W. C. Matrix metalloproteinases in repair. Wound Repair Regen. 7, 423-432 (1999).
    • (1999) Wound Repair Regen. , vol.7 , pp. 423-432
    • Parks, W.C.1
  • 44
    • 0030949650 scopus 로고    scopus 로고
    • The activity of collagenase-1 is required for keratinocyte migration on a type I collagen matrix
    • Pilcher, B. K. et al. The activity of collagenase-1 is required for keratinocyte migration on a type I collagen matrix. J. Cell Biol. 137, 1445-1457 (1997).
    • (1997) J. Cell Biol. , vol.137 , pp. 1445-1457
    • Pilcher, B.K.1
  • 45
    • 0032189325 scopus 로고    scopus 로고
    • Matrilysin expression and function in airway epithelium
    • Dunsmore, S. E. et al. Matrilysin expression and function in airway epithelium. J. Clin. Invest. 102, 1321-1331 (1998).
    • (1998) J. Clin. Invest. , vol.102 , pp. 1321-1331
    • Dunsmore, S.E.1
  • 46
    • 0037568364 scopus 로고    scopus 로고
    • Matrilysin (matrix metalloproteinase-7) mediates E-cadherin ectodomain shedding in injured lung epithelium
    • McGuire, J. K., Li, O. & Pariks, W. C. Matrilysin (matrix metalloproteinase-7) mediates E-cadherin ectodomain shedding in injured lung epithelium. Am. J. Pathol. 162, 1831-1843 (2003).
    • (2003) Am. J. Pathol. , vol.162 , pp. 1831-1843
    • McGuire, J.K.1    Li, O.2    Pariks, W.C.3
  • 47
    • 0033606774 scopus 로고    scopus 로고
    • Airway epithelial cell migration dynamics: MMP-9 role in cell-extracellular matrix remodeling
    • Legrand, C. et al. Airway epithelial cell migration dynamics: MMP-9 role in cell-extracellular matrix remodeling. J. Cell Biol. 146, 517-529 (1999).
    • (1999) J. Cell Biol. , vol.146 , pp. 517-529
    • Legrand, C.1
  • 48
    • 0033873628 scopus 로고    scopus 로고
    • Gelatinase B is required for alveolar bronchiolization after intratracheal bleomycin
    • Betsuyaku, T., Fukuda, Y., Parks, W. C., Shipley, J. M. & Senior, R. M. Gelatinase B is required for alveolar bronchiolization after intratracheal bleomycin. Am. J. Pathol. 157, 525-535 (2000).
    • (2000) Am. J. Pathol. , vol.157 , pp. 525-535
    • Betsuyaku, T.1    Fukuda, Y.2    Parks, W.C.3    Shipley, J.M.4    Senior, R.M.5
  • 49
    • 0029157653 scopus 로고
    • Matrix metalloproteinase matrilysin is constitutively expressed in human exocrine epithelium
    • Saarialho-Kere, U. K., Crouch, E. C. & Parks, W. C. Matrix metalloproteinase matrilysin is constitutively expressed in human exocrine epithelium. J. Invest. Dermatol. 105, 190-196 (1995).
    • (1995) J. Invest. Dermatol. , vol.105 , pp. 190-196
    • Saarialho-Kere, U.K.1    Crouch, E.C.2    Parks, W.C.3
  • 50
    • 0029819784 scopus 로고    scopus 로고
    • Paneth cell defensins: Endogenous peptide components of intestinal host defense
    • Ouellette, A. J. & Selsted, M. E. Paneth cell defensins: endogenous peptide components of intestinal host defense. FASEB J. 10, 1280-1289 (1996).
    • (1996) FASEB J. , vol.10 , pp. 1280-1289
    • Ouellette, A.J.1    Selsted, M.E.2
  • 51
    • 0033214433 scopus 로고    scopus 로고
    • Regulation of intestinal α-defensin activation by the metalloproteinase matrilysin in innate host defense
    • Wilson, C. L. et al. Regulation of intestinal α-defensin activation by the metalloproteinase matrilysin in innate host defense. Science 286, 113-117 (1999). This study identifies α-defensins as a new class of substrates for MMPs and demonstrates a specific role for MMP7 in innate immunity.
    • (1999) Science , vol.286 , pp. 113-117
    • Wilson, C.L.1
  • 52
    • 0032553579 scopus 로고    scopus 로고
    • Induction and evasion of host defenses by type 1-piliated uropathogenic Escherichia coli
    • Mulvey, M. A. et al. Induction and evasion of host defenses by type 1-piliated uropathogenic Escherichia coli. Science 262, 1494-1497 (1998).
    • (1998) Science , vol.262 , pp. 1494-1497
    • Mulvey, M.A.1
  • 53
    • 0033576645 scopus 로고    scopus 로고
    • The metalloproteinase matrilysin proteolytically generates active soluble Fas ligand and potentiates epithelial cell apoptosis
    • Powell, W. C., Fingleton, B., Wilson, C. L., Boothby, M. & Matrisian, L. M. The metalloproteinase matrilysin proteolytically generates active soluble Fas ligand and potentiates epithelial cell apoptosis. Curr. Biol. 9, 1441-1447 (1999). This study establishes that FASL is a substrate for MMP7. MMP-mediated apoptosis, through the activation of FASL, might provide a mechanism for bacterial clearance, as indicated in figure 4.
    • (1999) Curr. Biol. , vol.9 , pp. 1441-1447
    • Powell, W.C.1    Fingleton, B.2    Wilson, C.L.3    Boothby, M.4    Matrisian, L.M.5
  • 54
    • 0032793096 scopus 로고    scopus 로고
    • Macrophage elastase prevents Gemella morbillorum infection and improves outcome following murine bone marrow transplantation
    • Hartzell, W. & Shapiro, S. D. Macrophage elastase prevents Gemella morbillorum infection and improves outcome following murine bone marrow transplantation. Chest 116, 31S-32S (1999).
    • (1999) Chest , vol.116
    • Hartzell, W.1    Shapiro, S.D.2
  • 55
    • 0034689027 scopus 로고    scopus 로고
    • Bacterial exposure induces and activates matrilysin in mucosal epithelial cells
    • López-Boado, Y. S. et al. Bacterial exposure induces and activates matrilysin in mucosal epithelial cells. J. Cell Biol. 148, 1305-1315 (2000).
    • (2000) J. Cell Biol. , vol.148 , pp. 1305-1315
    • López-Boado, Y.S.1
  • 56
    • 0035798708 scopus 로고    scopus 로고
    • Regulation of matrilysin expression in airway epithelial cells by Pseudomonas aeruginosa flagellin
    • López-Boado, Y. S., Wilson, C. L. & Parks, W. C. Regulation of matrilysin expression in airway epithelial cells by Pseudomonas aeruginosa flagellin. J. Biol. Chem. 276, 41417-41423 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 41417-41423
    • López-Boado, Y.S.1    Wilson, C.L.2    Parks, W.C.3
  • 57
    • 0030061278 scopus 로고    scopus 로고
    • Matrilysin: An epithelial matrix metalloproteinase with potentially novel functions
    • Wilson, C. L. & Matrisian, L. M. Matrilysin: an epithelial matrix metalloproteinase with potentially novel functions. Int. J. Biochem. Cell Biol. 28, 123-136 (1996).
    • (1996) Int. J. Biochem. Cell Biol. , vol.28 , pp. 123-136
    • Wilson, C.L.1    Matrisian, L.M.2
  • 58
    • 0030747245 scopus 로고    scopus 로고
    • Epithelial cells as sensors for microbiol infection
    • Kagnoff, M. F. & Eckmann, L. Epithelial cells as sensors for microbiol infection. J. Clin. Invest. 100, 6-10 (1997).
    • (1997) J. Clin. Invest. , vol.100 , pp. 6-10
    • Kagnoff, M.F.1    Eckmann, L.2
  • 60
    • 0037103183 scopus 로고    scopus 로고
    • Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties in vivo
    • McQuibban, G. A. et al. Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties in vivo. Blood 100, 1160-1167 (2002).
    • (2002) Blood , vol.100 , pp. 1160-1167
    • McQuibban, G.A.1
  • 61
    • 0035941359 scopus 로고    scopus 로고
    • Matrix metalloproteinase activity inactivates the CXC chemokine stromal cell-derived factor-1
    • McQuibban, G.A. etal. Matrix metalloproteinase activity inactivates the CXC chemokine stromal cell-derived factor-1. J. Biol. Chem. 276, 43503-43508 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 43503-43508
    • McQuibban, G.A.1
  • 62
    • 0034667542 scopus 로고    scopus 로고
    • Neutrophil gelatinase B potentiates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAP-III, PF-4, and GRO-α and leaves RANTES and MCP-2 intact
    • Van den Steen, P. E., Proost, P., Wuyts, A., Van Damme, J. & Opdenakker, G. Neutrophil gelatinase B potentiates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAP-III, PF-4, and GRO-α and leaves RANTES and MCP-2 intact. Blood 96, 2673-2681 (2000).
    • (2000) Blood , vol.96 , pp. 2673-2681
    • Van Den Steen, P.E.1    Proost, P.2    Wuyts, A.3    Van Damme, J.4    Opdenakker, G.5
  • 63
    • 0141782259 scopus 로고    scopus 로고
    • Gelatinase B/MMP-9 and neutrophil collagenase/MMP-8 process the chemokines human GCP-2/CXCL6, ENA-78/CXCL5 and mouse GCP-2/UX and modulate their physiological activities
    • Van Den Steen, P. E. et al. Gelatinase B/MMP-9 and neutrophil collagenase/MMP-8 process the chemokines human GCP-2/CXCL6, ENA-78/CXCL5 and mouse GCP-2/UX and modulate their physiological activities. Eur. J. Biochem. 270, 3739-3749 (2003).
    • (2003) Eur. J. Biochem. , vol.270 , pp. 3739-3749
    • Van Den Steen, P.E.1
  • 64
    • 0036229419 scopus 로고    scopus 로고
    • Decreased allergic lung inflammatory cell egression and increased susceptibility to asphyxiation in MMP2-deficiency
    • Corry, D. B. et al. Decreased allergic lung inflammatory cell egression and increased susceptibility to asphyxiation in MMP2-deficiency. Nature Immunol. 3, 347-353 (2002). One the first papers to show that MMPs establish chemokine gradients in vivo. Reference 71 is a follow-up to these studies.
    • (2002) Nature Immunol. , vol.3 , pp. 347-353
    • Corry, D.B.1
  • 65
    • 0032845155 scopus 로고    scopus 로고
    • Prevention of interleukin-8-induced mobilization of hematopoietic progenitor cells in rhesus monkeys by inhibitory antibodies against the metalloproteinase gelatinase B (MMP-9)
    • Pruijt, J. F. et al. Prevention of interleukin-8-induced mobilization of hematopoietic progenitor cells in rhesus monkeys by inhibitory antibodies against the metalloproteinase gelatinase B (MMP-9). Proc. Natl Acad. Sci. USA 96, 10863-10868 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 10863-10868
    • Pruijt, J.F.1
  • 66
    • 18744383614 scopus 로고    scopus 로고
    • Matrilysin shedding of syndecan-1 regulates chemokine mobilization and transepithelial efflux of neutrophils in acute lung injury
    • Li, Q., Park, P. W., Wilson, O. L. & Parks, W. C. Matrilysin shedding of syndecan-1 regulates chemokine mobilization and transepithelial efflux of neutrophils in acute lung injury. Cell 111, 635-646 (2002). This paper describes a mechanism in which three epithelial products - an MMP, a CXC-chemokine and a proteoglycan - interact to control and coordinate acute inflammation at sites of injury.
    • (2002) Cell , vol.111 , pp. 635-646
    • Li, Q.1    Park, P.W.2    Wilson, O.L.3    Parks, W.C.4
  • 67
    • 0141653868 scopus 로고    scopus 로고
    • HIV-induced metalloproteinase processing of the chemokine stromal cell derived factor-1 causes neurodegeneration
    • Zhang, K. et al. HIV-induced metalloproteinase processing of the chemokine stromal cell derived factor-1 causes neurodegeneration. Nature Neurosci. 6, 1064-1071 (2003). This interesting study shows that MMP2 secreted by HIV-infected macrophages cleaves CXCL12 to generate a potent neurotoxin.
    • (2003) Nature Neurosci. , vol.6 , pp. 1064-1071
    • Zhang, K.1
  • 68
    • 0242361314 scopus 로고    scopus 로고
    • Loss of collagenase-2 confers increased skin tumor susceptibility to male mice
    • Balbin, M. et al. Loss of collagenase-2 confers increased skin tumor susceptibility to male mice. Nature Genet. 35, 252-257 (2003).
    • (2003) Nature Genet. , vol.35 , pp. 252-257
    • Balbin, M.1
  • 69
    • 0033120707 scopus 로고    scopus 로고
    • Metalloproteinases are involved in lipopolysaccharide- and tumor necrosis factor-α-mediated regulation of CXCR1 and CXCR2 chemokine receptor expression
    • Khandaker, M. H. et al. Metalloproteinases are involved in lipopolysaccharide- and tumor necrosis factor-α-mediated regulation of CXCR1 and CXCR2 chemokine receptor expression. Blood 93, 2173-2185 (1999).
    • (1999) Blood , vol.93 , pp. 2173-2185
    • Khandaker, M.H.1
  • 70
    • 0029356278 scopus 로고
    • The role of tumor necrosis factor in increased airspace epithelial permeability in acute lung inflammation
    • Li, X. Y., Donaldson, K., Brown, D. & Macnee, W. The role of tumor necrosis factor in increased airspace epithelial permeability in acute lung inflammation. Am. J. Resp. Cell Mol. Biol. 13, 185-195 (1995).
    • (1995) Am. J. Resp. Cell Mol. Biol. , vol.13 , pp. 185-195
    • Li, X.Y.1    Donaldson, K.2    Brown, D.3    Macnee, W.4
  • 71
    • 3543136879 scopus 로고    scopus 로고
    • Overlapping and independent contributions of MMP2 and MMP9 to lung allergic inflammatory cell egression through decreased CC chemokines
    • Corry, D. B. et al. Overlapping and independent contributions of MMP2 and MMP9 to lung allergic inflammatory cell egression through decreased CC chemokines. FASEB J. 18, 995-997 (2004).
    • (2004) FASEB J. , vol.18 , pp. 995-997
    • Corry, D.B.1
  • 72
    • 0033966204 scopus 로고    scopus 로고
    • Matrix metalloproteinase-3-dependent generation of a macrophage chemoattractant in a model of herniated disc resorption
    • Haro, H. et al. Matrix metalloproteinase-3-dependent generation of a macrophage chemoattractant in a model of herniated disc resorption. J. Clin. Invest. 105, 133-141 (2000). Together with reference 102, this paper shows that specific MMPs function as crucial components of an inflammatory network between different cell types, using a model of tissue resorption.
    • (2000) J. Clin. Invest. , vol.105 , pp. 133-141
    • Haro, H.1
  • 73
    • 0030823772 scopus 로고    scopus 로고
    • Requirement for macrophage elastase for cigarette smoke-induced emphysema
    • Hautamaki, R. D., Kobayashi, D. K., Senior, R. M. & Shapiro, S. D. Requirement for macrophage elastase for cigarette smoke-induced emphysema. Science 277, 2002-2004 (1997).
    • (1997) Science , vol.277 , pp. 2002-2004
    • Hautamaki, R.D.1    Kobayashi, D.K.2    Senior, R.M.3    Shapiro, S.D.4
  • 74
    • 0038015502 scopus 로고    scopus 로고
    • Gelatinase B/matrix metalloproteinase-9 cleaves interferon-β and is a target for immunotherapy
    • Nelissen, I. et al. Gelatinase B/matrix metalloproteinase-9 cleaves interferon-β and is a target for immunotherapy. Brain 126, 1371-1381 (2003).
    • (2003) Brain , vol.126 , pp. 1371-1381
    • Nelissen, I.1
  • 75
    • 0000391746 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 triggers the angiogenic switch during carcinogenesis
    • Bergers, G. etal. Matrix metalloproteinase-9 triggers the angiogenic switch during carcinogenesis. Nature Cell Biol. 2, 737-744 (2000).
    • (2000) Nature Cell Biol. , vol.2 , pp. 737-744
    • Bergers, G.1
  • 76
    • 0031467314 scopus 로고    scopus 로고
    • Matrix metalloproteinase-3 releases active heparin-binding EGF-like growth factor by cleavage at a specific juxtamembrane site
    • Suzuki, M., Raab, G., Moses, M. A., Fernandez, C. A. & Klagsbrun, M. Matrix metalloproteinase-3 releases active heparin-binding EGF-like growth factor by cleavage at a specific juxtamembrane site. J. Biol. Chem. 272, 31730-31737 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 31730-31737
    • Suzuki, M.1    Raab, G.2    Moses, M.A.3    Fernandez, C.A.4    Klagsbrun, M.5
  • 77
    • 0029959437 scopus 로고    scopus 로고
    • Matrix metalloproteinase 2 releases active soluble ectodomain of fibroblast growth factor receptor 1
    • Levi, E. et al. Matrix metalloproteinase 2 releases active soluble ectodomain of fibroblast growth factor receptor 1. Proc. Natl Acad. Sci. USA 93, 7069-7074 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 7069-7074
    • Levi, E.1
  • 78
    • 0026799402 scopus 로고
    • Targeted disruption of the mouse transforming growth factor-β 1 gene results in multifocal inflammatory disease
    • Shull, M. M. et al. Targeted disruption of the mouse transforming growth factor-β 1 gene results in multifocal inflammatory disease. Nature 359, 693-699 (1992).
    • (1992) Nature , vol.359 , pp. 693-699
    • Shull, M.M.1
  • 79
    • 0027724228 scopus 로고
    • Transforming growth factor-β 1 knockout mice. A mutation in one cytokine gene causes a dramatic inflammatory disease
    • Kulkarni, A. B. & Karlsson, S. Transforming growth factor-β 1 knockout mice. A mutation in one cytokine gene causes a dramatic inflammatory disease. Am. J. Pathol. 143, 3-9 (1993).
    • (1993) Am. J. Pathol. , vol.143 , pp. 3-9
    • Kulkarni, A.B.1    Karlsson, S.2
  • 80
    • 0033524949 scopus 로고    scopus 로고
    • 6 binds and activates latent TGFβ1: A mechanism for regulating pulmonary inflammation and fibrosis
    • 6 binds and activates latent TGFβ1: a mechanism for regulating pulmonary inflammation and fibrosis. Cell 96, 319-328 (1999).
    • (1999) Cell , vol.96 , pp. 319-328
    • Munger, J.S.1
  • 81
    • 0036371374 scopus 로고    scopus 로고
    • The first stage of transforming growth factor β1 activation is release of the large latent complex from the extracellular matrix of growth plate chondrocytes by matrix vesicle stromelysin-1 (MMP-3)
    • Maeda, S., Dean, D. D., Gomez, R., Schwartz, Z. & Boyan, B. D. The first stage of transforming growth factor β1 activation is release of the large latent complex from the extracellular matrix of growth plate chondrocytes by matrix vesicle stromelysin-1 (MMP-3). Calcif Tissue Int. 70, 54-65 (2002).
    • (2002) Calcif Tissue Int. , vol.70 , pp. 54-65
    • Maeda, S.1    Dean, D.D.2    Gomez, R.3    Schwartz, Z.4    Boyan, B.D.5
  • 82
    • 0037114003 scopus 로고    scopus 로고
    • Matrix metalloproteinase-dependent activation of latent transforming growth factor-β controls the conversion of osteoblasts into osteocytes by blocking osteoblast apoptosis
    • Karsdal, M. A. et al. Matrix metalloproteinase-dependent activation of latent transforming growth factor-β controls the conversion of osteoblasts into osteocytes by blocking osteoblast apoptosis. J. Biol. Chem. 277, 44061-44067 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 44061-44067
    • Karsdal, M.A.1
  • 83
    • 0031568401 scopus 로고    scopus 로고
    • Response to local inflammation of IL-1β-converting enzyme-deficient mice
    • Fantuzzi, G. et al. Response to local inflammation of IL-1β-converting enzyme-deficient mice. J. Immunol. 158, 1818-1824 (1997).
    • (1997) J. Immunol. , vol.158 , pp. 1818-1824
    • Fantuzzi, G.1
  • 84
    • 0032194115 scopus 로고    scopus 로고
    • Generation of biologically active IL-1β by matrix metalloproteinases: A novel caspase-1-independent pathway of IL-1β processing
    • Schonbeck, U., Mach, F. & Libby, P. Generation of biologically active IL-1β by matrix metalloproteinases: a novel caspase-1-independent pathway of IL-1β processing. J. Immunol. 161, 3340-3346 (1998).
    • (1998) J. Immunol. , vol.161 , pp. 3340-3346
    • Schonbeck, U.1    Mach, F.2    Libby, P.3
  • 85
    • 0030596456 scopus 로고    scopus 로고
    • Degradation of interleukin 1β by matrix metalloproteinases
    • Ito, A. et al. Degradation of interleukin 1β by matrix metalloproteinases. J. Biol. Chem. 271, 14657-14660 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 14657-14660
    • Ito, A.1
  • 86
    • 0028485654 scopus 로고
    • Processing of tumour necrosis factor-α precursor by metalloproteinases
    • Gearing, A. J. H. et al. Processing of tumour necrosis factor-α precursor by metalloproteinases. Nature 370, 555-557 (1994).
    • (1994) Nature , vol.370 , pp. 555-557
    • Gearing, A.J.H.1
  • 87
    • 8044257704 scopus 로고    scopus 로고
    • A metalloproteinase disintegrin that releases tumour-necrosis factor-α from cells
    • Black, R. A. et al. A metalloproteinase disintegrin that releases tumour-necrosis factor-α from cells. Nature 385, 729-733 (1997).
    • (1997) Nature , vol.385 , pp. 729-733
    • Black, R.A.1
  • 88
    • 8044250278 scopus 로고    scopus 로고
    • Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-α
    • Moss, M. L. et al. Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-α. Nature 385, 733-736 (1997).
    • (1997) Nature , vol.385 , pp. 733-736
    • Moss, M.L.1
  • 89
    • 18444368391 scopus 로고    scopus 로고
    • The tumor necrosis factor-α converting enzyme (TACE): A unique metalloproteinase with highly defined substrate selectivity
    • Mohan, M. J. et al. The tumor necrosis factor-α converting enzyme (TACE): a unique metalloproteinase with highly defined substrate selectivity Biochemistry 41, 9462-9469 (2002).
    • (2002) Biochemistry , vol.41 , pp. 9462-9469
    • Mohan, M.J.1
  • 90
    • 0034640282 scopus 로고    scopus 로고
    • Membrane type 4 matrix metalloproteinase (MMP 17) has tumor necrosis factor-α convertase activity but does not activate pro-MMP2
    • English, W. R. et al. Membrane type 4 matrix metalloproteinase (MMP 17) has tumor necrosis factor-α convertase activity but does not activate pro-MMP2. J. Biol. Chem. 275, 14046-14055 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 14046-14055
    • English, W.R.1
  • 91
    • 0037693895 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tissue inhibitors of metalloproteinases: Structure, function, and biochemistry
    • Visse, R. & Nagase, H. Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry. Circ. Res. 92, 827-839 (2003).
    • (2003) Circ. Res. , vol.92 , pp. 827-839
    • Visse, R.1    Nagase, H.2
  • 92
    • 0037393850 scopus 로고    scopus 로고
    • A novel function for tissue inhibitor of metalloproteinases-3 (TIMP3): Inhibition of angiogenesis by blockage of VEGF binding to VEGF receptor-2
    • Qi, J. H. et al. A novel function for tissue inhibitor of metalloproteinases-3 (TIMP3): inhibition of angiogenesis by blockage of VEGF binding to VEGF receptor-2. Nature Med. 9, 407-415 (2003).
    • (2003) Nature Med. , vol.9 , pp. 407-415
    • Qi, J.H.1
  • 93
    • 0042197340 scopus 로고    scopus 로고
    • TIMP-2 mediated inhibition of angiogenesis: An MMP-independent mechanism
    • Seo, D. W. et al. TIMP-2 mediated inhibition of angiogenesis: an MMP-independent mechanism. Cell 114, 171-180 (2003).
    • (2003) Cell , vol.114 , pp. 171-180
    • Seo, D.W.1
  • 94
    • 18244367390 scopus 로고    scopus 로고
    • The membrane-anchored MMP inhibitor RECK is a key regulator of extracellular matrix integrity and angiogenesis
    • Oh, J. et al. The membrane-anchored MMP inhibitor RECK is a key regulator of extracellular matrix integrity and angiogenesis. Cell 107, 789-800 (2001).
    • (2001) Cell , vol.107 , pp. 789-800
    • Oh, J.1
  • 95
    • 0037192458 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors and cancer: Trials and tribulations
    • Coussens, L. M., Fingleton, B. & Matrisian, L. M. Matrix metalloproteinase inhibitors and cancer: trials and tribulations. Science 295, 2387-2392 (2002).
    • (2002) Science , vol.295 , pp. 2387-2392
    • Coussens, L.M.1    Fingleton, B.2    Matrisian, L.M.3
  • 96
    • 0036716282 scopus 로고    scopus 로고
    • Strategies for MMP inhibition in cancer; innovations for the post-trial era
    • Overall, C. M. & Lopez-Otin, C. Strategies for MMP inhibition in cancer; innovations for the post-trial era. Nature Rev. Cancer 2, 657-672 (2002).
    • (2002) Nature Rev. Cancer , vol.2 , pp. 657-672
    • Overall, C.M.1    Lopez-Otin, C.2
  • 97
    • 0033955104 scopus 로고    scopus 로고
    • Post-translational proteolytic processing of procollagen C-terminal proteinase enhancer releases a metalloproteinese inhibiton
    • Mott, J. D. et al. Post-translational proteolytic processing of procollagen C-terminal proteinase enhancer releases a metalloproteinese inhibiton J. Biol. Chem. 275, 1384-1390 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 1384-1390
    • Mott, J.D.1
  • 98
    • 0031836105 scopus 로고    scopus 로고
    • Mice lacking neutrophil elastase reveal impaired host defense against gram negative bacterial sepsis
    • Belaaouaj, A. et al. Mice lacking neutrophil elastase reveal impaired host defense against gram negative bacterial sepsis. Nature Med. 4, 615-618 (1998).
    • (1998) Nature Med. , vol.4 , pp. 615-618
    • Belaaouaj, A.1
  • 99
    • 0034257889 scopus 로고    scopus 로고
    • The serpin α1-proteinase inhibitor is a critical substrate for gelatinase B/MMP-9 in vivo
    • Liu, Z. et al. The serpin α1-proteinase inhibitor is a critical substrate for gelatinase B/MMP-9 in vivo. Cell 102, 647-655 (2000). Using an experimental model of blister formation, this paper shows that MMP9 contributes to inflammation-mediated tissue damage by cleaving and inactivating the serpin α1-antiproteinase (a potent inhibitor of neutrophil elastase).
    • (2000) Cell , vol.102 , pp. 647-655
    • Liu, Z.1
  • 100
    • 0031426654 scopus 로고    scopus 로고
    • Matrix metalloproteinase stromelysin-1 triggers a cascade of molecular alterations that leads to stable epithelial-to-mesenchymal conversion and a premalignant phenotype in mammary epithelial cells
    • Lochter, A. et al. Matrix metalloproteinase stromelysin-1 triggers a cascade of molecular alterations that leads to stable epithelial-to-mesenchymal conversion and a premalignant phenotype in mammary epithelial cells. J. Cell Biol. 139, 1861-1872 (1997).
    • (1997) J. Cell Biol. , vol.139 , pp. 1861-1872
    • Lochter, A.1
  • 101
    • 0028302990 scopus 로고
    • Targeted expression of stromelysin-1 in mammary gland provides evidence for a role of proteinases in branching morphogenesis and the requirement for an intact basement membrane for tissue-specific gene expression
    • Sympson, C. J. et al. Targeted expression of stromelysin-1 in mammary gland provides evidence for a role of proteinases in branching morphogenesis and the requirement for an intact basement membrane for tissue-specific gene expression. J. Cell Biol. 125, 681-693 (1994).
    • (1994) J. Cell Biol. , vol.125 , pp. 681-693
    • Sympson, C.J.1
  • 102
    • 0033966350 scopus 로고    scopus 로고
    • Matrix metalloproteinase-7-dependent release of tumor necrosis factor-α in a model of herniated disc resorption
    • Haro, H. et al. Matrix metalloproteinase-7-dependent release of tumor necrosis factor-α in a model of herniated disc resorption. J. Clin. Invest. 105, 143-150 (2000).
    • (2000) J. Clin. Invest. , vol.105 , pp. 143-150
    • Haro, H.1
  • 103
    • 0035478029 scopus 로고    scopus 로고
    • Effects of matrix metalloproteinase-9 gene knock-out on the proteolysis of blood-brain barrier and white matter components after cerebral ischemia
    • Asahi, M. et al. Effects of matrix metalloproteinase-9 gene knock-out on the proteolysis of blood-brain barrier and white matter components after cerebral ischemia. J. Neurosci. 21, 7724-7732 (2001).
    • (2001) J. Neurosci. , vol.21 , pp. 7724-7732
    • Asahi, M.1
  • 104
    • 0035794294 scopus 로고    scopus 로고
    • Matrix metalloproteinase 9 protects mice from anti-glomerular basement membrane nephritis through its fibrinolytic activity
    • Lelongt, B. et al. Matrix metalloproteinase 9 protects mice from anti-glomerular basement membrane nephritis through its fibrinolytic activity. J. Exp. Med. 193, 793-802 (2001).
    • (2001) J. Exp. Med. , vol.193 , pp. 793-802
    • Lelongt, B.1
  • 105
    • 0346749451 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 facilitates remyelination in part by processing the inhibitory NG2 proteoglycan
    • Larsen, P. H., Wells, J. E., Stallcup, W. B., Opdenakker, G. & Yong, V. W. Matrix metalloproteinase-9 facilitates remyelination in part by processing the inhibitory NG2 proteoglycan. J. Neurosci. 23, 11127-11135 (2003).
    • (2003) J. Neurosci. , vol.23 , pp. 11127-11135
    • Larsen, P.H.1    Wells, J.E.2    Stallcup, W.B.3    Opdenakker, G.4    Yong, V.W.5
  • 106
    • 0037447184 scopus 로고    scopus 로고
    • Macrophage metalloelastase mediates acute cigarette smoke-induced inflammation via tumor necrosis factor-α release
    • Churg, A. et al. Macrophage metalloelastase mediates acute cigarette smoke-induced inflammation via tumor necrosis factor-α release. Am. J. Respir. Crit. Care Med. 187, 1083-1089 (2003).
    • (2003) Am. J. Respir. Crit. Care Med. , vol.187 , pp. 1083-1089
    • Churg, A.1
  • 107
    • 0037017385 scopus 로고    scopus 로고
    • Matrix metalloproteinases (MMPs) regulate fibrin-invasive activity via MT1-MMP-dependent and -independent processes
    • Hotary, K. B. et al. Matrix metalloproteinases (MMPs) regulate fibrin-invasive activity via MT1-MMP-dependent and -independent processes. J. Exp. Med. 195, 295-308 (2002).
    • (2002) J. Exp. Med. , vol.195 , pp. 295-308
    • Hotary, K.B.1
  • 108
    • 0142103466 scopus 로고    scopus 로고
    • Cleavage of syndecan-1 by membrane type matrix metalloproteinase-1 stimulates cell migration
    • Endo, K. et al. Cleavage of syndecan-1 by membrane type matrix metalloproteinase-1 stimulates cell migration. J. Biol. Chem. 278, 40764-40770 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 40764-40770
    • Endo, K.1
  • 109
    • 1442290120 scopus 로고    scopus 로고
    • Proteolytic processing of laminin-5 by MT1-MMP in tissues and its effects on epithelial cell morphology
    • Koshikawa, N. et al. Proteolytic processing of laminin-5 by MT1-MMP in tissues and its effects on epithelial cell morphology. FASEB J. 18, 364-366 (2004).
    • (2004) FASEB J. , vol.18 , pp. 364-366
    • Koshikawa, N.1
  • 110
    • 0346668319 scopus 로고    scopus 로고
    • Enamelysin (matrix metalloproteinase 20)-deficient mice display an amelogenesis imperfecta phenotype
    • Catarina, J. J. et al. Enamelysin (matrix metalloproteinase 20)-deficient mice display an amelogenesis imperfecta phenotype. J. Biol. Chem. 277, 49598-49604 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 49598-49604
    • Catarina, J.J.1
  • 111
    • 0030891983 scopus 로고    scopus 로고
    • Enhanced cleavage of type II collagen by collagenases in osteoarthritic articular cartilage
    • Billinghurst, R. C. et al. Enhanced cleavage of type II collagen by collagenases in osteoarthritic articular cartilage. J. Clin. Invest. 99, 1534-1545 (1997).
    • (1997) J. Clin. Invest. , vol.99 , pp. 1534-1545
    • Billinghurst, R.C.1
  • 112
    • 0032764330 scopus 로고    scopus 로고
    • Detection of collagenase-induced damage of collagen by 9A4, a monoclonal C-terminal neoepitope antibody
    • Otterness, I. G. et al. Detection of collagenase-induced damage of collagen by 9A4, a monoclonal C-terminal neoepitope antibody. Matrix Biol. 18, 331-341 (1999).
    • (1999) Matrix Biol. , vol.18 , pp. 331-341
    • Otterness, I.G.1
  • 113
    • 0036674028 scopus 로고    scopus 로고
    • Sites of collagenase cleavage and denaturation of type II collagen in aging and osteoarthritic articular cartilage and their relationship to the distribution of matrix metalloproteinase 1 and matrix metalloproteinase 13
    • Wu, W. et al. Sites of collagenase cleavage and denaturation of type II collagen in aging and osteoarthritic articular cartilage and their relationship to the distribution of matrix metalloproteinase 1 and matrix metalloproteinase 13. Arthritis Rheum. 46, 2087-2094 (2002).
    • (2002) Arthritis Rheum. , vol.46 , pp. 2087-2094
    • Wu, W.1
  • 114
    • 0038784546 scopus 로고    scopus 로고
    • Membrane type I matrix metalloproteinase usurps tumor growth control imposed by the three-dimensional extracellular matrix
    • Hotary, K. B. et al. Membrane type I matrix metalloproteinase usurps tumor growth control imposed by the three-dimensional extracellular matrix. Cell 114, 33-45 (2003).
    • (2003) Cell , vol.114 , pp. 33-45
    • Hotary, K.B.1
  • 115
    • 85047691853 scopus 로고    scopus 로고
    • Identification and enzymatic characterization of two diverging murine counterparts of human interstitial collagenase (MMP-1) expressed at sites of embryo implantation
    • Balbin, M. et al. Identification and enzymatic characterization of two diverging murine counterparts of human interstitial collagenase (MMP-1) expressed at sites of embryo implantation. J. Biol. Chem. 276, 10253-10262 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 10253-10262
    • Balbin, M.1
  • 117
    • 0029825963 scopus 로고    scopus 로고
    • Identification and characterization of a novel collagenase in Xenopus laevis: Possible roles during frog development
    • Stolow, M. A. et al. Identification and characterization of a novel collagenase in Xenopus laevis: possible roles during frog development. Mol. Biol. Cell 7, 1471-1483 (1996).
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1471-1483
    • Stolow, M.A.1
  • 118
    • 10744220468 scopus 로고    scopus 로고
    • The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: A bioinformatics assessment
    • Clark, H. F. et al. The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 13, 2265-2270 (2003).
    • (2003) Genome Res. , vol.13 , pp. 2265-2270
    • Clark, H.F.1
  • 119
    • 0032031861 scopus 로고    scopus 로고
    • Reduced angiogenesis and tumor progression in gelatinase A-deficient mice
    • Itoh, T. et al. Reduced angiogenesis and tumor progression in gelatinase A-deficient mice. Cancer Res. 58. 1048-1051 (1998).
    • (1998) Cancer Res. , vol.58 , pp. 1048-1051
    • Itoh, T.1
  • 120
    • 0035900495 scopus 로고    scopus 로고
    • Diminished corneal angiogenesis in gelatinase A-deficient mice
    • Kato, T. et al. Diminished corneal angiogenesis in gelatinase A-deficient mice. FEBS Lett. 508, 187-190 (2001).
    • (2001) FEBS Lett. , vol.508 , pp. 187-190
    • Kato, T.1
  • 121
    • 0344420010 scopus 로고    scopus 로고
    • Reduced retinal angiogenesis in MMP-2-deficient mice
    • Ohno-Matsui, K. et al. Reduced retinal angiogenesis in MMP-2-deficient mice. Invest. Ophthalmol Vis. Sci. 44, 5370-5375 (2003).
    • (2003) Invest. Ophthalmol Vis. Sci. , vol.44 , pp. 5370-5375
    • Ohno-Matsui, K.1
  • 122
    • 0037253085 scopus 로고    scopus 로고
    • Reduced choroidal neovascular membrane formation in matrix metalloproteinase-2-deficient mice
    • Berglin, L. et al. Reduced choroidal neovascular membrane formation in matrix metalloproteinase-2-deficient mice. Invest. Ophthalmol. Vis. Sci. 44, 403-408 (2003).
    • (2003) Invest. Ophthalmol. Vis. Sci. , vol.44 , pp. 403-408
    • Berglin, L.1
  • 123
    • 0033536007 scopus 로고    scopus 로고
    • Matrix metalloproteinase deficiencies affect contact hypersensitivity: Stromelysin-1 deficiency prevents the response and gelatinase B deficiency prolongs the response
    • Wang, M. et al. Matrix metalloproteinase deficiencies affect contact hypersensitivity: stromelysin-1 deficiency prevents the response and gelatinase B deficiency prolongs the response. Proc. Natl Acad. Sci. USA 96, 6885-6889 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 6885-6889
    • Wang, M.1
  • 124
    • 0035033287 scopus 로고    scopus 로고
    • Role of stromelysin 1 and gelatinase B in experimental acute lung injury
    • Warner, R. L. et al. Role of stromelysin 1 and gelatinase B in experimental acute lung injury. Am. J. Respir. Cell Mol. Biol. 24, 537-544 (2001).
    • (2001) Am. J. Respir. Cell Mol. Biol. , vol.24 , pp. 537-544
    • Warner, R.L.1
  • 125
    • 0035572899 scopus 로고    scopus 로고
    • Persistence of atherosclerotic plaque but reduced aneurysm formation in mice with stromelysin-1 (MMP-3) gene inactivation
    • Silence, J., Lupu, F., Collen, D. & Lijnen, H. R. Persistence of atherosclerotic plaque but reduced aneurysm formation in mice with stromelysin-1 (MMP-3) gene inactivation. Arterioscler. Thromb. Vasc. Biol. 21, 1440-1445 (2001).
    • (2001) Arterioscler. Thromb. Vasc. Biol. , vol.21 , pp. 1440-1445
    • Silence, J.1    Lupu, F.2    Collen, D.3    Lijnen, H.R.4
  • 126
    • 0037251043 scopus 로고    scopus 로고
    • Corneal neovascularization after excimer keratectomy wounds in matrilysin-deficient mice
    • Kure, T. et al. Corneal neovascularization after excimer keratectomy wounds in matrilysin-deficient mice. Invest. Ophthalmol. Vis. Sci. 44, 137-144 (2003).
    • (2003) Invest. Ophthalmol. Vis. Sci. , vol.44 , pp. 137-144
    • Kure, T.1
  • 127
    • 0033405694 scopus 로고    scopus 로고
    • Resistance of young gelatinase B-deficient mice to experimental autoimmune encephalomyelitis and necrotising tail lesions
    • Dubois, B. et al. Resistance of young gelatinase B-deficient mice to experimental autoimmune encephalomyelitis and necrotising tail lesions. J. Clin. Invest. 104, 1507-1515 (1999).
    • (1999) J. Clin. Invest. , vol.104 , pp. 1507-1515
    • Dubois, B.1
  • 128
    • 0036686258 scopus 로고    scopus 로고
    • Gelatinase B deficiency protects against endotoxin shock
    • Dubois, B. et al. Gelatinase B deficiency protects against endotoxin shock. Eur. J. Immunol. 32, 2163-2171 (2002).
    • (2002) Eur. J. Immunol. , vol.32 , pp. 2163-2171
    • Dubois, B.1
  • 129
    • 0036568954 scopus 로고    scopus 로고
    • Matrix metalloproteinases 9 and 2 are necessary for the migration of Langerhans cells and dermal dendritic cells from human and murine skin
    • Ratzinger, G. et al. Matrix metalloproteinases 9 and 2 are necessary for the migration of Langerhans cells and dermal dendritic cells from human and murine skin. J. Immunol. 168, 4361-4371 (2002).
    • (2002) J. Immunol. , vol.168 , pp. 4361-4371
    • Ratzinger, G.1
  • 130
    • 0032479967 scopus 로고    scopus 로고
    • Gelatinase B-deficient mice are resistant to experimental bullous pemphigoid
    • Liu, Z. et al. Gelatinase B-deficient mice are resistant to experimental bullous pemphigoid. J. Exp. Med. 188, 475-482 (1998).
    • (1998) J. Exp. Med. , vol.188 , pp. 475-482
    • Liu, Z.1
  • 131
    • 0346963598 scopus 로고    scopus 로고
    • MMP-9/gelatinase B is a key regulator of growth plate angiogenesis and apoptosis of hypertrophic chondrocytes
    • Vu, T. H. et al. MMP-9/gelatinase B is a key regulator of growth plate angiogenesis and apoptosis of hypertrophic chondrocytes. Cell 93, 411-422 (1998).
    • (1998) Cell , vol.93 , pp. 411-422
    • Vu, T.H.1
  • 132
    • 0034721666 scopus 로고    scopus 로고
    • MMP-9 supplied by bone marrow-derived cells contributes to skin carcinogenesis
    • Coussens, L. M., Tinkle, C. L., Hanahan, D. & Werb, Z. MMP-9 supplied by bone marrow-derived cells contributes to skin carcinogenesis. Cell 103, 481-490 (2000).
    • (2000) Cell , vol.103 , pp. 481-490
    • Coussens, L.M.1    Tinkle, C.L.2    Hanahan, D.3    Werb, Z.4
  • 133
    • 1042268055 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 is required for adequate angiogenic revascularization of ischemic tissues: Potential role in capillary branching
    • Johnson, C., Sung, H. J., Lessner, S. M., Fini, M. E. & Galis, Z. S. Matrix metalloproteinase-9 is required for adequate angiogenic revascularization of ischemic tissues: potential role in capillary branching. Circ. Res. 94, 262-268 (2004).
    • (2004) Circ. Res. , vol.94 , pp. 262-268
    • Johnson, C.1    Sung, H.J.2    Lessner, S.M.3    Fini, M.E.4    Galis, Z.S.5
  • 134
    • 0842300350 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 deficiency results in enhanced allergen-induced airway inflammation
    • McMillan, S. J. et al. Matrix metalloproteinase-9 deficiency results in enhanced allergen-induced airway inflammation. J. Immunol. 172, 2586-2594 (2004).
    • (2004) J. Immunol. , vol.172 , pp. 2586-2594
    • McMillan, S.J.1
  • 135
    • 0036968724 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 deficiency impairs cellular infiltration and bronchial hyperresponsiveness during allergen-induced airway inflammation
    • Cataldo, D. D. et al. Matrix metalloproteinase-9 deficiency impairs cellular infiltration and bronchial hyperresponsiveness during allergen-induced airway inflammation, Am. J. Pathol. 161, 491-498 (2002).
    • (2002) Am. J. Pathol. , vol.161 , pp. 491-498
    • Cataldo, D.D.1
  • 136
    • 0036679426 scopus 로고    scopus 로고
    • Overlapping and enzyme-specific contributions of matrix metalloproteinases-9 and-12 in IL-13-induced inflammation and remodeling
    • Lanone, S. et al. Overlapping and enzyme-specific contributions of matrix metalloproteinases-9 and-12 in IL-13-induced inflammation and remodeling. J. Clin. Invest. 110, 463-474 (2002).
    • (2002) J. Clin. Invest. , vol.110 , pp. 463-474
    • Lanone, S.1
  • 137
    • 1642362387 scopus 로고    scopus 로고
    • Loss of matrix metalloproteinase-9 or matrix metalloproteinase-12 protects apolipoprotein E-deficient mice against atherosclerotic media destruction but differentially affects plaque growth
    • Luttun, A. et al. Loss of matrix metalloproteinase-9 or matrix metalloproteinase-12 protects apolipoprotein E-deficient mice against atherosclerotic media destruction but differentially affects plaque growth. Circulation 109, 1408-1414 (2004).
    • (2004) Circulation , vol.109 , pp. 1408-1414
    • Luttun, A.1
  • 138
    • 0036733629 scopus 로고    scopus 로고
    • Matrix metalloproteinase 2 and 9 work in concert to produce aortic aneurysms
    • Longo, G. M. et al. Matrix metalloproteinase 2 and 9 work in concert to produce aortic aneurysms, J. Clin. Invest. 110, 625-632 (2002).
    • (2002) J. Clin. Invest. , vol.110 , pp. 625-632
    • Longo, G.M.1
  • 139
    • 0034090148 scopus 로고    scopus 로고
    • Targeted gene disruption of matrix metalloproteinase-9 (gelatinase B) suppresses development of experimental abdominal aortic aneurysms
    • Pyo, R. et al. Targeted gene disruption of matrix metalloproteinase-9 (gelatinase B) suppresses development of experimental abdominal aortic aneurysms. J. Clin. Invest. 105, 1641-1649 (2000).
    • (2000) J. Clin. Invest. , vol.105 , pp. 1641-1649
    • Pyo, R.1
  • 140
    • 0033638508 scopus 로고    scopus 로고
    • Role for matrix metalloproteinase 9 after focal cerebral ischemia: Effects of gene knockout and enzyme inhibition with BB-94
    • Asahi, M. at al. Role for matrix metalloproteinase 9 after focal cerebral ischemia: effects of gene knockout and enzyme inhibition with BB-94. J. Cereb. Blood Flow Metab. 20, 1681-1689 (2000).
    • (2000) J. Cereb. Blood Flow Metab. , vol.20 , pp. 1681-1689
    • Asahi, M.1
  • 141
    • 0642364446 scopus 로고    scopus 로고
    • MMP-2 and MMP-9 synergize in promoting choroidal neovascularization
    • Lambert, V. et al. MMP-2 and MMP-9 synergize in promoting choroidal neovascularization. FASEB J. 17, 2290-2292 (2003).
    • (2003) FASEB J. , vol.17 , pp. 2290-2292
    • Lambert, V.1
  • 143
    • 0242442568 scopus 로고    scopus 로고
    • An adverse role for matrix metalloproteinase 12 after spinal cord injury in mice
    • Wells, J. E. et al. An adverse role for matrix metalloproteinase 12 after spinal cord injury in mice. J. Neurosci. 23, 10107-10115 (2003).
    • (2003) J. Neurosci. , vol.23 , pp. 10107-10115
    • Wells, J.E.1
  • 144
    • 0034977464 scopus 로고    scopus 로고
    • The role of metalloelastase in immune complex-induced acute lung injury
    • Warner, R. L. et al. The role of metalloelastase in immune complex-induced acute lung injury. Am. J. Pathol. 158, 2139-2144 (2001).
    • (2001) Am. J. Pathol. , vol.158 , pp. 2139-2144
    • Warner, R.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.