메뉴 건너뛰기




Volumn 4, Issue 5, 2004, Pages 295-319

Matrix metalloproteinases and the immune response

Author keywords

Host Response; Immune Cells; Inflammation; Martix metalloproteinases

Indexed keywords

COLONY STIMULATING FACTOR; GELATINASE A; GELATINASE B; INTERCELLULAR ADHESION MOLECULE 1; INTERSTITIAL COLLAGENASE; MACROPHAGE ELASTASE; MATRILYSIN; MATRIX METALLOPROTEINASE; STROMELYSIN; TUMOR NECROSIS FACTOR; VASCULAR CELL ADHESION MOLECULE 1;

EID: 3242776237     PISSN: 15291049     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cair.2004.02.001     Document Type: Review
Times cited : (38)

References (224)
  • 2
    • 0029822375 scopus 로고    scopus 로고
    • Degradation of cross-linked fibrin by matrix metalloproteinase 3 (stromelysin 1): Hydrolysis of the gamma Gly 404-Ala 405 peptide bond
    • Bini A. Itoh Y. Kudryk B.J. Nagase H. Degradation of cross-linked fibrin by matrix metalloproteinase 3 (stromelysin 1): hydrolysis of the gamma Gly 404-Ala 405 peptide bond Biochemistry 35 1996 13056-13063
    • (1996) Biochemistry , vol.35 , pp. 13056-13063
    • Bini, A.1    Itoh, Y.2    Kudryk, B.J.3    Nagase, H.4
  • 3
    • 15444352707 scopus 로고    scopus 로고
    • Angiostatin-converting enzyme activities of human matrilysin (MMP-7) and gelatinase B/Type IV collagenase (MMP-9)
    • Patterson B.C. Sang Q.A. Angiostatin-converting enzyme activities of human matrilysin (MMP-7) and gelatinase B/Type IV collagenase (MMP-9) J Biol Chem 272 1997 28823-28825
    • (1997) J. Biol. Chem. , vol.272 , pp. 28823-28825
    • Patterson, B.C.1    Sang, Q.A.2
  • 6
    • 0033994361 scopus 로고    scopus 로고
    • Extrinsic regulators of epithelial tumour progression: Metalloproteinases
    • Bergers G. Coussens L.M. Extrinsic regulators of epithelial tumour progression: metalloproteinases Curr Opin Genet Dev 10 2000 120-127
    • (2000) Curr. Opin. Genet. Dev. , vol.10 , pp. 120-127
    • Bergers, G.1    Coussens, L.M.2
  • 7
    • 0034693163 scopus 로고    scopus 로고
    • Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type-1 matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII
    • Hiller O. Lichte A. Oberpichler A. Kocourek A. Tschesche H. Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type-1 matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII J Biol Chem 275 2000 33008-33013
    • (2000) J. Biol. Chem. , vol.275 , pp. 33008-33013
    • Hiller, O.1    Lichte, A.2    Oberpichler, A.3    Kocourek, A.4    Tschesche, H.5
  • 10
    • 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 2001 534-540
    • (2001) Curr. Opin.Cell. Biol. , vol.13 , pp. 534-540
    • McCawley, L.J.1    Matrisian, L.M.2
  • 12
    • 0034749944 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Multifunctional effectors of inflammation in multiple sclerosis and bacterial meningitis
    • Leppert D. Lindberg R.L. Kappos L. Leib S.L. Matrix metalloproteinases: multifunctional effectors of inflammation in multiple sclerosis and bacterial meningitis Brain Res Brain Res Rev 36 2001 249-257
    • (2001) Brain Res. Brain Res. Rev. , vol.36 , pp. 249-257
    • Leppert, D.1    Lindberg, R.L.2    Kappos, L.3    Leib, S.L.4
  • 13
    • 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 2002 2387-2392
    • (2002) Science , vol.295 , pp. 2387-2392
    • Coussens, L.M.1    Fingleton, B.2    Matrisian, L.M.3
  • 14
    • 0036728623 scopus 로고    scopus 로고
    • MMPs and TIMPs-an historical perspective
    • Woessner Jr. J.F. MMPs and TIMPs-an historical perspective Mol Biotechnol 22 2002 33-49
    • (2002) Mol. Biotechnol. , vol.22 , pp. 33-49
    • Woessner Jr., J.F.1
  • 15
    • 0033931053 scopus 로고    scopus 로고
    • Structural studies of matrix metalloproteinases
    • Borkakoti N. Structural studies of matrix metalloproteinases J Mol Med 78 2000 261-268
    • (2000) J. Mol. Med. , vol.78 , pp. 261-268
    • Borkakoti, N.1
  • 17
    • 0345643514 scopus 로고    scopus 로고
    • Regulation of matrix metalloproteinase expression in tumor invasion
    • Westermarck J. Kähäri V. Regulation of matrix metalloproteinase expression in tumor invasion FASEB J 13 1999 781-792
    • (1999) FASEB J. , vol.13 , pp. 781-792
    • Westermarck, J.1    Kähäri, V.2
  • 18
  • 19
    • 0034751435 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors: Current developments and future perspectives
    • Hoekstra R. Eskens F.A. Verweij E. Matrix metalloproteinase inhibitors: current developments and future perspectives Oncologist 6 2001 415-427
    • (2001) Oncologist , vol.6 , pp. 415-427
    • Hoekstra, R.1    Eskens, F.A.2    Verweij, E.3
  • 21
    • 0027768570 scopus 로고
    • Cytokine regulation of metalloproteinase gene expression
    • Mauviel A. Cytokine regulation of metalloproteinase gene expression J Cell Biochem 53 1993 288-295
    • (1993) J. Cell. Biochem. , vol.53 , pp. 288-295
    • Mauviel, A.1
  • 22
    • 0029853789 scopus 로고    scopus 로고
    • Regulation of the expression of stromelysin-2 by growth factors in keritanocytes: Implications for normal and impaired wound healing
    • Madlener M. Mauch C. Conca W. Brauchle M. Parks W.C. Werner S. Regulation of the expression of stromelysin-2 by growth factors in keritanocytes: implications for normal and impaired wound healing Biochem J 320 1996 659-664
    • (1996) Biochem. J. , vol.320 , pp. 659-664
    • Madlener, M.1    Mauch, C.2    Conca, W.3    Brauchle, M.4    Parks, W.C.5    Werner, S.6
  • 23
    • 0003089209 scopus 로고    scopus 로고
    • Regulation of MMP gene expression
    • W. C. Parks, & R. P. Mecham (Eds.), San Diego, CA: Academic Press
    • Fini M.E. Cook J.R. Mohan R. Regulation of MMP gene expression Parks W.C. Mecham R.P. Matrix metalloproteinases 1998 299-356 Academic Press San Diego, CA
    • (1998) Matrix Metalloproteinases , pp. 299-356
    • Fini, M.E.1    Cook, J.R.2    Mohan, R.3
  • 24
    • 0023522614 scopus 로고
    • Transcription from the stromelysin promotor is induced by interleukin-1 and repressed by dexamethasone
    • Frisch S.M. Ruley H.E. Transcription from the stromelysin promotor is induced by interleukin-1 and repressed by dexamethasone J Biol Chem 262 1987 16300-16304
    • (1987) J. Biol. Chem. , vol.262 , pp. 16300-16304
    • Frisch, S.M.1    Ruley, H.E.2
  • 25
    • 0025344028 scopus 로고
    • TGF-beta 1 inhibition of transin/stromelysin gene expression is mediated through a Fos binding sequence
    • Kerr L.D. Miller D.B. Martrisian L.M. TGF-beta 1 inhibition of transin/stromelysin gene expression is mediated through a Fos binding sequence Cell 61 1990 267-278
    • (1990) Cell. , vol.61 , pp. 267-278
    • Kerr, L.D.1    Miller, D.B.2    Martrisian, L.M.3
  • 26
    • 0024999675 scopus 로고
    • Interleukin-1 stimulates and all-trans-retinoic acid inhibits collagenase gene expression through its 5′ activator protein-1-binding site
    • Lafyatis R. Kim S.J. Angel P. Roberts A.B. Sporn M.B. Karin M. et al. Interleukin-1 stimulates and all-trans-retinoic acid inhibits collagenase gene expression through its 5′ activator protein-1-binding site Mol Endocrinol 4 1990 973-980
    • (1990) Mol. Endocrinol. , vol.4 , pp. 973-980
    • Lafyatis, R.1    Kim, S.J.2    Angel, P.3    Roberts, A.B.4    Sporn, M.B.5    Karin, M.6
  • 27
    • 0025602652 scopus 로고
    • Negative regulation of the rat stromelysin gene promotor by retinoic acid is mediated by an AP1 binding site
    • Nicholson R.C. Mader S. Nagpal S. Leid M. Rochette-Egly C. Chambon P. Negative regulation of the rat stromelysin gene promotor by retinoic acid is mediated by an AP1 binding site EMBO J 9 1990 4443-4454
    • (1990) EMBO J. , vol.9 , pp. 4443-4454
    • Nicholson, R.C.1    Mader, S.2    Nagpal, S.3    Leid, M.4    Rochette-Egly, C.5    Chambon, P.6
  • 28
    • 0026714363 scopus 로고
    • Post-transcriptional regulation of collagenase and stromelysin gene expression by epidermal growth factor and dexamethasone in cultured human fibroblasts
    • Delany A.M. Brinckerhoff C.E. Post-transcriptional regulation of collagenase and stromelysin gene expression by epidermal growth factor and dexamethasone in cultured human fibroblasts J Cell Biochem 50 1992 400-410
    • (1992) J. Cell. Biochem. , vol.50 , pp. 400-410
    • Delany, A.M.1    Brinckerhoff, C.E.2
  • 29
    • 0025096722 scopus 로고
    • Multiple modes of activation of latent human fibroblast collagenase: Evidence for the role of a Cys73 active-site zinc complex in latency and a "cysteine switch" mechanism for activation
    • Springman E.B. Angleton E.L. Birkedal-Hansen H. Van Wart H.E. Multiple modes of activation of latent human fibroblast collagenase: evidence for the role of a Cys73 active-site zinc complex in latency and a "cysteine switch" mechanism for activation Proc Natl Acad Sci USA 87 1990 364-368
    • (1990) Proc. Natl. Acad Sci. USA , vol.87 , pp. 364-368
    • Springman, E.B.1    Angleton, E.L.2    Birkedal-Hansen, H.3    Van Wart, H.E.4
  • 30
  • 31
    • 0024241283 scopus 로고
    • Selective up-regulation of human alveolar macrophage collagenase production by lipopolysaccharide and comparison to collagenase production by fibroblasts
    • Cury J.D. Campbell E.J. Lazarus C.J. Albin R.J. Welgus H.G. Selective up-regulation of human alveolar macrophage collagenase production by lipopolysaccharide and comparison to collagenase production by fibroblasts J Immunol 141 1988 4306-4312
    • (1988) J. Immunol. , vol.141 , pp. 4306-4312
    • Cury, J.D.1    Campbell, E.J.2    Lazarus, C.J.3    Albin, R.J.4    Welgus, H.G.5
  • 32
    • 0025059594 scopus 로고
    • Neutral metalloproteinases produced by human alveolar mononuclear phagocytes. Enzyme profile, regulation, and expression during cellular development
    • Welgus H.G. Campbell E.J. Cury J.D. Eisen A.Z. Senior R.M. Wilhelm S.M. et al. Neutral metalloproteinases produced by human alveolar mononuclear phagocytes. Enzyme profile, regulation, and expression during cellular development J Clin Invest 86 1990 1496-1502
    • (1990) J. Clin. Invest. , vol.86 , pp. 1496-1502
    • Welgus, H.G.1    Campbell, E.J.2    Cury, J.D.3    Eisen, A.Z.4    Senior, R.M.5    Wilhelm, S.M.6
  • 33
    • 0026033779 scopus 로고
    • Neutral proteinases of human mononuclear phagocytes. Cellular differentiation markedly alters cell phenotype for serine proteinases, metalloproteinases, and tissue inhibitor of metalloproteinases
    • Campbell E.J. Cury J.D. Shapiro S.D. Goldberg G.I. Welgus H.G. Neutral proteinases of human mononuclear phagocytes. Cellular differentiation markedly alters cell phenotype for serine proteinases, metalloproteinases, and tissue inhibitor of metalloproteinases J Immunol 146 1991 1286-1293
    • (1991) J. Immunol. , vol.146 , pp. 1286-1293
    • Campbell, E.J.1    Cury, J.D.2    Shapiro, S.D.3    Goldberg, G.I.4    Welgus, H.G.5
  • 34
    • 0026785711 scopus 로고
    • The matrix metalloproteinase matrilysin (PUMP) is expressed in developing human mononuclear phagocytes
    • Busiek D.F. Ross F.P. McDonnell S. Murphy G. Matrisian L.M. Welgus H.G. The matrix metalloproteinase matrilysin (PUMP) is expressed in developing human mononuclear phagocytes J Biol Chem 267 1992 9087-9092
    • (1992) J. Biol. Chem. , vol.267 , pp. 9087-9092
    • Busiek, D.F.1    Ross, F.P.2    McDonnell, S.3    Murphy, G.4    Matrisian, L.M.5    Welgus, H.G.6
  • 35
    • 0027515289 scopus 로고
    • Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages
    • Shapiro S.D. Kobayashi D.K. Ley T.J. Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages J Biol Chem 268 1993 23824-23829
    • (1993) J. Biol. Chem. , vol.268 , pp. 23824-23829
    • Shapiro, S.D.1    Kobayashi, D.K.2    Ley, T.J.3
  • 36
    • 0027971976 scopus 로고
    • Elastolytic metalloproteinases produced by human mononuclear phagocytes. Potential roles in destructive lung disease
    • Shapiro S.D. Elastolytic metalloproteinases produced by human mononuclear phagocytes. Potential roles in destructive lung disease Am J Respir Crit Care Med 150 1994 S160-S164
    • (1994) Am. J. Respir. Crit. Care Med. , vol.150
    • Shapiro, S.D.1
  • 37
    • 0028267620 scopus 로고
    • Regulatory mechanisms for the expression of type IV collagenases/gelatinases in murine macrophages
    • Xie B. Dong Z. Fidler I.J. Regulatory mechanisms for the expression of type IV collagenases/gelatinases in murine macrophages J Immunol 152 1994 3637-3644
    • (1994) J. Immunol. , vol.152 , pp. 3637-3644
    • Xie, B.1    Dong, Z.2    Fidler, I.J.3
  • 38
    • 0029005284 scopus 로고
    • Human macrophage metalloelastase. Genomic organization, chromosomal location, gene linkage, and tissue-specific expression
    • Belaaouaj A. Shipley J.M. Kobayashi D.K. Zimonjic D.B. Popescu N. Silverman G.A. et al. Human macrophage metalloelastase. Genomic organization, chromosomal location, gene linkage, and tissue-specific expression J Biol Chem 270 1995 14568-14575
    • (1995) J. Biol. Chem. , vol.270 , pp. 14568-14575
    • Belaaouaj, A.1    Shipley, J.M.2    Kobayashi, D.K.3    Zimonjic, D.B.4    Popescu, N.5    Silverman, G.A.6
  • 39
    • 0030469388 scopus 로고    scopus 로고
    • Differential regulation of metalloelastase activity in murine peritoneal macrophages by granulocyte-macrophage colony-stimulating factor and macrophage colony-stimulating factor
    • Kumar R. Dong Z. Fidler I.J. Differential regulation of metalloelastase activity in murine peritoneal macrophages by granulocyte-macrophage colony-stimulating factor and macrophage colony-stimulating factor J Immunol 157 1996 5104-5111
    • (1996) J. Immunol. , vol.157 , pp. 5104-5111
    • Kumar, R.1    Dong, Z.2    Fidler, I.J.3
  • 40
    • 0034096943 scopus 로고    scopus 로고
    • Th2 cell membrane factors in association with IL-4 enhance matrix metalloproteinase-1 (MMP-1) while decreasing MMP-9 production by granulocyte-macrophage colony-stimulating factor-differentiated human monocytes
    • Chizzolini C. Rezzonico R. De Luca C. Burger D. Dayer J.M. Th2 cell membrane factors in association with IL-4 enhance matrix metalloproteinase-1 (MMP-1) while decreasing MMP-9 production by granulocyte-macrophage colony-stimulating factor-differentiated human monocytes J Immunol 164 2000 5952-5960
    • (2000) J. Immunol. , vol.164 , pp. 5952-5960
    • Chizzolini, C.1    Rezzonico, R.2    De Luca, C.3    Burger, D.4    Dayer, J.M.5
  • 44
    • 0024602827 scopus 로고
    • Tissue destruction by neutrophils
    • Weiss S.J. Tissue destruction by neutrophils N Engl J Med 320 1989 365-376
    • (1989) N. Engl. J. Med. , vol.320 , pp. 365-376
    • Weiss, S.J.1
  • 46
    • 0028658358 scopus 로고
    • Effects of tetracyclines on neutrophil, gingival, and salivary collagenases. A functional and western-blot assessment with special reference to their cellular sources in periodontal diseases
    • Sorsa T. Ding Y. Salo T. Lauhio A. Teronen O. Ingman T. et al. Effects of tetracyclines on neutrophil, gingival, and salivary collagenases. A functional and western-blot assessment with special reference to their cellular sources in periodontal diseases Ann N Y Acad Sci 732 1994 112-131
    • (1994) Ann. N. Y. Acad Sci. , vol.732 , pp. 112-131
    • Sorsa, T.1    Ding, Y.2    Salo, T.3    Lauhio, A.4    Teronen, O.5    Ingman, T.6
  • 48
    • 0031880691 scopus 로고    scopus 로고
    • Soluble factor(s) released from neutrophils activates endothelial cell matrix metalloproteinase-2
    • Schwartz J.D. Monea S. Marcus S.G. Patel S. Eng K. Galloway A.C. et al. Soluble factor(s) released from neutrophils activates endothelial cell matrix metalloproteinase-2 J Surg Res 76 1998 79-85
    • (1998) J. Surg. Res. , vol.76 , pp. 79-85
    • Schwartz, J.D.1    Monea, S.2    Marcus, S.G.3    Patel, S.4    Eng, K.5    Galloway, A.C.6
  • 49
    • 0028021464 scopus 로고
    • Direct contact beween T lymphocytes and monocytes is a major pathway for induction of metalloproteinase expression
    • Lacraz S. Isler P. Vey E. Welgus H.G. Dayer J.M. Direct contact beween T lymphocytes and monocytes is a major pathway for induction of metalloproteinase expression J Biol Chem 269 1994 22027-22033
    • (1994) J. Biol. Chem. , vol.269 , pp. 22027-22033
    • Lacraz, S.1    Isler, P.2    Vey, E.3    Welgus, H.G.4    Dayer, J.M.5
  • 50
    • 0032520784 scopus 로고    scopus 로고
    • Bi-directional induction of matrix metalloproteinase-9 and tissue inhibitor of matrix metalloproteinase-1 during T lymphoma/endothelial cell contact: Implication of ICAM-1
    • Aoudjit F. Potworowski E.F. St-Pierre Y. Bi-directional induction of matrix metalloproteinase-9 and tissue inhibitor of matrix metalloproteinase-1 during T lymphoma/endothelial cell contact: implication of ICAM-1 J Immunol 160 1998 2967-2973
    • (1998) J. Immunol. , vol.160 , pp. 2967-2973
    • Aoudjit, F.1    Potworowski, E.F.2    St-Pierre, Y.3
  • 51
    • 0035477996 scopus 로고    scopus 로고
    • Human mast cells release metalloproteinase-9 on contact with activated T cells: Juxtacrine regulation by TNF-alpha
    • Baram D. Vaday G.G. Salamon P. Drucker I. Hershkoviz R. Mekori Y.A. Human mast cells release metalloproteinase-9 on contact with activated T cells: juxtacrine regulation by TNF-alpha J Immunol 167 2001 4008-4016
    • (2001) J. Immunol. , vol.167 , pp. 4008-4016
    • Baram, D.1    Vaday, G.G.2    Salamon, P.3    Drucker, I.4    Hershkoviz, R.5    Mekori, Y.A.6
  • 52
    • 0031908391 scopus 로고    scopus 로고
    • Activated T lymphocytes induce degranulation and cytokine production by human mast cells following cell-to-cell contact
    • Bhattacharyya S.P. Drucker I. Reshef T. Kirshenbaum A.S. Metcalfe D.D. Mekori Y.A. Activated T lymphocytes induce degranulation and cytokine production by human mast cells following cell-to-cell contact J Leukoc Biol 63 1998 337-341
    • (1998) J. Leukoc. Biol. , vol.63 , pp. 337-341
    • Bhattacharyya, S.P.1    Drucker, I.2    Reshef, T.3    Kirshenbaum, A.S.4    Metcalfe, D.D.5    Mekori, Y.A.6
  • 53
    • 0031689268 scopus 로고    scopus 로고
    • Imbalance between interstitial collagenase and tissue inhibitor of metalloproteinases 1 in synoviocytes and fibroblasts upon direct contact with stimulated T lymphocytes: Involvement of membrane-associated cytokines
    • Burger D. Rezzonico R. Li J.M. Modoux C. Pierce R.A. Welgus H.G. et al. Imbalance between interstitial collagenase and tissue inhibitor of metalloproteinases 1 in synoviocytes and fibroblasts upon direct contact with stimulated T lymphocytes: involvement of membrane-associated cytokines Arthritis Rheum 41 1998 1748-1759
    • (1998) Arthritis Rheum. , vol.41 , pp. 1748-1759
    • Burger, D.1    Rezzonico, R.2    Li, J.M.3    Modoux, C.4    Pierce, R.A.5    Welgus, H.G.6
  • 54
    • 0026571239 scopus 로고
    • Neutrophil stimulation and priming by direct contact with activated human T lymphocytes
    • Zhang J.H. Ferrante A. Arrigo A.P. Dayer J.M. Neutrophil stimulation and priming by direct contact with activated human T lymphocytes J Immunol 148 1992 177-181
    • (1992) J. Immunol. , vol.148 , pp. 177-181
    • Zhang, J.H.1    Ferrante, A.2    Arrigo, A.P.3    Dayer, J.M.4
  • 55
    • 0029983775 scopus 로고    scopus 로고
    • Activation of human monocytes through CD40 induces matrix metalloproteinases
    • Malik N. Greenfield B.W. Wahl A.F. Kiener P.A. Activation of human monocytes through CD40 induces matrix metalloproteinases J Immunol 156 1996 3952-3960
    • (1996) J. Immunol. , vol.156 , pp. 3952-3960
    • Malik, N.1    Greenfield, B.W.2    Wahl, A.F.3    Kiener, P.A.4
  • 56
    • 0028860849 scopus 로고
    • Stimulation of matrix metalloproteinase-dependent migration of T cells by eicosanoids
    • Leppert D. Hauser S.L. Kishiyama J.L. An S. Zeng L. Goetzl E.J. Stimulation of matrix metalloproteinase-dependent migration of T cells by eicosanoids FASEB J 9 1995 1473-1481
    • (1995) FASEB J. , vol.9 , pp. 1473-1481
    • Leppert, D.1    Hauser, S.L.2    Kishiyama, J.L.3    An, S.4    Zeng, L.5    Goetzl, E.J.6
  • 59
    • 0030581634 scopus 로고    scopus 로고
    • Macrophage metalloelastase degrades matrix and myelin proteins and processes a tumour necrosis factor-alpha fusion protein
    • Chandler S. Cossins J. Lury J. Wells G. Macrophage metalloelastase degrades matrix and myelin proteins and processes a tumour necrosis factor-alpha fusion protein Biochem Biophys Res Commun 228 1996 421-429
    • (1996) Biochem. Biophys. Res. Commun. , vol.228 , pp. 421-429
    • Chandler, S.1    Cossins, J.2    Lury, J.3    Wells, G.4
  • 62
    • 0025274640 scopus 로고
    • Cytokines and cytokine inhibitors or antagonists in rheumatoid arthritis
    • Arend W.P. Dayer J.M. Cytokines and cytokine inhibitors or antagonists in rheumatoid arthritis Arthritis Rheum 33 1990 305-315
    • (1990) Arthritis Rheum. , vol.33 , pp. 305-315
    • Arend, W.P.1    Dayer, J.M.2
  • 63
    • 0028136769 scopus 로고
    • Chemokines, inflammation and the immune system
    • Taub D.D. Oppenheim J.J. Chemokines, inflammation and the immune system Ther Immunol 1 1994 229-246
    • (1994) Ther. Immunol. , vol.1 , pp. 229-246
    • Taub, D.D.1    Oppenheim, J.J.2
  • 64
    • 0025792013 scopus 로고
    • Constitutive expression of a 92-kD gelatinase (type V collagenase) by rheumatoid synovial fibroblasts and its induction in normal human fibroblasts by inflammatory cytokines
    • Unemori E.N. Hibbs M.S. Amento E.P. Constitutive expression of a 92-kD gelatinase (type V collagenase) by rheumatoid synovial fibroblasts and its induction in normal human fibroblasts by inflammatory cytokines J Clin Invest 88 1991 1656
    • (1991) J. Clin. Invest. , vol.88 , pp. 1656
    • Unemori, E.N.1    Hibbs, M.S.2    Amento, E.P.3
  • 65
    • 15444347160 scopus 로고    scopus 로고
    • Matrix metalloproteinase-8 is expressed in rheumatoid synovial fibroblasts and endothelial cells
    • Hanemaaijer R. Sorsa T. Konttinen Y.T. Ding Y. Sutinen M. Visser H. et al. Matrix metalloproteinase-8 is expressed in rheumatoid synovial fibroblasts and endothelial cells J Biol Chem 272 1997 31504-31509
    • (1997) J. Biol. Chem. , vol.272 , pp. 31504-31509
    • Hanemaaijer, R.1    Sorsa, T.2    Konttinen, Y.T.3    Ding, Y.4    Sutinen, M.5    Visser, H.6
  • 67
    • 0031660472 scopus 로고    scopus 로고
    • Regulation of monocyte MMP-9 production by TNF-alpha and a tumour-derived soluble factor (MMPSF)
    • Leber T.M. Balkwill F.R. Regulation of monocyte MMP-9 production by TNF-alpha and a tumour-derived soluble factor (MMPSF) Br J Cancer 78 1998 724-732
    • (1998) Br. J. Cancer , vol.78 , pp. 724-732
    • Leber, T.M.1    Balkwill, F.R.2
  • 68
    • 0033755867 scopus 로고    scopus 로고
    • Fibronectin-bound TNF-alpha stimulates monocyte matrix metalloproteinase-9 expression and regulates chemotaxis
    • Vaday G.G. Hershkoviz R. Rahat M.A. Lahat N. Cahalon L. Lider O. Fibronectin-bound TNF-alpha stimulates monocyte matrix metalloproteinase-9 expression and regulates chemotaxis J Leukoc Biol 68 2000 737-747
    • (2000) J. Leukoc. Biol. , vol.68 , pp. 737-747
    • Vaday, G.G.1    Hershkoviz, R.2    Rahat, M.A.3    Lahat, N.4    Cahalon, L.5    Lider, O.6
  • 69
    • 0035071646 scopus 로고    scopus 로고
    • Transforming growth factor-beta suppresses tumor necrosis factor alpha-induced matrix metalloproteinase-9 expression in monocytes
    • Vaday G.G. Schor H. Rahat M.A. Lahat N. Lider O. Transforming growth factor-beta suppresses tumor necrosis factor alpha-induced matrix metalloproteinase-9 expression in monocytes J Leukoc Biol 69 2001 613-621
    • (2001) J. Leukoc. Biol. , vol.69 , pp. 613-621
    • Vaday, G.G.1    Schor, H.2    Rahat, M.A.3    Lahat, N.4    Lider, O.5
  • 70
    • 0036178923 scopus 로고    scopus 로고
    • Chemokine stimulation of monocyte matrix metalloproteinase-9 requires endogenous TNF-alpha
    • Robinson S.C. Scott K.A. Balkwill F.R. Chemokine stimulation of monocyte matrix metalloproteinase-9 requires endogenous TNF-alpha Eur J Immunol 32 2002 404-412
    • (2002) Eur. J. Immunol. , vol.32 , pp. 404-412
    • Robinson, S.C.1    Scott, K.A.2    Balkwill, F.R.3
  • 71
    • 0030292766 scopus 로고    scopus 로고
    • TNF-alpha and IL-1 beta selectively induce expression of 92-kDa gelatinase by human macrophages
    • Sarén P. Welgus H.G. Kovanen P.T. TNF-alpha and IL-1 beta selectively induce expression of 92-kDa gelatinase by human macrophages J Immunol 157 1996 4159-4165
    • (1996) J. Immunol. , vol.157 , pp. 4159-4165
    • Sarén, P.1    Welgus, H.G.2    Kovanen, P.T.3
  • 72
    • 0028864991 scopus 로고
    • A distinct array of proinflammatory cytokines is expressed in human colon epithelial cells in response to bacterial invasion
    • Jung H.C. Eckmann L. Yang S.K. Panja A. Fierer J. Morzycka-Wroblewska E. et al. A distinct array of proinflammatory cytokines is expressed in human colon epithelial cells in response to bacterial invasion J Clin Invest 95 1995 55-65
    • (1995) J. Clin. Invest. , vol.95 , pp. 55-65
    • Jung, H.C.1    Eckmann, L.2    Yang, S.K.3    Panja, A.4    Fierer, J.5    Morzycka-Wroblewska, E.6
  • 73
    • 0028362088 scopus 로고
    • The induction of 72-kD gelatinase in T cells upon adhesion to endothelial cells is VCAM-1 dependent
    • Romanic A.M. Madri J.A. The induction of 72-kD gelatinase in T cells upon adhesion to endothelial cells is VCAM-1 dependent J Cell Biol 125 1994 1165-1178
    • (1994) J. Cell. Biol. , vol.125 , pp. 1165-1178
    • Romanic, A.M.1    Madri, J.A.2
  • 74
    • 0029953307 scopus 로고    scopus 로고
    • Integrin-dependent role of human T cell matrix metalloproteinase activity in chemotaxis through a model basement membrane
    • Xia M. Sreedharan S.P. Dazin P. Damsky C.H. Goetzl E.J. Integrin-dependent role of human T cell matrix metalloproteinase activity in chemotaxis through a model basement membrane J Cell Biochem 61 1996 452-458
    • (1996) J. Cell. Biochem. , vol.61 , pp. 452-458
    • Xia, M.1    Sreedharan, S.P.2    Dazin, P.3    Damsky, C.H.4    Goetzl, E.J.5
  • 75
    • 0033563257 scopus 로고    scopus 로고
    • Regulation of monocyte survival in vitro by deposited IgG: Role of macrophage colony-stimulating factor
    • Marsh C.B. Pomerantz R.P. Parker J.M. Winnard A.V. Mazzaferri E.L. Moldovan N. et al. Regulation of monocyte survival in vitro by deposited IgG: role of macrophage colony-stimulating factor J Immunol 162 1999 6217-6225
    • (1999) J. Immunol. , vol.162 , pp. 6217-6225
    • Marsh, C.B.1    Pomerantz, R.P.2    Parker, J.M.3    Winnard, A.V.4    Mazzaferri, E.L.5    Moldovan, N.6
  • 76
    • 0023771429 scopus 로고
    • Effects of granulocyte-macrophage colony-stimulating factor and colony-stimulating factor-1 on the proliferation and differentiation of murine alveolar macrophages
    • Akagawa K.S. Kamoshita K. Tokunaga T. Effects of granulocyte-macrophage colony-stimulating factor and colony-stimulating factor-1 on the proliferation and differentiation of murine alveolar macrophages J Immunol 141 1988 3383-3390
    • (1988) J. Immunol. , vol.141 , pp. 3383-3390
    • Akagawa, K.S.1    Kamoshita, K.2    Tokunaga, T.3
  • 77
    • 0030043188 scopus 로고    scopus 로고
    • Kinetics and dose dependence of macrophage colony-stimulating factor-induced proliferation and activation of murine mononuclear phagocytes in situ: Differences between lungs, liver and spleen
    • Held T.K. Mielke M.E. Unger M. Trautmann M. Cross A.S. Kinetics and dose dependence of macrophage colony-stimulating factor-induced proliferation and activation of murine mononuclear phagocytes in situ: differences between lungs, liver and spleen J Interferon Cytokine Res 16 1996 159-168
    • (1996) J. Interferon. Cytokine Res. , vol.16 , pp. 159-168
    • Held, T.K.1    Mielke, M.E.2    Unger, M.3    Trautmann, M.4    Cross, A.S.5
  • 79
    • 0033178501 scopus 로고    scopus 로고
    • Serial analysis of gene expression in human monocytes and macrophages
    • Hashimoto S. Suzuki T. Dong H.Y. Yamazaki N. Matsushima K. Serial analysis of gene expression in human monocytes and macrophages Blood 94 1999 837-844
    • (1999) Blood , vol.94 , pp. 837-844
    • Hashimoto, S.1    Suzuki, T.2    Dong, H.Y.3    Yamazaki, N.4    Matsushima, K.5
  • 80
    • 0032530673 scopus 로고    scopus 로고
    • Differential regulation of monocyte matrix metalloproteinase and TIMP-1 production by TNF-alpha, granulocyte-macrophage CSF, and IL-1 beta through prostaglandin-dependent and independent mechanisms
    • Zhang Y. McCluskey K. Fujii K. Wahl L.M. Differential regulation of monocyte matrix metalloproteinase and TIMP-1 production by TNF-alpha, granulocyte-macrophage CSF, and IL-1 beta through prostaglandin-dependent and independent mechanisms J Immunol 161 1998 3071-3076
    • (1998) J. Immunol. , vol.161 , pp. 3071-3076
    • Zhang, Y.1    McCluskey, K.2    Fujii, K.3    Wahl, L.M.4
  • 81
    • 0037043820 scopus 로고    scopus 로고
    • Matrix metalloproteinase 9 (MMP-9/gelatinase B) proteolytically cleaves ICAM-1 and participates in tumor cell resistance to natural killer cell-mediated cytotoxicity
    • Fiore E. Fusco C. Romero P. Stamenkovic I. Matrix metalloproteinase 9 (MMP-9/gelatinase B) proteolytically cleaves ICAM-1 and participates in tumor cell resistance to natural killer cell-mediated cytotoxicity Oncogene 21 2002 5213-5223
    • (2002) Oncogene , vol.21 , pp. 5213-5223
    • Fiore, E.1    Fusco, C.2    Romero, P.3    Stamenkovic, I.4
  • 84
    • 0032510494 scopus 로고    scopus 로고
    • A casual role for E-cadherin in the translation from adenocarcinoma to carcinoma
    • Perl A.K. Wilgenbus P. Dahl U. Semb H. Christofori G. A casual role for E-cadherin in the translation from adenocarcinoma to carcinoma Nature 392 1998 190-193
    • (1998) Nature , vol.392 , pp. 190-193
    • Perl, A.K.1    Wilgenbus, P.2    Dahl, U.3    Semb, H.4    Christofori, G.5
  • 85
    • 0032147124 scopus 로고    scopus 로고
    • Adenosine triphosphate-induced shedding of CD23 and L-selectin (CD62L) from lymphocytes is mediated by the same receptor but different metalloproteinases
    • Gu B. Bendall L.J. Wiley J.S. Adenosine triphosphate-induced shedding of CD23 and L-selectin (CD62L) from lymphocytes is mediated by the same receptor but different metalloproteinases Blood 92 1998 946-951
    • (1998) Blood , vol.92 , pp. 946-951
    • Gu, B.1    Bendall, L.J.2    Wiley, J.S.3
  • 86
    • 0033580237 scopus 로고    scopus 로고
    • CD44 cleavage induced by a membrane-associated metalloproteinase plays a critical role in tumor cell migration
    • Okamoto I. Kawano Y. Tsuiki H. Sasaki J. Nakao M. Matsumoto M. et al. CD44 cleavage induced by a membrane-associated metalloproteinase plays a critical role in tumor cell migration Oncogene 18 1999 1435-1446
    • (1999) Oncogene , vol.18 , pp. 1435-1446
    • Okamoto, I.1    Kawano, Y.2    Tsuiki, H.3    Sasaki, J.4    Nakao, M.5    Matsumoto, M.6
  • 87
    • 0028483534 scopus 로고
    • Regulation of tumour necrosis factor-alpha processing by a metalloproteinase inhibitor
    • McGeehan G.M. Becherer J.D. Bast R.C. Boyer C.M. Champion B. Connolly K.M. et al. Regulation of tumour necrosis factor-alpha processing by a metalloproteinase inhibitor Nature 370 1994 558-561
    • (1994) Nature , vol.370 , pp. 558-561
    • McGeehan, G.M.1    Becherer, J.D.2    Bast, R.C.3    Boyer, C.M.4    Champion, B.5    Connolly, K.M.6
  • 88
    • 0025134586 scopus 로고
    • Immune modulation of metalloproteinase production in human macrophages. Selective pretranslational suppression of interstitial collagenase and stromelysin biosynthesis by interferon-gamma
    • Shapiro S.D. Campbell E.J. Kobayashi D.K. Welgus H.G. Immune modulation of metalloproteinase production in human macrophages. Selective pretranslational suppression of interstitial collagenase and stromelysin biosynthesis by interferon-gamma J Clin Invest 86 1990 1204-1210
    • (1990) J. Clin. Invest. , vol.86 , pp. 1204-1210
    • Shapiro, S.D.1    Campbell, E.J.2    Kobayashi, D.K.3    Welgus, H.G.4
  • 89
    • 0025239695 scopus 로고
    • Inhibition of phospholipase activity in human monocytes by IFN-gamma blocks endogenous prostaglandin E2-dependent collagenase production
    • Wahl L.M. Corcoran M.E. Mergenhagen S.E. Finbloom D.S. Inhibition of phospholipase activity in human monocytes by IFN-gamma blocks endogenous prostaglandin E2-dependent collagenase production J Immunol 144 1990 3518-3522
    • (1990) J Immunol , vol.144 , pp. 3518-3522
    • Wahl, L.M.1    Corcoran, M.E.2    Mergenhagen, S.E.3    Finbloom, D.S.4
  • 90
    • 0025847582 scopus 로고
    • Matrix metalloproteinases and their inhibitors in connective tissue remodeling
    • Woessner Jr. J.F. Matrix metalloproteinases and their inhibitors in connective tissue remodeling FASEB J 5 1991 2145-2154
    • (1991) FASEB J. , vol.5 , pp. 2145-2154
    • Woessner Jr., J.F.1
  • 91
    • 0026515544 scopus 로고
    • Interleukin 4 inhibition of prostaglandin E2 synthesis blocks interstitial collagenase and 92-kDa type IV collagenase/gelatinase production by human monocytes
    • Corcoran M.L. Stetler-Stevenson W.G. Brown P.D. Wahl L.M. Interleukin 4 inhibition of prostaglandin E2 synthesis blocks interstitial collagenase and 92-kDa type IV collagenase/gelatinase production by human monocytes J Biol Chem 267 1992 515-519
    • (1992) J. Biol. Chem. , vol.267 , pp. 515-519
    • Corcoran, M.L.1    Stetler-Stevenson, W.G.2    Brown, P.D.3    Wahl, L.M.4
  • 93
    • 0027990831 scopus 로고
    • Interleukin 10 suppression of monocyte prostaglandin H synthase-2. Mechanism of inhibition of prostaglandin-dependent matrix metalloproteinase production
    • Mertz P.M. DeWitt D.L. Stetler-Stevenson W.G. Wahl L.M. Interleukin 10 suppression of monocyte prostaglandin H synthase-2. Mechanism of inhibition of prostaglandin-dependent matrix metalloproteinase production J Biol Chem 269 1994 21322-21329
    • (1994) J. Biol. Chem. , vol.269 , pp. 21322-21329
    • Mertz, P.M.1    DeWitt, D.L.2    Stetler-Stevenson, W.G.3    Wahl, L.M.4
  • 94
    • 0028855894 scopus 로고
    • IL-10 inhibits metalloproteinase and stimulates TIMP-1 production in human mononuclear phagocytes
    • Lacraz S. Nicod L. Chicheportiche R. Welgus H.G. Dayer J.M. IL-10 inhibits metalloproteinase and stimulates TIMP-1 production in human mononuclear phagocytes J Clin Invest 96 1995 2304-2310
    • (1995) J. Clin. Invest. , vol.96 , pp. 2304-2310
    • Lacraz, S.1    Nicod, L.2    Chicheportiche, R.3    Welgus, H.G.4    Dayer, J.M.5
  • 95
    • 0030891497 scopus 로고    scopus 로고
    • Bacterial lipopolysaccharide rapidly inhibits expression of C-C chemokine receptors in human monocytes
    • Sica A. Saccani A. Borsatti A. Power C.A. Wells T.N. Luini W. et al. Bacterial lipopolysaccharide rapidly inhibits expression of C-C chemokine receptors in human monocytes J Exp Med 185 1997 969-974
    • (1997) J. Exp. Med. , vol.185 , pp. 969-974
    • Sica, A.1    Saccani, A.2    Borsatti, A.3    Power, C.A.4    Wells, T.N.5    Luini, W.6
  • 96
    • 0033049705 scopus 로고    scopus 로고
    • Downregulation by tumor necrosis factor-alpha of monocyte CCR2 expression and monocyte chemotactic protein-1-induced transendothelial migration is antagonized by oxidized low-density lipoprotein: A potential mechanism of monocyte retention in atherosclerotic lesions
    • Weber C. Draude G. Weber K.S. Wubert J. Lorenz R.L. Weber P.C. Downregulation by tumor necrosis factor-alpha of monocyte CCR2 expression and monocyte chemotactic protein-1-induced transendothelial migration is antagonized by oxidized low-density lipoprotein: a potential mechanism of monocyte retention in atherosclerotic lesions Atherosclerosis 145 1999 115-123
    • (1999) Atherosclerosis , vol.145 , pp. 115-123
    • Weber, C.1    Draude, G.2    Weber, K.S.3    Wubert, J.4    Lorenz, R.L.5    Weber, P.C.6
  • 97
    • 0031851423 scopus 로고    scopus 로고
    • Autocrine regulation of matrix metalloproteinase-9 gene expression and secretion by tumor necrosis factor-alpha (TNF-alpha) in NB4 leukemic cells: Specific involvement of TNF receptor type 1
    • Ismair M.G. Ries C. Lottspeich F. Zang C. Kolb H.J. Petrides P.E. Autocrine regulation of matrix metalloproteinase-9 gene expression and secretion by tumor necrosis factor-alpha (TNF-alpha) in NB4 leukemic cells: specific involvement of TNF receptor type 1 Leukemia 12 1998 1136-1143
    • (1998) Leukemia , vol.12 , pp. 1136-1143
    • Ismair, M.G.1    Ries, C.2    Lottspeich, F.3    Zang, C.4    Kolb, H.J.5    Petrides, P.E.6
  • 98
    • 0032479967 scopus 로고    scopus 로고
    • Gelatinase B-deficient mice are resistant to experimental bullous pemphigoid
    • Liu Z. Shipley J.M. Vu T.H. Zhou X. Diaz L.A. Werb Z. et al. Gelatinase B-deficient mice are resistant to experimental bullous pemphigoid J Exp Med 188 1998 475-482
    • (1998) J. Exp. Med. , vol.188 , pp. 475-482
    • Liu, Z.1    Shipley, J.M.2    Vu, T.H.3    Zhou, X.4    Diaz, L.A.5    Werb, Z.6
  • 99
    • 0030483220 scopus 로고    scopus 로고
    • Interferon beta-1b inhibits gelatinase secretion and in vitro migration of human T cells: A possible mechanism for treatment efficacy in multiple sclerosis
    • Leppert D. Waubant E. Burk M.R. Oksenberg J.R. Hauser S.L. Interferon beta-1b inhibits gelatinase secretion and in vitro migration of human T cells: a possible mechanism for treatment efficacy in multiple sclerosis Ann Neurol 40 1996 846-852
    • (1996) Ann. Neurol. , vol.40 , pp. 846-852
    • Leppert, D.1    Waubant, E.2    Burk, M.R.3    Oksenberg, J.R.4    Hauser, S.L.5
  • 100
    • 0030066034 scopus 로고    scopus 로고
    • Stimulus specificity of matrix metalloproteinase dependence of human T cell migration through a model basement membrane
    • Xia M. Leppert D. Hauser S.L. Sneedharan S.P. Nelson P.J. Krensky A.M. et al. Stimulus specificity of matrix metalloproteinase dependence of human T cell migration through a model basement membrane J Immunol 156 1996 160-167
    • (1996) J. Immunol. , vol.156 , pp. 160-167
    • Xia, M.1    Leppert, D.2    Hauser, S.L.3    Sneedharan, S.P.4    Nelson, P.J.5    Krensky, A.M.6
  • 101
    • 0026570208 scopus 로고
    • Correlation in the expression of type IV collagenase and the invasive and chemotactic abilities of myelomonocytic cells during differentiation into macrophages
    • Pluznik D.H. Fridman R. Reich R. Correlation in the expression of type IV collagenase and the invasive and chemotactic abilities of myelomonocytic cells during differentiation into macrophages Exp Hematol 20 1992 57-63
    • (1992) Exp. Hematol. , vol.20 , pp. 57-63
    • Pluznik, D.H.1    Fridman, R.2    Reich, R.3
  • 105
    • 0033214433 scopus 로고    scopus 로고
    • Regulation of intestinal alpha-defensin activation by the metalloproteinase matrilysin in innate host defense
    • Wilson C.L. Ouellette A.J. Satchell D.P. Ayabe T. López-Boada Y.S. Stratman J.L. et al. Regulation of intestinal alpha-defensin activation by the metalloproteinase matrilysin in innate host defense Science 286 1999 113-117
    • (1999) Science , vol.286 , pp. 113-117
    • Wilson, C.L.1    Ouellette, A.J.2    Satchell, D.P.3    Ayabe, T.4    López-Boada, Y.S.5    Stratman, J.L.6
  • 106
    • 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. Gong J.H. Wong J.P. Wallace J.L. Clark-Lewis I. Overall C.M. Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties in vivo Blood 100 2002 1160-1167
    • (2002) Blood , vol.100 , pp. 1160-1167
    • McQuibban, G.A.1    Gong, J.H.2    Wong, J.P.3    Wallace, J.L.4    Clark-Lewis, I.5    Overall, C.M.6
  • 107
    • 0342872046 scopus 로고    scopus 로고
    • Regulation of matrix metalloproteinase expression in human vascular smooth muscle cells by T lymphocytes: A role for CD40 signaling in plaque rupture?
    • Schönbeck U. Mach F. Sukhova G.K. Murphy C. Bonnefoy J.Y. Fabunmi R.P. et al. Regulation of matrix metalloproteinase expression in human vascular smooth muscle cells by T lymphocytes: a role for CD40 signaling in plaque rupture? Circ Res 81 1997 448-454
    • (1997) Circ. Res. , vol.81 , pp. 448-454
    • Schönbeck, U.1    Mach, F.2    Sukhova, G.K.3    Murphy, C.4    Bonnefoy, J.Y.5    Fabunmi, R.P.6
  • 108
    • 0023698767 scopus 로고
    • Transforming growth factor beta 1 and cAMP inhibit transcription of epidermal growth factor and oncogene-induced transin RNA
    • Kerr L.D. Olashaw N.E. Matrisian L.M. Transforming growth factor beta 1 and cAMP inhibit transcription of epidermal growth factor and oncogene-induced transin RNA J Biol Chem 263 1988 16999-17005
    • (1988) J. Biol. Chem. , vol.263 , pp. 16999-17005
    • Kerr, L.D.1    Olashaw, N.E.2    Matrisian, L.M.3
  • 109
    • 0025866180 scopus 로고
    • Transcriptional and post-transcriptional regulation of a 72-kDa gelatinase/type IV collagenase by transforming growth factor-beta 1 in human fibroblasts: Comparisons with collagenase and tissue inhibitor of matrix metalloproteinase gene expression
    • Overall C.M. Wrana J.L. Sodek J. Transcriptional and post-transcriptional regulation of a 72-kDa gelatinase/type IV collagenase by transforming growth factor-beta 1 in human fibroblasts: Comparisons with collagenase and tissue inhibitor of matrix metalloproteinase gene expression J Biol Chem 266 1991 14064-14071
    • (1991) J. Biol. Chem. , vol.266 , pp. 14064-14071
    • Overall, C.M.1    Wrana, J.L.2    Sodek, J.3
  • 110
    • 0036758650 scopus 로고    scopus 로고
    • Matrix metalloproteinases limit functional recovery after spinal cord injury by modulation of early vascular events
    • Noble L.J. Donovan F. Igarashi T. Goussev S. Werb Z. Matrix metalloproteinases limit functional recovery after spinal cord injury by modulation of early vascular events J Neurosci 22 2002 7526-7535
    • (2002) J. Neurosci. , vol.22 , pp. 7526-7535
    • Noble, L.J.1    Donovan, F.2    Igarashi, T.3    Goussev, S.4    Werb, Z.5
  • 111
    • 0036020282 scopus 로고    scopus 로고
    • Expression of matrix-metalloproteinases and their inhibitors in the wounds of diabetic and non-diabetic patients
    • Lobmann R. Ambrosch A. Schultz G. Waldmann K. Schiweck S. Lehnert H. Expression of matrix-metalloproteinases and their inhibitors in the wounds of diabetic and non-diabetic patients Diabetologia 45 2002 1011-1016
    • (2002) Diabetologia , vol.45 , pp. 1011-1016
    • Lobmann, R.1    Ambrosch, A.2    Schultz, G.3    Waldmann, K.4    Schiweck, S.5    Lehnert, H.6
  • 115
    • 0027409322 scopus 로고
    • Localization of intestinal interleukin 1 activity and protein and gene expression to lamina propria cells
    • Youngman K.R. Simon P.L. West G.A. Cominelli F. Rachmilewitz D. Klein J.S. et al. Localization of intestinal interleukin 1 activity and protein and gene expression to lamina propria cells Gastroenterology 104 1993 749-758
    • (1993) Gastroenterology , vol.104 , pp. 749-758
    • Youngman, K.R.1    Simon, P.L.2    West, G.A.3    Cominelli, F.4    Rachmilewitz, D.5    Klein, J.S.6
  • 116
    • 0028236232 scopus 로고
    • Tumor necrosis factor alpha-producing cells in the intestinal mucosa of children with inflammatory bowel disease
    • Breese E.J. Michie C.A. Nicholls S.W. Murch S.H. Williams C.B. Domizio P. et al. Tumor necrosis factor alpha-producing cells in the intestinal mucosa of children with inflammatory bowel disease Gastroenterology 106 1994 1455-1466
    • (1994) Gastroenterology , vol.106 , pp. 1455-1466
    • Breese, E.J.1    Michie, C.A.2    Nicholls, S.W.3    Murch, S.H.4    Williams, C.B.5    Domizio, P.6
  • 117
    • 0026531017 scopus 로고
    • Tumour necrosis factor alpha in stool as a marker of intestinal inflammation
    • Braegger C.P. Nicholls S. Murch S.H. Stephens S. MacDonald T.T. Tumour necrosis factor alpha in stool as a marker of intestinal inflammation Lancet 339 1992 89-91
    • (1992) Lancet , vol.339 , pp. 89-91
    • Braegger, C.P.1    Nicholls, S.2    Murch, S.H.3    Stephens, S.4    MacDonald, T.T.5
  • 118
    • 0027486125 scopus 로고
    • Location of tumour necrosis factor alpha by immunohistochemistry in chronic inflammatory bowel disease
    • Murch S.H. Braegger C.P. Walker-Smith J.A. MacDonald T.T. Location of tumour necrosis factor alpha by immunohistochemistry in chronic inflammatory bowel disease Gut 34 1993 1705-1709
    • (1993) Gut , vol.34 , pp. 1705-1709
    • Murch, S.H.1    Braegger, C.P.2    Walker-Smith, J.A.3    MacDonald, T.T.4
  • 119
    • 0032522666 scopus 로고    scopus 로고
    • A p55 TNF receptor immunoadhesion prevents T cell-mediated intestinal injury by inhibiting matrix metalloproteinase production
    • Pender S.L. Fell J.M. Chamow S.M. Ashkenazi A. MacDonald T.T. A p55 TNF receptor immunoadhesion prevents T cell-mediated intestinal injury by inhibiting matrix metalloproteinase production J Immunol 160 1998 4098-4103
    • (1998) J. Immunol. , vol.160 , pp. 4098-4103
    • Pender, S.L.1    Fell, J.M.2    Chamow, S.M.3    Ashkenazi, A.4    MacDonald, T.T.5
  • 120
    • 0028347680 scopus 로고
    • Distribution of the matrix metalloproteinases stromelysin, gelatinases A and B, and collagenase in Crohn's disease and normal intestine
    • Bailey C.J. Hembry R.M. Alexander A. Irving M.H. Grant M.E. Shuttleworth C.A. Distribution of the matrix metalloproteinases stromelysin, gelatinases A and B, and collagenase in Crohn's disease and normal intestine J Clin Pathol 47 1994 113-116
    • (1994) J. Clin. Pathol. , vol.47 , pp. 113-116
    • Bailey, C.J.1    Hembry, R.M.2    Alexander, A.3    Irving, M.H.4    Grant, M.E.5    Shuttleworth, C.A.6
  • 121
    • 0036785258 scopus 로고    scopus 로고
    • Upregulation of matrix metalloproteinases in a model of T cell mediated injury in the gut: Analysis by gene array and in situ hybridisation
    • Salmela M.T. MacDonald T.T. Black D. Irvine B. Zhuma T. Saarialho-Kere U. et al. Upregulation of matrix metalloproteinases in a model of T cell mediated injury in the gut: analysis by gene array and in situ hybridisation Gut 51 2002 540-547
    • (2002) Gut , vol.51 , pp. 540-547
    • Salmela, M.T.1    MacDonald, T.T.2    Black, D.3    Irvine, B.4    Zhuma, T.5    Saarialho-Kere, U.6
  • 122
    • 0024589689 scopus 로고
    • Extracellular matrix molecules that influence neural development
    • Sanes J.R. Extracellular matrix molecules that influence neural development Ann Rev Neurosci 12 1989 491-516
    • (1989) Ann. Rev. Neurosci. , vol.12 , pp. 491-516
    • Sanes, J.R.1
  • 123
    • 0031942524 scopus 로고    scopus 로고
    • The extracellular matrix in multiple sclerosis lesions
    • Sobel R.A. The extracellular matrix in multiple sclerosis lesions J Neuropathol Exp Neurol 57 1998 205-217
    • (1998) J. Neuropathol. Exp. Neurol. , vol.57 , pp. 205-217
    • Sobel, R.A.1
  • 124
    • 0036644958 scopus 로고    scopus 로고
    • Extracellular proteolysis in brain injury and inflammation: Role for plasminogen activators and matrix metalloproteinases
    • Lo E.H. Wang X. Cuzner M.L. Extracellular proteolysis in brain injury and inflammation: role for plasminogen activators and matrix metalloproteinases J Neurosci Res 69 2002 1-9
    • (2002) J. Neurosci. Res. , vol.69 , pp. 1-9
    • Lo, E.H.1    Wang, X.2    Cuzner, M.L.3
  • 125
    • 0034455606 scopus 로고    scopus 로고
    • Matrix metalloproteinase (MMP)-8 and and MMP-9 in cerebrospinal fluid during bacterial meningitis: Association with blood-brain barrier damage and neurological sequelae
    • Leppert D. Leib S.L. Grygar C. Miller K.M. Schaad U.B. Holländer G.A. Matrix metalloproteinase (MMP)-8 and and MMP-9 in cerebrospinal fluid during bacterial meningitis: association with blood-brain barrier damage and neurological sequelae Clin Infect Dis 31 2000 80-84
    • (2000) Clin. Infect. Dis. , vol.31 , pp. 80-84
    • Leppert, D.1    Leib, S.L.2    Grygar, C.3    Miller, K.M.4    Schaad, U.B.5    Holländer, G.A.6
  • 126
    • 0033081796 scopus 로고    scopus 로고
    • Plasminogen activators and matrix metalloproteinases, mediators of extracellular proteolysis in inflammatory demyelination of the central nervous system
    • Cuzner M.L. Opdenakker G. Plasminogen activators and matrix metalloproteinases, mediators of extracellular proteolysis in inflammatory demyelination of the central nervous system J Neuroimmunol 94 1999 1-14
    • (1999) J. Neuroimmunol. , vol.94 , pp. 1-14
    • Cuzner, M.L.1    Opdenakker, G.2
  • 127
    • 0022979424 scopus 로고
    • Secretion of metalloproteinases by stimulated capillary endothelial cells
    • Herron G.S. Banda M.J. Clark E.J. Gavrilovic J. Werb Z. Secretion of metalloproteinases by stimulated capillary endothelial cells J Biol Chem 261 1986 2814-2818
    • (1986) J. Biol. Chem. , vol.261 , pp. 2814-2818
    • Herron, G.S.1    Banda, M.J.2    Clark, E.J.3    Gavrilovic, J.4    Werb, Z.5
  • 128
    • 0028934085 scopus 로고
    • Cytokines regulate gelatinase A and B (matrix metalloproteinase 2 and 9) activity in cultured rat astrocytes
    • Gottschall P.E. Yu X. Cytokines regulate gelatinase A and B (matrix metalloproteinase 2 and 9) activity in cultured rat astrocytes J Neurochem 64 1995 1513-1520
    • (1995) J. Neurochem. , vol.64 , pp. 1513-1520
    • Gottschall, P.E.1    Yu, X.2
  • 129
    • 0029829594 scopus 로고    scopus 로고
    • Regulation of matrix metalloproteinase expressions in astrocytes, microglia and neurons
    • Gottschall P.E. Deb S. Regulation of matrix metalloproteinase expressions in astrocytes, microglia and neurons Neuroimmunomodulation 3 1996 69-75
    • (1996) Neuroimmunomodulation , vol.3 , pp. 69-75
    • Gottschall, P.E.1    Deb, S.2
  • 130
    • 0033215979 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9/gelatinase B is required for process outgrowth by oligodendrocytes
    • Oh L.Y. Larsen P.H. Krekoski C.A. Edwards D.R. Donovan F. Werb Z. et al. Matrix metalloproteinase-9/gelatinase B is required for process outgrowth by oligodendrocytes J Neurosci 19 1999 8464-8475
    • (1999) J. Neurosci. , vol.19 , pp. 8464-8475
    • Oh, L.Y.1    Larsen, P.H.2    Krekoski, C.A.3    Edwards, D.R.4    Donovan, F.5    Werb, Z.6
  • 131
    • 0034651082 scopus 로고    scopus 로고
    • Role of tissue plasminogen activator receptor LRP in hippocampal long-term potentiation
    • Zhuo M. Holtzman D.M. Li Y. Osaka H. DeMaro J. Jacquin M. et al. Role of tissue plasminogen activator receptor LRP in hippocampal long-term potentiation J Neurosci 20 2000 542-549
    • (2000) J. Neurosci. , vol.20 , pp. 542-549
    • Zhuo, M.1    Holtzman, D.M.2    Li, Y.3    Osaka, H.4    DeMaro, J.5    Jacquin, M.6
  • 132
    • 0034666112 scopus 로고    scopus 로고
    • Effects of matrix metalloproteinase-9 gene knock-out on morphological and motor outcomes after traumatic brain injury
    • Wang X. Jung J. Asahi M. Chwang W. Russo L. Moskowitz M.A. et al. Effects of matrix metalloproteinase-9 gene knock-out on morphological and motor outcomes after traumatic brain injury J Neurosci 20 2000 7037-7042
    • (2000) J. Neurosci. , vol.20 , pp. 7037-7042
    • Wang, X.1    Jung, J.2    Asahi, M.3    Chwang, W.4    Russo, L.5    Moskowitz, M.A.6
  • 133
    • 0031959973 scopus 로고    scopus 로고
    • Matrix metalloproteinase expression increases after cerebral focal ischemia in rats: Inhibition of matrix metalloproteinase-9 reduces infarct size
    • Romanic A.M. White R.F. Arleth A.J. Ohlstein E.H. Barone F.C. Matrix metalloproteinase expression increases after cerebral focal ischemia in rats: inhibition of matrix metalloproteinase-9 reduces infarct size Stroke 29 1998 1020-1030
    • (1998) Stroke , vol.29 , pp. 1020-1030
    • Romanic, A.M.1    White, R.F.2    Arleth, A.J.3    Ohlstein, E.H.4    Barone, F.C.5
  • 134
    • 0031693557 scopus 로고    scopus 로고
    • Matrix metalloproteinases and TIMPs are associated with blood-brain barrier opening after reperfusion in rat brain
    • Rosenberg G.A. Estrada E.Y. Dencoff J.E. Matrix metalloproteinases and TIMPs are associated with blood-brain barrier opening after reperfusion in rat brain Stroke 29 1998 2189-2195
    • (1998) Stroke , vol.29 , pp. 2189-2195
    • Rosenberg, G.A.1    Estrada, E.Y.2    Dencoff, J.E.3
  • 135
    • 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. Asahi K. Jung J.C. del Zoppo G.J. Fini M.E. Lo E.H. 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 2000 1681-1689
    • (2000) J. Cereb. Blood Flow. Metab. , vol.20 , pp. 1681-1689
    • Asahi, M.1    Asahi, K.2    Jung, J.C.3    del Zoppo, G.J.4    Fini, M.E.5    Lo, E.H.6
  • 136
    • 0035370582 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitor KB-R7785 attenuates brain damage resulting from permanent focal cerebral ischemia in mice
    • Jiang X. Namura S. Nagata I. Matrix metalloproteinase inhibitor KB-R7785 attenuates brain damage resulting from permanent focal cerebral ischemia in mice Neurosci Lett 305 2001 41-44
    • (2001) Neurosci Lett. , vol.305 , pp. 41-44
    • Jiang, X.1    Namura, S.2    Nagata, I.3
  • 137
    • 0035903828 scopus 로고    scopus 로고
    • Matrix metalloproteinase 2 gene knockout has no effect on acute brain injury after focal ischemia
    • Asahi M. Sumii T. Fini M.E. Itohara S. Lo E.H. Matrix metalloproteinase 2 gene knockout has no effect on acute brain injury after focal ischemia Neuroreport 12 2001 3003-3007
    • (2001) Neuroreport , vol.12 , pp. 3003-3007
    • Asahi, M.1    Sumii, T.2    Fini, M.E.3    Itohara, S.4    Lo, E.H.5
  • 139
    • 0029867128 scopus 로고    scopus 로고
    • Matrix metalloproteinases in the normal human central nervous system, microglial nodules and multiple sclerosis lesions
    • Maeda A. Sobel R.A. Matrix metalloproteinases in the normal human central nervous system, microglial nodules and multiple sclerosis lesions J Neuropathol Exp Neurol 55 1996 300-309
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , pp. 300-309
    • Maeda, A.1    Sobel, R.A.2
  • 141
    • 0032126878 scopus 로고    scopus 로고
    • Matrix metalloproteinase expression in an experimentally-induced DTH model of multiple sclerosis in the rat central nervous system (CNS)
    • Anthony D.C. Miller K.M. Fearn S. Townsend M.J. Openakker G. Wells G.M. et al. Matrix metalloproteinase expression in an experimentally-induced DTH model of multiple sclerosis in the rat central nervous system (CNS) J Neuroimmunol 87 1998 62-72
    • (1998) J. Neuroimmunol. , vol.87 , pp. 62-72
    • Anthony, D.C.1    Miller, K.M.2    Fearn, S.3    Townsend, M.J.4    Openakker, G.5    Wells, G.M.6
  • 142
    • 0032828062 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinase-9 and its inhibitors in mononuclear blood cells of patients with multiple sclerosis
    • Lichtinghagen R. Seifert T. Kracke A. Marckmann S. Wurster U. Heidenreich F. Expression of matrix metalloproteinase-9 and its inhibitors in mononuclear blood cells of patients with multiple sclerosis J Neuroimmunol 99 1999 19-26
    • (1999) J. Neuroimmunol. , vol.99 , pp. 19-26
    • Lichtinghagen, R.1    Seifert, T.2    Kracke, A.3    Marckmann, S.4    Wurster, U.5    Heidenreich, F.6
  • 143
    • 0033056463 scopus 로고    scopus 로고
    • The cell biology of leukocyte-mediated proteolysis
    • Owen C.A. Campbell E.J. The cell biology of leukocyte-mediated proteolysis J Leukoc Biol 65 1999 137-150
    • (1999) J. Leukoc. Biol. , vol.65 , pp. 137-150
    • Owen, C.A.1    Campbell, E.J.2
  • 144
    • 0025297592 scopus 로고
    • Production of hemopoietic colony-stimulating factors by astrocytes
    • Malipiero U.V. Frei K. Fontana A. Production of hemopoietic colony-stimulating factors by astrocytes J Immunol 144 1990 3816-3821
    • (1990) J. Immunol. , vol.144 , pp. 3816-3821
    • Malipiero, U.V.1    Frei, K.2    Fontana, A.3
  • 145
    • 0033595590 scopus 로고    scopus 로고
    • Nuclear factor kappa B activity is essential for matrix metalloproteinase-1 and -3 upregulation in rabbit dermal fibroblasts
    • Bond M. Baker A. Newby A.C. Nuclear factor kappa B activity is essential for matrix metalloproteinase-1 and -3 upregulation in rabbit dermal fibroblasts Biochem Biophys Res Commun 264 1999 561-567
    • (1999) Biochem. Biophys. Res. Commun. , vol.264 , pp. 561-567
    • Bond, M.1    Baker, A.2    Newby, A.C.3
  • 147
    • 0026442957 scopus 로고
    • Gelatinase in the cerebrospinal fluid of patients with multiple sclerosis and other inflammatory neurological disorders
    • Gijbels K. Masure S. Carton H. Opdenakker G. Gelatinase in the cerebrospinal fluid of patients with multiple sclerosis and other inflammatory neurological disorders J Neuroimmunol 41 1992 29-34
    • (1992) J. Neuroimmunol. , vol.41 , pp. 29-34
    • Gijbels, K.1    Masure, S.2    Carton, H.3    Opdenakker, G.4
  • 148
    • 0027169231 scopus 로고
    • Leukocyte gelatinase B cleavage releases encephalitogens from human myelin basic protein
    • Proost P. Van Damme J. Opdenakker G. Leukocyte gelatinase B cleavage releases encephalitogens from human myelin basic protein Biochem Biophys Res Commun 192 1993 1175-1181
    • (1993) Biochem. Biophys. Res. Commun. , vol.192 , pp. 1175-1181
    • Proost, P.1    Van Damme, J.2    Opdenakker, G.3
  • 150
    • 0036010527 scopus 로고    scopus 로고
    • Release and activity of matrix metalloproteinase-9 and tissue inhibitor of metalloproteinase-1 by alveolar macrophages from patients with chronic obstructive pulmonary disease
    • Russell R.E. Culpitt S.V. DeMatos C. Donnelly L. Smith M. Wiggins J. et al. Release and activity of matrix metalloproteinase-9 and tissue inhibitor of metalloproteinase-1 by alveolar macrophages from patients with chronic obstructive pulmonary disease Am J Respir Cell Mol Biol 26 2002 602-609
    • (2002) Am. J. Respir. Cell. Mol. Biol. , vol.26 , pp. 602-609
    • Russell, R.E.1    Culpitt, S.V.2    DeMatos, C.3    Donnelly, L.4    Smith, M.5    Wiggins, J.6
  • 151
    • 0023147156 scopus 로고
    • Secretory products of macrophages
    • Nathan C.F. Secretory products of macrophages J Clin Invest 79 1987 319-326
    • (1987) J. Clin. Invest. , vol.79 , pp. 319-326
    • Nathan, C.F.1
  • 152
    • 0025121957 scopus 로고
    • Macrophages and polymorphonuclear neutrophils in lung defence and injury
    • Sibille Y. Reynolds H.Y. Macrophages and polymorphonuclear neutrophils in lung defence and injury Am Rev Respir Dis 141 1990 471-501
    • (1990) Am. Rev. Respir. Dis. , vol.141 , pp. 471-501
    • Sibille, Y.1    Reynolds, H.Y.2
  • 153
    • 0030017051 scopus 로고    scopus 로고
    • Inflammatory mediators, cytokines and adhesion molecules in pulmonary inflammation and injury
    • Lukacs N.W. Ward P.A. Inflammatory mediators, cytokines and adhesion molecules in pulmonary inflammation and injury Adv Immunol 62 1996 257-304
    • (1996) Adv. Immunol. , vol.62 , pp. 257-304
    • Lukacs, N.W.1    Ward, P.A.2
  • 154
    • 0031126851 scopus 로고    scopus 로고
    • Recruitment of inflammatory cells into lungs: Roles of cytokines, adhesion molecules, and complement
    • Ward P.A. Recruitment of inflammatory cells into lungs: roles of cytokines, adhesion molecules, and complement J Lab Clin Med 129 1997 400-404
    • (1997) J. Lab. Clin. Med. , vol.129 , pp. 400-404
    • Ward, P.A.1
  • 157
    • 0027419081 scopus 로고
    • Induction of macrophage metalloproteinases by extracellular matrix: Evidence for enzyme and substrate-specific responses involving prostaglandin-dependent mechanisms
    • Shapiro S.D. Kobayashi D.K. Pentland A.P. Welgus H.G. Induction of macrophage metalloproteinases by extracellular matrix: Evidence for enzyme and substrate-specific responses involving prostaglandin-dependent mechanisms J Biol Chem 268 1993 8170-8175
    • (1993) J. Biol. Chem. , vol.268 , pp. 8170-8175
    • Shapiro, S.D.1    Kobayashi, D.K.2    Pentland, A.P.3    Welgus, H.G.4
  • 158
    • 0024360852 scopus 로고
    • Elastin degradation by human alveolar macrophages. A prominent role of metalloproteinase activity
    • Senior R.M. Connolly N.L. Cury J.D. Welgus H.G. Campbell E.J. Elastin degradation by human alveolar macrophages. A prominent role of metalloproteinase activity Am Rev Respir Dis 139 1989 1251-1256
    • (1989) Am. Rev. Respir. Dis. , vol.139 , pp. 1251-1256
    • Senior, R.M.1    Connolly, N.L.2    Cury, J.D.3    Welgus, H.G.4    Campbell, E.J.5
  • 159
    • 0030823772 scopus 로고    scopus 로고
    • Requirement for macrophage elastase for cigarette smoke-induced emphysema in mice
    • Hautamaki R.D. Kobayashi D.K. Senior R.M. Shapiro S.D. Requirement for macrophage elastase for cigarette smoke-induced emphysema in mice Science 277 1997 2002-2004
    • (1997) Science , vol.277 , pp. 2002-2004
    • Hautamaki, R.D.1    Kobayashi, D.K.2    Senior, R.M.3    Shapiro, S.D.4
  • 162
    • 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 1999 31S-32S
    • (1999) Chest , vol.116
    • Hartzell, W.1    Shapiro, S.D.2
  • 163
    • 0031280307 scopus 로고    scopus 로고
    • Increased release of matrix metalloproteinase-9 in bronchoalveolar lavage fluid and by alveolar macrophages of asthmatics
    • Mautino G. Oliver N. Chanez P. Bousquet J. Capony F. Increased release of matrix metalloproteinase-9 in bronchoalveolar lavage fluid and by alveolar macrophages of asthmatics Am J Respir Cell Mol Biol 17 1997 583-591
    • (1997) Am. J. Respir. Cell. Mol. Biol. , vol.17 , pp. 583-591
    • Mautino, G.1    Oliver, N.2    Chanez, P.3    Bousquet, J.4    Capony, F.5
  • 166
    • 0025304539 scopus 로고
    • Rheumatiod arthritis. Pathophysiology and implication for therapy
    • Harris E.D. Rheumatiod arthritis. Pathophysiology and implication for therapy N Engl J Med 322 1990 1277-1289
    • (1990) N. Engl. J. Med. , vol.322 , pp. 1277-1289
    • Harris, E.D.1
  • 167
    • 0028158689 scopus 로고
    • Synovial tissue macrophages and joint erosion in rheumatoid arthritis
    • Yanni G. Whelan A. Feighery C. Bresnihan B. Synovial tissue macrophages and joint erosion in rheumatoid arthritis Ann Rheum Dis 53 1994 39-44
    • (1994) Ann. Rheum. Dis. , vol.53 , pp. 39-44
    • Yanni, G.1    Whelan, A.2    Feighery, C.3    Bresnihan, B.4
  • 168
    • 0030066502 scopus 로고    scopus 로고
    • Synovial tissue macrophage populations and articular cartilage damage in rheumatoid arthritis
    • Mulherin D. Fitzgerald O. Bresnihan B. Synovial tissue macrophage populations and articular cartilage damage in rheumatoid arthritis Arthritis Rheum 39 1996 115-124
    • (1996) Arthritis Rheum. , vol.39 , pp. 115-124
    • Mulherin, D.1    Fitzgerald, O.2    Bresnihan, B.3
  • 169
    • 0031043106 scopus 로고    scopus 로고
    • Analysis of the synovial cell infiltrate in early rheumatoid synovial tissue in relation to local disease activty
    • Tak P.P. Smeets T.J. Daha M.R. Kluin P.M. Meijers K.A. Brand R. et al. Analysis of the synovial cell infiltrate in early rheumatoid synovial tissue in relation to local disease activty Arthritis Rheum 40 1997 217-225
    • (1997) Arthritis Rheum. , vol.40 , pp. 217-225
    • Tak, P.P.1    Smeets, T.J.2    Daha, M.R.3    Kluin, P.M.4    Meijers, K.A.5    Brand, R.6
  • 170
    • 0029790101 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinase 9 (96-kd gelatinase B) in human rheumatoid arthritis
    • Ahrens D. Koch A.E. Pope R.M. Stein-Picarella M. Niedbala M.J. Expression of matrix metalloproteinase 9 (96-kd gelatinase B) in human rheumatoid arthritis Arthritis Rheum 39 1996 1576-1587
    • (1996) Arthritis Rheum. , vol.39 , pp. 1576-1587
    • Ahrens, D.1    Koch, A.E.2    Pope, R.M.3    Stein-Picarella, M.4    Niedbala, M.J.5
  • 171
    • 1842602667 scopus 로고    scopus 로고
    • Analysis of 16 different matrix metalloproteinases (MMP-1 to MMP-20) in the synovial membrane: Different profiles in trauma and rheumatoid arthritis
    • Konttinen Y.T. Ainola M. Valleala H. Ma J. Ida H. Mandelin J. et al. Analysis of 16 different matrix metalloproteinases (MMP-1 to MMP-20) in the synovial membrane: different profiles in trauma and rheumatoid arthritis Ann Rheum Dis 58 1999 691-697
    • (1999) Ann. Rheum. Dis. , vol.58 , pp. 691-697
    • Konttinen, Y.T.1    Ainola, M.2    Valleala, H.3    Ma, J.4    Ida, H.5    Mandelin, J.6
  • 172
    • 0035029020 scopus 로고    scopus 로고
    • Selective matrix metalloproteinase (MMP) inhibition in rheumatoid arthritis-targetting gelatinase A activation
    • Jackson C. Nguyen M. Arkell J. Sambrook P. Selective matrix metalloproteinase (MMP) inhibition in rheumatoid arthritis-targetting gelatinase A activation Inflamm Res 50 2001 183-186
    • (2001) Inflamm. Res. , vol.50 , pp. 183-186
    • Jackson, C.1    Nguyen, M.2    Arkell, J.3    Sambrook, P.4
  • 173
    • 0032703283 scopus 로고    scopus 로고
    • Angiogenesis and arthritis
    • Walsh D.A. Angiogenesis and arthritis Rheumatol 38 1999 103-112
    • (1999) Rheumatol. , vol.38 , pp. 103-112
    • Walsh, D.A.1
  • 175
    • 0034881924 scopus 로고    scopus 로고
    • Synovial tissue protease gene expression and joint erosion in early rheumatoid arthritis
    • Cunnane G. Fitzgerald O. Hummel K.M. Synovial tissue protease gene expression and joint erosion in early rheumatoid arthritis Arthritis Rheum 44 2001 1744-1753
    • (2001) Arthritis Rheum. , vol.44 , pp. 1744-1753
    • Cunnane, G.1    Fitzgerald, O.2    Hummel, K.M.3
  • 176
    • 0034076456 scopus 로고    scopus 로고
    • Expression and tissue localization of membrane-types 1, 2, and 3 matrix metalloproteinases in rheumatoid synovium
    • Yamanaka H. Makino K. Takizawa M. Nakamura H. Fujimoto N. Moriya H. et al. Expression and tissue localization of membrane-types 1, 2, and 3 matrix metalloproteinases in rheumatoid synovium Lab Invest 80 2000 677-687
    • (2000) Lab. Invest. , vol.80 , pp. 677-687
    • Yamanaka, H.1    Makino, K.2    Takizawa, M.3    Nakamura, H.4    Fujimoto, N.5    Moriya, H.6
  • 177
    • 0035172262 scopus 로고    scopus 로고
    • Stromelysin-1 (MMP-3) in synovial fluid of patients with rheumatoid arthritis has potntial to cleave membrane bound Fas ligand
    • Matsuno H. Yudoh K. Watanabe Y. Nakazawa F. Aono H. Kimura T. Stromelysin-1 (MMP-3) in synovial fluid of patients with rheumatoid arthritis has potntial to cleave membrane bound Fas ligand J Rheumatol 28 2001 22-28
    • (2001) J. Rheumatol. , vol.28 , pp. 22-28
    • Matsuno, H.1    Yudoh, K.2    Watanabe, Y.3    Nakazawa, F.4    Aono, H.5    Kimura, T.6
  • 178
    • 0034041595 scopus 로고    scopus 로고
    • Stimulation of 92-kd gelatinase (matrix metalloproteinase 9) production by interleukin-17 in human monocyte/macrophages: A possible role in rheumatiod arthritis
    • Jovanovic D.V. Martel-Pelletier J. Di Battista J.A. Mineau F. Jolicoeur F.C. Benderdour M. et al. Stimulation of 92-kd gelatinase (matrix metalloproteinase 9) production by interleukin-17 in human monocyte/macrophages: a possible role in rheumatiod arthritis Arthritis Rheum 43 2000 1134-1144
    • (2000) Arthritis Rheum. , vol.43 , pp. 1134-1144
    • Jovanovic, D.V.1    Martel-Pelletier, J.2    Di Battista, J.A.3    Mineau, F.4    Jolicoeur, F.C.5    Benderdour, M.6
  • 179
    • 0034048349 scopus 로고    scopus 로고
    • Anti-cytokine therapy for rheumatoid arthritis
    • Maini R.N. Taylor P.C. Anti-cytokine therapy for rheumatoid arthritis Annu Rev Med 51 2000 207-229
    • (2000) Annu. Rev. Med. , vol.51 , pp. 207-229
    • Maini, R.N.1    Taylor, P.C.2
  • 181
    • 0028180434 scopus 로고
    • Macrophage inflammatory protein-alpha. A novel chemotactic cytokine for macrophages in rheumatoid arthritis
    • Koch A.E. Kunkel S.L. Harlow L.A. Mazarakis D.D. Haines G.K. Burdick M.D. et al. Macrophage inflammatory protein-alpha. A novel chemotactic cytokine for macrophages in rheumatoid arthritis J Clin Invest 93 1994 921-928
    • (1994) J. Clin. Invest. , vol.93 , pp. 921-928
    • Koch, A.E.1    Kunkel, S.L.2    Harlow, L.A.3    Mazarakis, D.D.4    Haines, G.K.5    Burdick, M.D.6
  • 183
    • 0029410736 scopus 로고
    • Localization of macrophage migration inhibitory factor (MIF) to secretory granules within the corticotrophic and thyrotrophic cells of the pituitary gland
    • Nishino T. Bernhagen J. Shiiki H. Calandra T. Dohi K. Bucala R. Localization of macrophage migration inhibitory factor (MIF) to secretory granules within the corticotrophic and thyrotrophic cells of the pituitary gland Mol Med 1 1995 781-788
    • (1995) Mol. Med. , vol.1 , pp. 781-788
    • Nishino, T.1    Bernhagen, J.2    Shiiki, H.3    Calandra, T.4    Dohi, K.5    Bucala, R.6
  • 184
    • 0028305693 scopus 로고
    • The macrophage is an important and previously unrecognized source of macrophage migration inhibitory factor
    • Calandra T. Bernhagen J. Mitchell R.A. Bucala R. The macrophage is an important and previously unrecognized source of macrophage migration inhibitory factor J Exp Med 179 1994 1895-1902
    • (1994) J. Exp. Med. , vol.179 , pp. 1895-1902
    • Calandra, T.1    Bernhagen, J.2    Mitchell, R.A.3    Bucala, R.4
  • 185
    • 0034614492 scopus 로고    scopus 로고
    • Macrophage migration inhibitory factor up-regulates expression of matrix metalloproteinases in synovial fibroblasts of rheumatoid arthritis
    • Onodera S. Kaneda K. Mizue Y. Koyama Y. Fujinaga M. Nishihira J. Macrophage migration inhibitory factor up-regulates expression of matrix metalloproteinases in synovial fibroblasts of rheumatoid arthritis J Biol Chem 275 2000 444-450
    • (2000) J. Biol. Chem. , vol.275 , pp. 444-450
    • Onodera, S.1    Kaneda, K.2    Mizue, Y.3    Koyama, Y.4    Fujinaga, M.5    Nishihira, J.6
  • 186
    • 0037438376 scopus 로고    scopus 로고
    • IL-6 and matrix metalloproteinase-1 are regulated by the cyclin-dependent kinase inhibitor p21 in synovial fibroblasts
    • Perlman H. Bradley K. Liu H. Cole S. Shamieyeh E. Smith R.C. et al. IL-6 and matrix metalloproteinase-1 are regulated by the cyclin-dependent kinase inhibitor p21 in synovial fibroblasts J Immunol 170 2003 838-845
    • (2003) J. Immunol. , vol.170 , pp. 838-845
    • Perlman, H.1    Bradley, K.2    Liu, H.3    Cole, S.4    Shamieyeh, E.5    Smith, R.C.6
  • 187
    • 0028080215 scopus 로고
    • Cytokine networks in solid human tumors: Regulation of angiogenesis
    • Leek R.D. Harris A.L. Lewis C.E. Cytokine networks in solid human tumors: regulation of angiogenesis J Leukoc Biol 56 1994 423-435
    • (1994) J. Leukoc. Biol. , vol.56 , pp. 423-435
    • Leek, R.D.1    Harris, A.L.2    Lewis, C.E.3
  • 189
    • 0035911148 scopus 로고    scopus 로고
    • Stromelysin-1 regulates adipogenesis during mammary gland involution
    • Alexander C.M. Selvarajan S. Mudgett J. Werb Z. Stromelysin-1 regulates adipogenesis during mammary gland involution J Cell Biol 152 2001 693-703
    • (2001) J. Cell. Biol. , vol.152 , pp. 693-703
    • Alexander, C.M.1    Selvarajan, S.2    Mudgett, J.3    Werb, Z.4
  • 191
    • 0031586362 scopus 로고    scopus 로고
    • Fibroblasts can modulate the phenotype of malignant epithelial cells in vitro
    • Atula S. Grenman R. Syrjanen S. Fibroblasts can modulate the phenotype of malignant epithelial cells in vitro Exp Cell Res 235 1997 180-187
    • (1997) Exp. Cell. Res. , vol.235 , pp. 180-187
    • Atula, S.1    Grenman, R.2    Syrjanen, S.3
  • 192
    • 0031947316 scopus 로고    scopus 로고
    • Stromal reaction in cancer tissue: Pathophysiologic significance of the expression of matrix-degrading enzymes in relation to matrix turnover and immune/inflammatory reactions
    • Ohtani H. Stromal reaction in cancer tissue: pathophysiologic significance of the expression of matrix-degrading enzymes in relation to matrix turnover and immune/inflammatory reactions Pathol Int 48 1998 1-9
    • (1998) Pathol. Int. , vol.48 , pp. 1-9
    • Ohtani, H.1
  • 193
    • 0030938479 scopus 로고    scopus 로고
    • Matrix metalloproteinases as stromal effectors of human carcinoma progression: Therapeutic implications
    • Basset P. Okada A. Chenard M.P. Kannan R. Stoll I. Anglard P. et al. Matrix metalloproteinases as stromal effectors of human carcinoma progression: therapeutic implications Matrix Biol 15 1997 535-541
    • (1997) Matrix. Biol. , vol.15 , pp. 535-541
    • Basset, P.1    Okada, A.2    Chenard, M.P.3    Kannan, R.4    Stoll, I.5    Anglard, P.6
  • 194
    • 0040351696 scopus 로고    scopus 로고
    • Regulation of collagenase-3 expression in human breast carcinomas is mediated by stromal-epithelial cell interactions
    • Uria J.A. Stahle-Backdahl M. Seiki M. Fueyo A. Lopez-Otin C. Regulation of collagenase-3 expression in human breast carcinomas is mediated by stromal-epithelial cell interactions Cancer Res 57 1997 4882-4888
    • (1997) Cancer Res. , vol.57 , pp. 4882-4888
    • Uria, J.A.1    Stahle-Backdahl, M.2    Seiki, M.3    Fueyo, A.4    Lopez-Otin, C.5
  • 195
    • 0031719897 scopus 로고    scopus 로고
    • Cancer invasion and tissue remodeling: Common themes in proteolytic matrix degradation
    • Johnsen M. Lund L.R. Romer J. Almholt K. Dano K. Cancer invasion and tissue remodeling: common themes in proteolytic matrix degradation Curr Opin Cell Biol 10 1998 667-671
    • (1998) Curr. Opin. Cell. Biol. , vol.10 , pp. 667-671
    • Johnsen, M.1    Lund, L.R.2    Romer, J.3    Almholt, K.4    Dano, K.5
  • 198
    • 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 2000 163-176
    • (2000) Genes Dev. , vol.14 , pp. 163-176
    • Yu, Q.1    Stamenkovic, I.2
  • 199
    • 0034770605 scopus 로고    scopus 로고
    • Immune-mediated eradication of tumors through the blockade of transforming growth factor-β signaling in T cells
    • Gorelik L. Flavell R.A. Immune-mediated eradication of tumors through the blockade of transforming growth factor-β signaling in T cells Nat Med 7 2001 1118-1122
    • (2001) Nat. Med. , vol.7 , pp. 1118-1122
    • Gorelik, L.1    Flavell, R.A.2
  • 200
    • 0032912952 scopus 로고    scopus 로고
    • Enhanced tumor growth and invasiveness in vivo by a carboxyl-terminal framgent of α1-Proteinase inhibitor generated by matrix metalloproteinases
    • Kataoka H. Uchino H. Iwamura T. Sseiki M. Nabeshima K. Koono M. Enhanced tumor growth and invasiveness in vivo by a carboxyl-terminal framgent of α1-Proteinase inhibitor generated by matrix metalloproteinases Am J Pathol 154 1999 457-468
    • (1999) Am. J. Pathol. , vol.154 , pp. 457-468
    • Kataoka, H.1    Uchino, H.2    Iwamura, T.3    Sseiki, M.4    Nabeshima, K.5    Koono, M.6
  • 201
    • 0022349271 scopus 로고
    • Infiltrating mononuclear cells in human breast carcinoma: Predominance of T4+ monocytic cells in the tumor stroma
    • Göttlinger H.G. Rieber P. Gokel J.M. Lohe K.J. Riethmuller G. Infiltrating mononuclear cells in human breast carcinoma: predominance of T4+ monocytic cells in the tumor stroma Int J Cancer 35 1985 199-205
    • (1985) Int. J. Cancer , vol.35 , pp. 199-205
    • Göttlinger, H.G.1    Rieber, P.2    Gokel, J.M.3    Lohe, K.J.4    Riethmuller, G.5
  • 202
    • 0023836831 scopus 로고
    • Macrophages in human breast disease: A quantitative immunohistochemical study
    • Kelly P.M. Davison R.S. Bliss E. McGee J.O. Macrophages in human breast disease: a quantitative immunohistochemical study Br J Cancer 57 1988 174-177
    • (1988) Br. J. Cancer. , vol.57 , pp. 174-177
    • Kelly, P.M.1    Davison, R.S.2    Bliss, E.3    McGee, J.O.4
  • 203
    • 0029816609 scopus 로고    scopus 로고
    • Association of macrophage infiltration with angiogenesis and prognosis in invasive breast carcinoma
    • Leek R.D. Lewis C.E. Whitehouse R. Greenall M. Clarke J. Harris A.L. Association of macrophage infiltration with angiogenesis and prognosis in invasive breast carcinoma Cancer Res 56 1996 4625-4629
    • (1996) Cancer Res. , vol.56 , pp. 4625-4629
    • Leek, R.D.1    Lewis, C.E.2    Whitehouse, R.3    Greenall, M.4    Clarke, J.5    Harris, A.L.6
  • 204
    • 0028199166 scopus 로고
    • Tumour-associated leukocytes: Friends or foes in breast carcinoma
    • O'Sullivan C. Lewis C.E. Tumour-associated leukocytes: friends or foes in breast carcinoma J Pathol 172 1994 229-235
    • (1994) J. Pathol. , vol.172 , pp. 229-235
    • O'Sullivan, C.1    Lewis, C.E.2
  • 205
    • 0022319412 scopus 로고
    • Macrophage infiltration and tumor progression
    • Normann S.J. Macrophage infiltration and tumor progression Cancer Metastasis Rev 4 1985 277-291
    • (1985) Cancer Metastasis. Rev. , vol.4 , pp. 277-291
    • Normann, S.J.1
  • 206
    • 0030874551 scopus 로고    scopus 로고
    • Expression of tissue inhibitor of metalloproteinases TIMP-2 in human colorectal cancer - A predictor of tumour stage
    • Ring P. Johansson K. Hoyhtya M. Rubin K. Lindmark G. Expression of tissue inhibitor of metalloproteinases TIMP-2 in human colorectal cancer - a predictor of tumour stage Br J Cancer 76 1997 805-811
    • (1997) Br. J. Cancer , vol.76 , pp. 805-811
    • Ring, P.1    Johansson, K.2    Hoyhtya, M.3    Rubin, K.4    Lindmark, G.5
  • 207
    • 0742331383 scopus 로고    scopus 로고
    • Matrix metalloproteinase 2 (MMP-2) immunoreactive protein is associated with poor grade and survival in brain neoplasms
    • Jaalinoja J. Herva R. Korpela M. Hoyhtya M. Turpeenniemi-Hujanen T. Matrix metalloproteinase 2 (MMP-2) immunoreactive protein is associated with poor grade and survival in brain neoplasms J Neurooncol 46 2000 81-90
    • (2000) J. Neurooncol. , vol.46 , pp. 81-90
    • Jaalinoja, J.1    Herva, R.2    Korpela, M.3    Hoyhtya, M.4    Turpeenniemi-Hujanen, T.5
  • 208
    • 0023178579 scopus 로고
    • Immunohistochemical analysis of HLA antigens and mononuclear infiltrates of benign and malignant breast
    • Zuk J.A. Walker R.A. Immunohistochemical analysis of HLA antigens and mononuclear infiltrates of benign and malignant breast J Pathol 152 1987 275-285
    • (1987) J. Pathol. , vol.152 , pp. 275-285
    • Zuk, J.A.1    Walker, R.A.2
  • 210
    • 0025687629 scopus 로고
    • Phenotypic characterization of macrophage subpopulations and localization of factor XIII in the stromal cells of carcinomas
    • Turnock K. Bulmer J.N. Gray C. Phenotypic characterization of macrophage subpopulations and localization of factor XIII in the stromal cells of carcinomas Histochem J 22 1990 661-666
    • (1990) Histochem. J. , vol.22 , pp. 661-666
    • Turnock, K.1    Bulmer, J.N.2    Gray, C.3
  • 213
    • 0025959226 scopus 로고
    • Monocyte chemotactic proteins from human tumor cells
    • Graves D.T. Valent A.J. Monocyte chemotactic proteins from human tumor cells Biochem Pharmacol 41 1991 333-337
    • (1991) Biochem. Pharmacol. , vol.41 , pp. 333-337
    • Graves, D.T.1    Valent, A.J.2
  • 214
    • 0026596656 scopus 로고
    • Regulation of leukocyte binding protein to endothelial tissues by tumor-derived granulocyte macrophage colony-stimulating factor (GM-CSF)
    • Fu Y.X. Cai J.P. Chin Y.H. Watson G.A. Lopez D.M. Regulation of leukocyte binding protein to endothelial tissues by tumor-derived granulocyte macrophage colony-stimulating factor (GM-CSF) Int J Cancer 50 1992 585-588
    • (1992) Int. J. Cancer , vol.50 , pp. 585-588
    • Fu, Y.X.1    Cai, J.P.2    Chin, Y.H.3    Watson, G.A.4    Lopez, D.M.5
  • 215
    • 0029134905 scopus 로고
    • Incidence of de-novo breast cancer in women chronically immunosuppressed after organ transplantation
    • Stewart T. Tsai S.C. Grayson H. Henderson R. Opelz G. Incidence of de-novo breast cancer in women chronically immunosuppressed after organ transplantation Lancet 346 1995 796-798
    • (1995) Lancet , vol.346 , pp. 796-798
    • Stewart, T.1    Tsai, S.C.2    Grayson, H.3    Henderson, R.4    Opelz, G.5
  • 217
    • 0028265599 scopus 로고
    • Production of angiogenic activity by human monocytes requires an L-arginine/nitric oxide-synthase-dependent effector mechanism
    • Leibovich S.J. Polverini P.J. Fong T.W. Harlow L.A. Koch A.E. Production of angiogenic activity by human monocytes requires an L-arginine/nitric oxide-synthase-dependent effector mechanism Proc Natl Acad Sci USA 91 1994 4190-4194
    • (1994) Proc. Natl. Acad Sci. USA , vol.91 , pp. 4190-4194
    • Leibovich, S.J.1    Polverini, P.J.2    Fong, T.W.3    Harlow, L.A.4    Koch, A.E.5
  • 220
    • 0031454617 scopus 로고    scopus 로고
    • Endostatin: An endogenous inhibitor of angiogenesis and tumor growth
    • O'Reilly M.S. Boehm T. Shing Y. Fukai N. Vasios G. Lane W.S. et al. Endostatin: an endogenous inhibitor of angiogenesis and tumor growth Cell 88 1997 277-285
    • (1997) Cell , vol.88 , pp. 277-285
    • O'Reilly, M.S.1    Boehm, T.2    Shing, Y.3    Fukai, N.4    Vasios, G.5    Lane, W.S.6
  • 221
    • 0030998660 scopus 로고    scopus 로고
    • Macrophage-derived metalloproteinase is responsible for the generation of angiostatin in Lewis lung carcinoma
    • Dong Z. Kumar R. Yang X. Fidler I.J. Macrophage-derived metalloproteinase is responsible for the generation of angiostatin in Lewis lung carcinoma Cell 88 1997 801-810
    • (1997) Cell , vol.88 , pp. 801-810
    • Dong, Z.1    Kumar, R.2    Yang, X.3    Fidler, I.J.4
  • 222
    • 0032492713 scopus 로고    scopus 로고
    • Generation of an angiostatin-like fragment from plasminogen by stromelysin-1 (MMP-3)
    • Lijnen H.R. Ugwu F. Bini A. Collen D. Generation of an angiostatin-like fragment from plasminogen by stromelysin-1 (MMP-3) Biochemistry 37 1998 4699-4702
    • (1998) Biochemistry , vol.37 , pp. 4699-4702
    • Lijnen, H.R.1    Ugwu, F.2    Bini, A.3    Collen, D.4
  • 223
    • 8044250278 scopus 로고    scopus 로고
    • Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha
    • Moss M.L. Jin S.L. Milla M.E. Bickett D.M. Burkhart W. Carter H.L. et al. Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha Nature 385 1997 733-736
    • (1997) Nature , vol.385 , pp. 733-736
    • Moss, M.L.1    Jin, S.L.2    Milla, M.E.3    Bickett, D.M.4    Burkhart, W.5    Carter, H.L.6
  • 224
    • 0025687446 scopus 로고
    • Solid tumours and wounds: Transformed cells misunderstood as injured tissue?
    • Whalen G.F. Solid tumours and wounds: transformed cells misunderstood as injured tissue? Lancet 336 1990 1489-1492
    • (1990) Lancet , vol.336 , pp. 1489-1492
    • Whalen, G.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.