메뉴 건너뛰기




Volumn 94, Issue 2, 2013, Pages 237-246

Membrane-type matrix metalloproteinases: Key mediators of leukocyte function

Author keywords

Extracellular matrix; Immune system cells; Inflammation; Migration; Proteases

Indexed keywords

GELATINASE A; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE 14; MATRIX METALLOPROTEINASE 15; MATRIX METALLOPROTEINASE 16; MATRIX METALLOPROTEINASE 17; RANTES; TISSUE INHIBITOR OF METALLOPROTEINASE 2; TISSUE INHIBITOR OF METALLOPROTEINASE 3; TISSUE INHIBITOR OF METALLOPROTEINASE 4;

EID: 84880967566     PISSN: 07415400     EISSN: 19383673     Source Type: Journal    
DOI: 10.1189/jlb.0612267     Document Type: Review
Times cited : (39)

References (98)
  • 2
    • 43049139847 scopus 로고    scopus 로고
    • Leukocyte cell surface proteinases: Regulation of expression, functions, and mechanisms of surface localization
    • Owen, C. A. (2008) Leukocyte cell surface proteinases: regulation of expression, functions, and mechanisms of surface localization. Int. J. Biochem. Cell Biol. 40, 1246-1272.
    • (2008) Int. J. Biochem. Cell Biol , vol.40 , pp. 1246-1272
    • Owen, C.A.1
  • 3
    • 0033056463 scopus 로고    scopus 로고
    • The cell biology of leukocyte-mediated proteolysis
    • Owen, C. A., Campbell, E. J. (1999) The cell biology of leukocyte-mediated proteolysis. J. Leukoc. Biol. 65, 137-150.
    • (1999) J. Leukoc. Biol , vol.65 , pp. 137-150
    • Owen, C.A.1    Campbell, E.J.2
  • 5
    • 0141782259 scopus 로고    scopus 로고
    • Gelatinase B/MMP-9 and neutrophil collage-nase/MMP-8 process the chemokines human GCP-2/CXCL6, ENA-78/ CXCL5 and mouse GCP-2/LIX and modulate their physiological activities
    • Van Den Steen, P. E., Wuyts, A., Husson, S. J., Proost, P., Van Damme, J., Opdenakker, G. (2003) Gelatinase B/MMP-9 and neutrophil collage-nase/MMP-8 process the chemokines human GCP-2/CXCL6, ENA-78/ CXCL5 and mouse GCP-2/LIX and modulate their physiological activities. Eur. J. Biochem. 270, 3739-3749.
    • (2003) Eur. J. Biochem , vol.270 , pp. 3739-3749
    • Van den, S.P.E.1    Wuyts, A.2    Husson, S.J.3    Proost, P.4    Van Damme, J.5    Opdenakker, G.6
  • 6
    • 65549113428 scopus 로고    scopus 로고
    • Macrophage met-alloelastase (MMP-12) as a target for inflammatory respiratory diseases
    • Lagente, V., Le Quement, C., Boichot, E. (2009) Macrophage met-alloelastase (MMP-12) as a target for inflammatory respiratory diseases. Expert Opin. Ther. Targets 13, 287-295.
    • (2009) Expert Opin. Ther. Targets , vol.13 , pp. 287-295
    • Lagente, V.1    Le, Q.C.2    Boichot, E.3
  • 7
    • 84855599269 scopus 로고    scopus 로고
    • Matrix metalloprotei-nases contribute to neuronal dysfunction in animal models of drug dependence, Alzheimer's disease, and epilepsy
    • Mizoguchi, H., Yamada, K., Nabeshima, T. (2011) Matrix metalloprotei-nases contribute to neuronal dysfunction in animal models of drug dependence, Alzheimer's disease, and epilepsy. Biochem. Res. Int. 2011, 681385.
    • (2011) Biochem. Res. Int , vol.2011 , pp. 681385
    • Mizoguchi, H.1    Yamada, K.2    Nabeshima, T.3
  • 8
    • 83555168313 scopus 로고    scopus 로고
    • An alternate perspective on the roles of TIMPs and MMPs in pathology
    • Moore, C. S., Crocker, S. J. (2012) An alternate perspective on the roles of TIMPs and MMPs in pathology. Am. J. Pathol. 180, 12-16.
    • (2012) Am. J. Pathol , vol.180 , pp. 12-16
    • Moore, C.S.1    Crocker, S.J.2
  • 9
    • 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. (1990) 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) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5578-5582
    • Van Wart, H.E.1    Birkedal-Hansen, H.2
  • 10
    • 77149164774 scopus 로고    scopus 로고
    • Matrix metallopro-teinases: What do they not do? New substrates and biological roles identified by murine models and proteomics
    • Rodriguez, D., Morrison, C. J., Overall, C. M. (2010) Matrix metallopro-teinases: what do they not do? New substrates and biological roles identified by murine models and proteomics. Biochim. Biophys. Acta 1803, 39-54.
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 39-54
    • Rodriguez, D.1    Morrison, C.J.2    Overall, C.M.3
  • 11
    • 77950931419 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Regulators of the tumor microenvironment
    • Kessenbrock, K., Plaks, V., Werb, Z. (2010) Matrix metalloproteinases: regulators of the tumor microenvironment. Cell 141, 52-67.
    • (2010) Cell , vol.141 , pp. 52-67
    • Kessenbrock, K.1    Plaks, V.2    Werb, Z.3
  • 13
    • 34447522132 scopus 로고    scopus 로고
    • Src-dependent phosphorylation of membrane type I matrix metalloproteinase on cytoplasmic tyrosine 573: Role in endothelial and tumor cell migration
    • Nyalendo, C., Michaud, M., Beaulieu, E., Roghi, C., Murphy, G., Gin-gras, D., Beliveau, R. (2007) Src-dependent phosphorylation of membrane type I matrix metalloproteinase on cytoplasmic tyrosine 573: role in endothelial and tumor cell migration. J. Biol. Chem. 282, 15690-15699.
    • (2007) J. Biol. Chem , vol.282 , pp. 15690-15699
    • Nyalendo, C.1    Michaud, M.2    Beaulieu, E.3    Roghi, C.4    Murphy, G.5    Gin-Gras, D.6    Beliveau, R.7
  • 14
    • 0035854654 scopus 로고    scopus 로고
    • Mutation analysis of membrane type-1 matrix metalloproteinase (MT1-MMP). The role of the cytoplasmic tail Cys(574), the active site Glu(240), and furin cleavage motifs in oligomerization, processing, and self-proteolysis of MT1-MMP expressed in breast carcinoma cells
    • Rozanov, D. V., Deryugina, E. I., Ratnikov, B. I., Monosov, E. Z., March-enko, G. N., Quigley, J. P., Strongin, A. Y. (2001) Mutation analysis of membrane type-1 matrix metalloproteinase (MT1-MMP). The role of the cytoplasmic tail Cys(574), the active site Glu(240), and furin cleavage motifs in oligomerization, processing, and self-proteolysis of MT1-MMP expressed in breast carcinoma cells. J. Biol. Chem. 276, 25705-25714.
    • (2001) J. Biol. Chem , vol.276 , pp. 25705-25714
    • Rozanov, D.V.1    Deryugina, E.I.2    Ratnikov, B.I.3    Monosov, E.Z.4    March-Enko, G.N.5    Quigley, J.P.6    Strongin, A.Y.7
  • 15
    • 34547606200 scopus 로고    scopus 로고
    • MMP25 (MT6-MMP) is highly expressed in human colon cancer, promotes tumor growth, and exhibits unique biochemical properties
    • Sun, Q., Weber, C. R., Sohail, A., Bernardo, M. M., Toth, M., Zhao, H., Turner, J. R., Fridman, R. (2007) MMP25 (MT6-MMP) is highly expressed in human colon cancer, promotes tumor growth, and exhibits unique biochemical properties. J. Biol. Chem. 282, 21998-22010.
    • (2007) J. Biol. Chem , vol.282 , pp. 21998-22010
    • Sun, Q.1    Weber, C.R.2    Sohail, A.3    Bernardo, M.M.4    Toth, M.5    Zhao, H.6    Turner, J.R.7    Fridman, R.8
  • 16
    • 77955039982 scopus 로고    scopus 로고
    • MT6-MMP is present in lipid rafts and faces inward in living human PMNs but translocates to the cell surface during neutrophil apo-ptosis
    • Fortin, C. F., Sohail, A., Sun, Q., McDonald, P. P., Fridman, R., Fulop, T. (2010) MT6-MMP is present in lipid rafts and faces inward in living human PMNs but translocates to the cell surface during neutrophil apo-ptosis. Int. Immunol. 22, 637-649.
    • (2010) Int. Immunol , vol.22 , pp. 637-649
    • Fortin, C.F.1    Sohail, A.2    Sun, Q.3    McDonald, P.P.4    Fridman, R.5    Fulop, T.6
  • 17
    • 80053033214 scopus 로고    scopus 로고
    • Characterization of the dimerization interface of membrane type 4 (MT4)-matrix metalloproteinase
    • Sohail, A., Marco, M., Zhao, H., Shi, Q., Merriman, S., Mobashery, S., Fridman, R. (2011) Characterization of the dimerization interface of membrane type 4 (MT4)-matrix metalloproteinase. J. Biol. Chem. 286, 33178-33189.
    • (2011) J. Biol. Chem , vol.286 , pp. 33178-33189
    • Sohail, A.1    Marco, M.2    Zhao, H.3    Shi, Q.4    Merriman, S.5    Mobashery, S.6    Fridman, R.7
  • 18
    • 0032722873 scopus 로고    scopus 로고
    • Catalytic activities and substrate specificity of the human membrane type 4 matrix metallo-proteinase catalytic domain
    • Wang, Y., Johnson, A. R., Ye, Q. Z., Dyer, R. D. (1999) Catalytic activities and substrate specificity of the human membrane type 4 matrix metallo-proteinase catalytic domain. J. Biol. Chem. 274, 33043-33049.
    • (1999) J. Biol. Chem , vol.274 , pp. 33043-33049
    • Wang, Y.1    Johnson, A.R.2    Ye, Q.Z.3    Dyer, R.D.4
  • 19
    • 0034640282 scopus 로고    scopus 로고
    • Membrane type4 matrix metalloproteinase (MMP17) has tumor necrosis factor-a convertase activity but does not activate pro-MMP2
    • English, W. R., Puente, X. S., Freije, J. M., Knauper, V., Amour, A., Merryweather, A., Lopez-Otin, C., Murphy, G. (2000) Membrane type4 matrix metalloproteinase (MMP17) has tumor necrosis factor-a convertase activity but does not activate pro-MMP2. J. Biol. Chem. 275, 14046-14055.
    • (2000) J. Biol. Chem , vol.275 , pp. 14046-14055
    • English, W.R.1    Puente, X.S.2    Freije, J.M.3    Knauper, V.4    Amour, A.5    Merryweather, A.6    Lopez-Otin, C.7    Murphy, G.8
  • 20
    • 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., Collier, I., Bannikov, G., Marmer, B. L., Grant, G. A., Goldberg, G. I. (1995) 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) J. Biol. Chem , vol.270 , pp. 5331-5338
    • Strongin, A.Y.1    Collier, I.2    Bannikov, G.3    Marmer, B.L.4    Grant, G.A.5    Goldberg, G.I.6
  • 21
    • 10744221757 scopus 로고    scopus 로고
    • Differential inhibition of membrane type 3 (MT3)-matrix metalloproteinase (MMP) and MT1-MMP by tissue inhibitor of metalloproteinase (TIMP)-2 and TIMP-3 regulates pro-MMP-2 activation
    • Zhao, H., Bernardo, M. M., Osenkowski, P., Sohail, A., Pei, D., Nagase, H., Kashiwagi, M., Soloway, P. D., DeClerck, Y. A, Fridman, R. (2004) Differential inhibition of membrane type 3 (MT3)-matrix metalloproteinase (MMP) and MT1-MMP by tissue inhibitor of metalloproteinase (TIMP)-2 and TIMP-3 regulates pro-MMP-2 activation. J. Biol. Chem. 279, 8592-8601.
    • (2004) J. Biol. Chem , vol.279 , pp. 8592-8601
    • Zhao, H.1    Bernardo, M.M.2    Osenkowski, P.3    Sohail, A.4    Pei, D.5    Nagase, H.6    Kashiwagi, M.7    Soloway, P.D.8    Declerck, Y.A.9    Fridman, R.10
  • 22
    • 2642546699 scopus 로고    scopus 로고
    • Processing, shedding, and endocytosis of membrane type 1-matrix metalloproteinase (MT1-MMP)
    • Osenkowski, P., Toth, M., Fridman, R. (2004) Processing, shedding, and endocytosis of membrane type 1-matrix metalloproteinase (MT1-MMP). J. Cell. Physiol. 200, 2-10.
    • (2004) J. Cell. Physiol , vol.200 , pp. 2-10
    • Osenkowski, P.1    Toth, M.2    Fridman, R.3
  • 23
    • 34250312341 scopus 로고    scopus 로고
    • The biochemical, biological, and pathological kaleidoscope of cell surface substrates processed by matrix metalloproteinases
    • Cauwe, B., Van den Steen, P. E., Opdenakker, G. (2007) The biochemical, biological, and pathological kaleidoscope of cell surface substrates processed by matrix metalloproteinases. Crit. Rev. Biochem. Mol. Biol. 42, 113-185.
    • (2007) Crit. Rev. Biochem. Mol. Biol , vol.42 , pp. 113-185
    • Cauwe, B.1    Van den, S.P.E.2    Opdenakker, G.3
  • 24
    • 3543134126 scopus 로고    scopus 로고
    • Matrix metallo-proteinases as modulators of inflammation and innate immunity
    • Parks, W. C, Wilson, C. L., Lopez-Boado, Y S. (2004) Matrix metallo-proteinases as modulators of inflammation and innate immunity. Nat. Rev. Immunol. 4, 617-629.
    • (2004) Nat. Rev. Immunol , vol.4 , pp. 617-629
    • Parks, W.C.1    Wilson, C.L.2    Lopez-Boado, Y.S.3
  • 25
    • 37049015152 scopus 로고    scopus 로고
    • Membrane type 1-matrix metalloproteinase: Substrate diversity in pericellular proteolysis
    • Barbolina, M. V., Stack, M. S. (2008) Membrane type 1-matrix metalloproteinase: substrate diversity in pericellular proteolysis. Semin. Cell. Dev. Biol. 19, 24-33.
    • (2008) Semin. Cell. Dev. Biol , vol.19 , pp. 24-33
    • Barbolina, M.V.1    Stack, M.S.2
  • 26
    • 0035936899 scopus 로고    scopus 로고
    • Catalytic activities of membrane-type 6 matrix metalloproteinase (MMP25)
    • English, W. R, Velasco, G., Stracke, J. O., Knauper, V., Murphy, G (2001) Catalytic activities of membrane-type 6 matrix metalloproteinase (MMP25). FEBS Lett. 491, 137-142.
    • (2001) FEBS Lett , vol.491 , pp. 137-142
    • English, W.R.1    Velasco, G.2    Stracke, J.O.3    Knauper, V.4    Murphy, G.5
  • 27
    • 2342460878 scopus 로고    scopus 로고
    • Membrane protease proteomics: Isotope-coded 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. (2004) Membrane protease proteomics: isotope-coded affinity tag MS identification of undescribed MT1-matrix metalloproteinase substrates. Proc. Natl. Acad. Sci. USA 101, 6917-6922.
    • (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
  • 28
    • 84859738660 scopus 로고    scopus 로고
    • Biochemical characterization and N-terminomics analysis of leu-kolysin, the membrane-type 6 matrix metalloprotease (MMP25): Chemo-kine and vimentin cleavages enhance cell migration and macrophage phagocytic activities
    • Starr, A. E., Bellac, C. L., Dufour, A, Goebeler, V., Overall, C. M. (2012) Biochemical characterization and N-terminomics analysis of leu-kolysin, the membrane-type 6 matrix metalloprotease (MMP25): chemo-kine and vimentin cleavages enhance cell migration and macrophage phagocytic activities. J. Biol. Chem. 287, 13382-13395.
    • (2012) J. Biol. Chem , vol.287 , pp. 13382-13395
    • Starr, A.E.1    Bellac, C.L.2    Dufour, A.3    Goebeler, V.4    Overall, C.M.5
  • 29
    • 77956564117 scopus 로고    scopus 로고
    • KIF5B and KIF3A/KIF3B kinesins drive MT1-MMP surface exposure, CD44 shedding, and extracellular matrix degradation in primary macrophages
    • Wiesner, C, Faix, J., Himmel, M., Bentzien, F., Linder, S. (2010) KIF5B and KIF3A/KIF3B kinesins drive MT1-MMP surface exposure, CD44 shedding, and extracellular matrix degradation in primary macrophages. Blood 116, 1559-1569.
    • (2010) Blood , vol.116 , pp. 1559-1569
    • Wiesner, C.1    Faix, J.2    Himmel, M.3    Bentzien, F.4    Linder, S.5
  • 30
    • 79151479015 scopus 로고    scopus 로고
    • The non-redundant role of N-WASP in podosome-mediated matrix degradation in macrophages
    • Nusblat, L. M., Dovas, A, Cox, D. (2011) The non-redundant role of N-WASP in podosome-mediated matrix degradation in macrophages. Eur. J. Cell Biol. 90, 205-212.
    • (2011) Eur. J. Cell Biol , vol.90 , pp. 205-212
    • Nusblat, L.M.1    Dovas, A.2    Cox, D.3
  • 31
    • 84867398827 scopus 로고    scopus 로고
    • ATAT1/MEC-17 acetyltransferase and HDAC6 deacetylase control a balance of acetylation of a-tubulin and cortactin and regulate MT1-MMP trafficking and breast tumor cell invasion
    • Castro-Castro, A, Janke, C, Montagnac, G., Paul-Gilloteaux, P., Chavrier, P. (2012) ATAT1/MEC-17 acetyltransferase and HDAC6 deacetylase control a balance of acetylation of a-tubulin and cortactin and regulate MT1-MMP trafficking and breast tumor cell invasion. Eur. J. Cell Biol. 91, 950-960.
    • (2012) Eur. J. Cell Biol , vol.91 , pp. 950-960
    • Castro-Castro, A.1    Janke, C.2    Montagnac, G.3    Paul-Gilloteaux, P.4    Chavrier, P.5
  • 32
    • 70350417461 scopus 로고    scopus 로고
    • Matrix invasion by tumour cells: A focus on MT1-MMP trafficking to invadopodia
    • Poincloux, R., Lizarraga, F., Chavrier, P. (2009) Matrix invasion by tumour cells: a focus on MT1-MMP trafficking to invadopodia. J. Cell Sci. 122, 3015-3024.
    • (2009) J. Cell Sci , vol.122 , pp. 3015-3024
    • Poincloux, R.1    Lizarraga, F.2    Chavrier, P.3
  • 33
    • 43049104500 scopus 로고    scopus 로고
    • Fragments of extracellular matrix as mediators of inflammation
    • Adair-Kirk, T. L., Senior, R M. (2008) Fragments of extracellular matrix as mediators of inflammation. Int. J. Biochem. Cell Biol. 40, 1101-1110.
    • (2008) Int. J. Biochem. Cell Biol , vol.40 , pp. 1101-1110
    • Adair-Kirk, T.L.1    Senior, R.M.2
  • 34
    • 65649095931 scopus 로고    scopus 로고
    • Multiple roles of the extracellular matrix in inflammation
    • Korpos, E., Wu, C, Sorokin, L. (2009) Multiple roles of the extracellular matrix in inflammation. Curr. Pharm. Des. 15, 1349-1357.
    • (2009) Curr. Pharm. Des , vol.15 , pp. 1349-1357
    • Korpos, E.1    Wu, C.2    Sorokin, L.3
  • 35
    • 33746928340 scopus 로고    scopus 로고
    • Emerging roles for ect-odomain shedding in the regulation of inflammatory responses
    • Garton, K. J., Gough, P. J., Raines, E. W. (2006) Emerging roles for ect-odomain shedding in the regulation of inflammatory responses. J. Leu-koc. Biol. 79, 1105-1116.
    • (2006) J. Leu-koc. Biol , vol.79 , pp. 1105-1116
    • Garton, K.J.1    Gough, P.J.2    Raines, E.W.3
  • 36
    • 0035947766 scopus 로고    scopus 로고
    • Membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration
    • Kajita, M., Itoh, Y, Chiba, T., Mori, H., Okada, A, Kinoh, H., Seiki, M. (2001) Membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration. J. Cell Biol. 153, 893-904.
    • (2001) J. Cell Biol , vol.153 , pp. 893-904
    • Kajita, M.1    Itoh, Y.2    Chiba, T.3    Mori, H.4    Okada, A.5    Kinoh, H.6    Seiki, M.7
  • 37
    • 34548316487 scopus 로고    scopus 로고
    • Membrane-type 1-matrix metalloproteinase regulates intracellular adhesion molecule-1 (ICAM-1)-mediated monocyte transmigration
    • Sithu, S. D., English, W. R, Olson, P., Krubasik, D., Baker, A. H., Murphy, G., D'Souza, S. E. (2007) Membrane-type 1-matrix metalloproteinase regulates intracellular adhesion molecule-1 (ICAM-1)-mediated monocyte transmigration. J. Biol. Chem. 282, 25010-25019.
    • (2007) J. Biol. Chem , vol.282 , pp. 25010-25019
    • Sithu, S.D.1    English, W.R.2    Olson, P.3    Krubasik, D.4    Baker, A.H.5    Murphy, G.6    D'Souza, S.E.7
  • 38
    • 0142103466 scopus 로고    scopus 로고
    • Cleavage of syndecan-1 by membrane type matrix metalloproteinase-1 stimulates cell migration
    • Endo, K, Takino, T., Miyamori, H., Kinsen, H., Yoshizaki, T., Furukawa, M., Sato, H. (2003) Cleavage of syndecan-1 by membrane type matrix metalloproteinase-1 stimulates cell migration. J. Biol. Chem. 278, 40764-40770.
    • (2003) J. Biol. Chem , vol.278 , pp. 40764-40770
    • Endo, K.1    Takino, T.2    Miyamori, H.3    Kinsen, H.4    Yoshizaki, T.5    Furukawa, M.6    Sato, H.7
  • 39
    • 25844523991 scopus 로고    scopus 로고
    • Cell-surface enzymes in control of leukocyte trafficking
    • Salmi, M., Jalkanen, S. (2005) Cell-surface enzymes in control of leukocyte trafficking. Nat. Rev. Immunol. 5, 760-771.
    • (2005) Nat. Rev. Immunol , vol.5 , pp. 760-771
    • Salmi, M.1    Jalkanen, S.2
  • 40
    • 61349189762 scopus 로고    scopus 로고
    • Matrix metalloproteinases, T cell homing and /3-cell mass in type 1 diabetes
    • Savinov, A. Y, Strongin, A. Y (2009) Matrix metalloproteinases, T cell homing and /3-cell mass in type 1 diabetes. Vitam. Horm. 80, 541-562.
    • (2009) Vitam. Horm , vol.80 , pp. 541-562
    • Savinov, A.Y.1    Strongin, A.Y.2
  • 41
    • 56449115869 scopus 로고    scopus 로고
    • Membrane type 1 matrix metalloproteinase-mediated stromal syndecan-1 shedding stimulates breast carcinoma cell proliferation
    • Su, G., Blaine, S. A, Qiao, D., Friedl, A. (2008) Membrane type 1 matrix metalloproteinase-mediated stromal syndecan-1 shedding stimulates breast carcinoma cell proliferation. Cancer Res. 68, 9558-9565.
    • (2008) Cancer Res , vol.68 , pp. 9558-9565
    • Su, G.1    Blaine, S.A.2    Qiao, D.3    Friedl, A.4
  • 42
    • 0035947675 scopus 로고    scopus 로고
    • Matrix-dependent proteolysis of surface transglutaminase by membrane-type metalloproteinase regulates cancer cell adhesion and locomotion
    • Belkin, A. M., Akimov, S. S., Zaritskaya, L. S., Ratnikov, B. I., Deryugina, E. I., Strongin, A. Y (2001) Matrix-dependent proteolysis of surface transglutaminase by membrane-type metalloproteinase regulates cancer cell adhesion and locomotion. J. Biol. Chem. 276, 18415-18422.
    • (2001) J. Biol. Chem , vol.276 , pp. 18415-18422
    • Belkin, A.M.1    Akimov, S.S.2    Zaritskaya, L.S.3    Ratnikov, B.I.4    Deryugina, E.I.5    Strongin, A.Y.6
  • 43
    • 84857287661 scopus 로고    scopus 로고
    • Biochemical analysis of matrix metalloproteinase activation of chemokines CCL15 and CCL23 and increased glycosaminoglycan binding of CCL16
    • Starr, A. E., Dufour, A, Maier, J., Overall, C. M. (2012) Biochemical analysis of matrix metalloproteinase activation of chemokines CCL15 and CCL23 and increased glycosaminoglycan binding of CCL16. J. Biol. Chem. 287, 5848-5860.
    • (2012) J. Biol. Chem , vol.287 , pp. 5848-5860
    • Starr, A.E.1    Dufour, A.2    Maier, J.3    Overall, C.M.4
  • 44
    • 0034667542 scopus 로고    scopus 로고
    • Neutrophil gelatinase B potentiates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAP-III, PF-4, and GRO-a and leaves RANTES and MCP-2 intact
    • Van den Steen, P. E., Proost, P., Wuyts, A., Van Damme, J., Opdenak-ker, G. (2000) Neutrophil gelatinase B potentiates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAP-III, PF-4, and GRO-a and leaves RANTES and MCP-2 intact. Blood 96, 2673-2681.
    • (2000) Blood , vol.96 , pp. 2673-2681
    • Van den, S.P.E.1    Proost, P.2    Wuyts, A.3    van Damme, J.4    Opdenak-Ker, G.5
  • 47
    • 0037114003 scopus 로고    scopus 로고
    • Matrix metalloproteinase-depen-dent activation of latent transforming growth factor-/3 controls the conversion of osteoblasts into osteocytes by blocking osteoblast apoptosis
    • Karsdal, M. A, Larsen, L., Engsig, M. T., Lou, H., Ferreras, M., Lochter, A, Delaisse, J. M., Foged, N. T. (2002) Matrix metalloproteinase-depen-dent activation of latent transforming growth factor-/3 controls the conversion of osteoblasts into osteocytes by blocking osteoblast apoptosis. J. Biol. Chem. 277, 44061-44067.
    • (2002) J. Biol. Chem , vol.277 , pp. 44061-44067
    • Karsdal, M.A.1    Larsen, L.2    Engsig, M.T.3    Lou, H.4    Ferreras, M.5    Lochter, A.6    Delaisse, J.M.7    Foged, N.T.8
  • 48
    • 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. (2002) Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties in vivo. Blood 100, 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
  • 50
    • 6844250127 scopus 로고    scopus 로고
    • Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases
    • D'Ortho, M. P., Will, H., Atkinson, S., Butler, G., Messent, A, Gavrilovic, J., Smith, B., Timpl, R, Zardi, L., Murphy, G. (1997) Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases. Eur. J. Biochem. 250, 751-757.
    • (1997) Eur. J. Biochem , vol.250 , pp. 751-757
    • D'Ortho, M.P.1    Will, H.2    Atkinson, S.3    Butler, G.4    Messent, A.5    Gavrilovic, J.6    Smith, B.7    Timpl, R.8    Zardi, L.9    Murphy, G.10
  • 51
    • 34548403035 scopus 로고    scopus 로고
    • Establishment of an MT4-MMP-deficient mouse strain representing an efficient tracking system for MT4-MMP/MMP-17 expression in vivo using /3-galactosidase
    • Rikimaru, A, Komori, K, Sakamoto, T., Ichise, H., Yoshida, N., Yana, I., Seiki, M. (2007) Establishment of an MT4-MMP-deficient mouse strain representing an efficient tracking system for MT4-MMP/MMP-17 expression in vivo using /3-galactosidase. Genes Cells 12, 1091-1100.
    • (2007) Genes Cells , vol.12 , pp. 1091-1100
    • Rikimaru, A.1    Komori, K.2    Sakamoto, T.3    Ichise, H.4    Yoshida, N.5    Yana, I.6    Seiki, M.7
  • 52
    • 2442630306 scopus 로고    scopus 로고
    • Rapid inactivation of a-1-proteinase inhibitor by neutrophil specific leukolysin/membrane-type matrix metalloproteinase 6
    • Nie, J., Pei, D. (2004) Rapid inactivation of a-1-proteinase inhibitor by neutrophil specific leukolysin/membrane-type matrix metalloproteinase 6. Exp. Cell. Res. 296, 145-150.
    • (2004) Exp. Cell. Res , vol.296 , pp. 145-150
    • Nie, J.1    Pei, D.2
  • 53
    • 0344443218 scopus 로고    scopus 로고
    • Analyses of all matrix metalloproteinase members in leukocytes emphasize monocytes as major inflammatory mediators in multiple sclerosis
    • Bar-Or, A, Nuttall, R K, Duddy, M., Alter, A, Kim, H. J., Ifergan, I., Pennington, C. J., Bourgoin, P., Edwards, D. R., Yong, V. W. (2003) Analyses of all matrix metalloproteinase members in leukocytes emphasize monocytes as major inflammatory mediators in multiple sclerosis. Brain 126, 2738-2749.
    • (2003) Brain , vol.126 , pp. 2738-2749
    • Bar-Or, A.1    Nuttall, R.K.2    Duddy, M.3    Alter, A.4    Kim, H.J.5    Ifergan, I.6    Pennington, C.J.7    Bourgoin, P.8    Edwards, D.R.9    Yong, V.W.10
  • 55
    • 84864535402 scopus 로고    scopus 로고
    • Classical macrophage activation up-regulates several matrix metalloproteinases through mitogen activated protein kinases and nuclear factor-KB
    • Huang, W. C, Sala-Newby, G. B., Susana, A, Johnson, J. L., Newby,C. (2012) Classical macrophage activation up-regulates several matrix metalloproteinases through mitogen activated protein kinases and nuclear factor-KB. PLoS One 7, e42507.
    • (2012) PLoS One , vol.7
    • Huang, W.C.1    Sala-Newby, G.B.2    Susana, A.3    Johnson, J.L.4
  • 56
    • 84861058085 scopus 로고    scopus 로고
    • LPS counter regulates RNA expression of extracellular proteases and their inhibitors in murine macrophages
    • Hald, A, Rono, B., Lund, L. R, Egerod, K L. (2012) LPS counter regulates RNA expression of extracellular proteases and their inhibitors in murine macrophages. Mediators Inflamm. 2012, 157-894.
    • (2012) Mediators Inflamm , vol.2012 , pp. 157-894
    • Hald, A.1    Rono, B.2    Lund, L.R.3    Egerod, K.L.4
  • 57
    • 79960903578 scopus 로고    scopus 로고
    • Diverse patterns of cyclooxygenase-independent metalloproteinase gene regulation in human monocytes
    • Reel, B., Sala-Newby, G. B., Huang, W. C, Newby, A. C. (2011) Diverse patterns of cyclooxygenase-independent metalloproteinase gene regulation in human monocytes. Br. J. Pharmacol. 163, 1679-1690.
    • (2011) Br. J. Pharmacol , vol.163 , pp. 1679-1690
    • Reel, B.1    Sala-Newby, G.B.2    Huang, W.C.3    Newby, A.C.4
  • 59
    • 0033966536 scopus 로고    scopus 로고
    • Progesterone inhibits activation of latent matrix metalloproteinase (MMP)-2 by membrane-type 1 MMP: Enzymes coordinately expressed in human endometrium
    • Zhang, J., Hampton, A. L., Nie, G., Salamonsen, L. A. (2000) Progesterone inhibits activation of latent matrix metalloproteinase (MMP)-2 by membrane-type 1 MMP: enzymes coordinately expressed in human endometrium. Biol. Reprod. 62, 85-94.
    • (2000) Biol. Reprod , vol.62 , pp. 85-94
    • Zhang, J.1    Hampton, A.L.2    Nie, G.3    Salamonsen, L.A.4
  • 62
    • 18544367029 scopus 로고    scopus 로고
    • Membrane type 1-matrix metalloproteinase is involved in migration of human monocytes and is regulated through their interaction with fibronectin or endothelium
    • Matias-Roman, S., Galvez, B. G., Genis, L., Yanez-Mo, M., de la Rosa, G., Sanchez-Mateos, P., Sanchez-Madrid, F., Arroyo, A. G. (2005) Membrane type 1-matrix metalloproteinase is involved in migration of human monocytes and is regulated through their interaction with fibronectin or endothelium. Blood 105, 3956-3964.
    • (2005) Blood , vol.105 , pp. 3956-3964
    • Matias-Roman, S.1    Galvez, B.G.2    Genis, L.3    Yanez-Mo, M.4    De la, R.G.5    Sanchez-Mateos, P.6    Sanchez-Madrid, F.7    Arroyo, A.G.8
  • 63
    • 80053119490 scopus 로고    scopus 로고
    • Genetic dissection of proteolytic and non-proteolytic contributions of MT1-MMP to macrophage invasion
    • Hara, T., Mimura, K, Seiki, M., Sakamoto, T. (2011) Genetic dissection of proteolytic and non-proteolytic contributions of MT1-MMP to macrophage invasion. Biochem. Biophys. Res. Commun. 413, 277-281.
    • (2011) Biochem. Biophys. Res. Commun , vol.413 , pp. 277-281
    • Hara, T.1    Mimura, K.2    Seiki, M.3    Sakamoto, T.4
  • 64
    • 65449123485 scopus 로고    scopus 로고
    • Cytoplasmic tail of MT1-MMP regulates macrophage motility independently from its protease activity
    • Sakamoto, T., Seiki, M. (2009) Cytoplasmic tail of MT1-MMP regulates macrophage motility independently from its protease activity. Genes Cells 14, 617-626.
    • (2009) Genes Cells , vol.14 , pp. 617-626
    • Sakamoto, T.1    Seiki, M.2
  • 66
    • 59449107340 scopus 로고    scopus 로고
    • Membrane-type 1 matrix metalloproteinase regulates macrophage-dependent elastolytic activity and aneurysm formation in vivo
    • Xiong, W., Knispel, R, MacTaggart, J., Greiner, T. C, Weiss, S. J., Baxter, B. T. (2009) Membrane-type 1 matrix metalloproteinase regulates macrophage-dependent elastolytic activity and aneurysm formation in vivo. J. Biol. Chem. 284, 1765-1771.
    • (2009) J. Biol. Chem , vol.284 , pp. 1765-1771
    • Xiong, W.1    Knispel, R.2    Mactaggart, J.3    Greiner, T.C.4    Weiss, S.J.5    Baxter, B.T.6
  • 70
    • 0036020957 scopus 로고    scopus 로고
    • Relationship between expression of matrix metalloproteinases and migration of epidermal and in vitro generated Lang-erhans cells
    • Noirey, N., Staquet, M. J., Gariazzo, M. J., Serres, M., Andre, C, Schmitt, D., Vincent, C. (2002) Relationship between expression of matrix metalloproteinases and migration of epidermal and in vitro generated Lang-erhans cells. Eur. J. Cell Biol. 81, 383-389.
    • (2002) Eur. J. Cell Biol , vol.81 , pp. 383-389
    • Noirey, N.1    Staquet, M.J.2    Gariazzo, M.J.3    Serres, M.4    Andre, C.5    Schmitt, D.6    Vincent, C.7
  • 71
    • 33750466237 scopus 로고    scopus 로고
    • Membrane type 1-matrix metalloproteinase is involved in the migration of human monocyte-derived dendritic cells
    • Yang, M. X., Qu, X., Kong, B. H., Lam, Q. L., Shao, Q. Q, Deng, B. P., Ko, K H., Lu, L. (2006) Membrane type 1-matrix metalloproteinase is involved in the migration of human monocyte-derived dendritic cells. Immunol. Cell Biol. 84, 557-562.
    • (2006) Immunol. Cell Biol , vol.84 , pp. 557-562
    • Yang, M.X.1    Qu, X.2    Kong, B.H.3    Lam, Q.L.4    Shao, Q.Q.5    Deng, B.P.6    Ko, K.H.7    Lu, L.8
  • 72
    • 51349132659 scopus 로고    scopus 로고
    • Mechanisms and consequences of dendritic cell migration
    • Alvarez, D., Vollmann, E. H., von Andrian, U. H. (2008) Mechanisms and consequences of dendritic cell migration. Immunity 29, 325-342.
    • (2008) Immunity , vol.29 , pp. 325-342
    • Alvarez, D.1    Vollmann, E.H.2    von Andrian, U.H.3
  • 73
    • 0034579433 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinases and their inhibitors by rat NK cells: Inhibition of their expression by genistein
    • Kim, M. H., Albertsson, P., Xue, Y, Kitson, R P., Nannmark, U., Gold-farb, R H. (2000) Expression of matrix metalloproteinases and their inhibitors by rat NK cells: inhibition of their expression by genistein. In Vivo 14, 557-564.
    • (2000) Vivo , vol.14 , pp. 557-564
    • Kim, M.H.1    Albertsson, P.2    Xue, Y.3    Kitson, R.P.4    Nannmark, U.5    Gold-Farb, R.H.6
  • 78
    • 0033256294 scopus 로고    scopus 로고
    • Leukolysin/MMP25/MT6-MMP: A novel matrix metalloproteinase specifically expressed in the leukocyte lineage
    • Pei, D. (1999) Leukolysin/MMP25/MT6-MMP: a novel matrix metalloproteinase specifically expressed in the leukocyte lineage. Cell. Res. 9, 291-303.
    • (1999) Cell. Res , vol.9 , pp. 291-303
    • Pei, D.1
  • 79
    • 0037044851 scopus 로고    scopus 로고
    • Proteomic analysis of a detergent-resistant membrane skeleton from neutrophil plasma membranes
    • Nebl, T., Pestonjamasp, K N., Leszyk, J. D., Crowley, J. L., Oh, S. W., Luna, E. J. (2002) Proteomic analysis of a detergent-resistant membrane skeleton from neutrophil plasma membranes. J. Biol. Chem. 277, 43399-43409.
    • (2002) J. Biol. Chem , vol.277 , pp. 43399-43409
    • Nebl, T.1    Pestonjamasp, K.N.2    Leszyk, J.D.3    Crowley, J.L.4    Oh, S.W.5    Luna, E.J.6
  • 80
    • 0035877649 scopus 로고    scopus 로고
    • Subcellular distribution and cytokine-and chemokine-regulated secretion of leukolysin/MT6-MMP/MMP-25 in neutrophils
    • Kang, T., Yi, J., Guo, A, Wang, X., Overall, C. M., Jiang, W., Elde, R, Borregaard, N., Pei, D. (2001) Subcellular distribution and cytokine-and chemokine-regulated secretion of leukolysin/MT6-MMP/MMP-25 in neutrophils. J. Biol. Chem. 276, 21960-21968.
    • (2001) J. Biol. Chem , vol.276 , pp. 21960-21968
    • Kang, T.1    Yi, J.2    Guo, A.3    Wang, X.4    Overall, C.M.5    Jiang, W.6    Elde, R.7    Borregaard, N.8    Pei, D.9
  • 81
    • 0142219888 scopus 로고    scopus 로고
    • Direct activation of pro-matrix metalloprotei-nase-2 by leukolysin/membrane-type 6 matrix metalloproteinase/matrix metalloproteinase 25 at the asn(109)-Tyr bond
    • Nie, J., Pei, D. (2003) Direct activation of pro-matrix metalloprotei-nase-2 by leukolysin/membrane-type 6 matrix metalloproteinase/matrix metalloproteinase 25 at the asn(109)-Tyr bond. Cancer Res. 63, 6758-6762.
    • (2003) Cancer Res , vol.63 , pp. 6758-6762
    • Nie, J.1    Pei, D.2
  • 83
    • 0141815661 scopus 로고    scopus 로고
    • Clusterin, an abundant serum factor, is a possible negative regulator of MT6-MMP/MMP-25 produced by neutrophils
    • Matsuda, A, Itoh, Y, Koshikawa, N., Akizawa, T., Yana, I., Seiki, M. (2003) Clusterin, an abundant serum factor, is a possible negative regulator of MT6-MMP/MMP-25 produced by neutrophils. J. Biol. Chem. 278, 36350-36357.
    • (2003) J. Biol. Chem , vol.278 , pp. 36350-36357
    • Matsuda, A.1    Itoh, Y.2    Koshikawa, N.3    Akizawa, T.4    Yana, I.5    Seiki, M.6
  • 84
    • 33646088738 scopus 로고    scopus 로고
    • Cell surface expression of intermediate filament proteins vimentin and lamin B1 in human neutrophil spontaneous apoptosis
    • Moisan, E., Girard, D. (2006) Cell surface expression of intermediate filament proteins vimentin and lamin B1 in human neutrophil spontaneous apoptosis. J. Leukoc. Biol. 79, 489-498.
    • (2006) J. Leukoc. Biol , vol.79 , pp. 489-498
    • Moisan, E.1    Girard, D.2
  • 85
    • 33645787738 scopus 로고    scopus 로고
    • Production of matrix metalloproteinases in human cultured mast cells: Involvement of protein kinase C-mitogen activated protein kinase kinase-extracellular signal-regulated kinase pathway
    • Kimata, M., Ishizaki, M., Tanaka, H., Nagai, H., Inagaki, N. (2006) Production of matrix metalloproteinases in human cultured mast cells: involvement of protein kinase C-mitogen activated protein kinase kinase-extracellular signal-regulated kinase pathway. Allergol. Int. 55, 67-76.
    • (2006) Allergol. Int , vol.55 , pp. 67-76
    • Kimata, M.1    Ishizaki, M.2    Tanaka, H.3    Nagai, H.4    Inagaki, N.5
  • 87
    • 20344368596 scopus 로고    scopus 로고
    • Furin-like proprotein convertases are central regulators of the membrane type matrix metalloproteinase-pro-matrix metalloproteinase-2 proteolytic cascade in atherosclerosis
    • Stawowy, P., Meyborg, H., Stibenz, D., Borges Pereira Stawowy, N., Roser, M., Thanabalasingam, U., Veinot, J. P., Chretien, M., Seidah, N. G., Fleck, E., Graf, K. (2005) Furin-like proprotein convertases are central regulators of the membrane type matrix metalloproteinase-pro-matrix metalloproteinase-2 proteolytic cascade in atherosclerosis. Circulation 111, 2820-2827.
    • (2005) Circulation , vol.111 , pp. 2820-2827
    • Stawowy, P.1    Meyborg, H.2    Stibenz, D.3    Stawowy, B.P.N.4    Roser, M.5    Thanabalasingam, U.6    Veinot, J.P.7    Chretien, M.8    Seidah, N.G.9    Fleck, E.10    Graf, K.11
  • 90
    • 33847066678 scopus 로고    scopus 로고
    • Defining the roles of T cell membrane proteinase and CD44 in type 1 diabetes
    • Savinov, A. Y., Strongin, A. Y. (2007) Defining the roles of T cell membrane proteinase and CD44 in type 1 diabetes. IUBMB Life 59, 6-13.
    • (2007) IUBMB Life , vol.59 , pp. 6-13
    • Savinov, A.Y.1    Strongin, A.Y.2
  • 92
    • 2942751908 scopus 로고    scopus 로고
    • Pro-MMP-9 is a specific macrophage product and is activated by osteoar-thritic chondrocytes via MMP-3 or a MT1-MMP/MMP-13 cascade
    • Dreier, R., Grassel, S., Fuchs, S., Schaumburger, J., Bruckner, P. (2004) Pro-MMP-9 is a specific macrophage product and is activated by osteoar-thritic chondrocytes via MMP-3 or a MT1-MMP/MMP-13 cascade. Exp. Cell. Res. 297, 303-312.
    • (2004) Exp. Cell. Res , vol.297 , pp. 303-312
    • Dreier, R.1    Grassel, S.2    Fuchs, S.3    Schaumburger, J.4    Bruckner, P.5
  • 94
    • 36148965872 scopus 로고    scopus 로고
    • Downregulation of membrane type-matrix metalloproteinases in the inflamed or injured central nervous system
    • Toft-Hansen, H., Babcock, A. A., Millward, J. M., Owens, T. (2007) Downregulation of membrane type-matrix metalloproteinases in the inflamed or injured central nervous system. J. Neuroinflammation 4, 24.
    • (2007) J. Neuroinflammation , vol.4 , pp. 24
    • Toft-Hansen, H.1    Babcock, A.A.2    Millward, J.M.3    Owens, T.4
  • 95
    • 6344252618 scopus 로고    scopus 로고
    • Key metalloproteinases are expressed by specific cell types in experimental autoimmune encephalomyelitis
    • Toft-Hansen, H., Nuttall, R. K, Edwards, D. R., Owens, T. (2004) Key metalloproteinases are expressed by specific cell types in experimental autoimmune encephalomyelitis. J. Immunol. 173, 5209-5218.
    • (2004) J. Immunol , vol.173 , pp. 5209-5218
    • Toft-Hansen, H.1    Nuttall, R.K.2    Edwards, D.R.3    Owens, T.4
  • 97
    • 0031596366 scopus 로고    scopus 로고
    • The interrelationship of a4 integrin and matrix metalloprotei-nase-2 in the pathogenesis of experimental autoimmune encephalomyelitis
    • Graesser, D., Mahooti, S., Haas, T., Davis, S., Clark, R B., Madri, J. A (1998) The interrelationship of a4 integrin and matrix metalloprotei-nase-2 in the pathogenesis of experimental autoimmune encephalomyelitis. Lab. Invest. 78, 1445-1458.
    • (1998) Lab. Invest , vol.78 , pp. 1445-1458
    • Graesser, D.1    Mahooti, S.2    Haas, T.3    Davis, S.4    Clark, R.B.5    Madri, J.A.6
  • 98
    • 0031755719 scopus 로고    scopus 로고
    • Enhanced expression of membrane type-1 matrix metalloprotei-nase in mesangial proliferative glomerulonephritis
    • Hayashi, K, Osada, S., Shofuda, K, Horikoshi, S., Shirato, I., Tomino, Y (1998) Enhanced expression of membrane type-1 matrix metalloprotei-nase in mesangial proliferative glomerulonephritis. J. Am. Soc. Nephrol. 9, 2262-2271.
    • (1998) J. Am. Soc. Nephrol , vol.9 , pp. 2262-2271
    • Hayashi, K.1    Osada, S.2    Shofuda, K.3    Horikoshi, S.4    Shirato, I.5    Tomino, Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.