메뉴 건너뛰기




Volumn 4, Issue 3, 2011, Pages 351-360

Matrix metalloproteinases in cytotoxic lymphocytes impact on tumour infiltration and immunomodulation

Author keywords

Cytotoxic lymphocyte; Matrix metalloproteinases; Natural killer cell; Proteases; T lymphocyte; Tumour infiltration

Indexed keywords

BATIMASTAT; COLLAGENASE 3; FOCAL ADHESION KINASE; GAMMA INTERFERON; GELATINASE A; GELATINASE B; HEPARANASE; ILOMASTAT; INTERLEUKIN 2; INTERSTITIAL COLLAGENASE; LAMIN; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE 14; MATRIX METALLOPROTEINASE 15; MATRIX METALLOPROTEINASE 16; RANTES; STROMAL CELL DERIVED FACTOR 1; TISSUE INHIBITOR OF METALLOPROTEINASE;

EID: 84856422630     PISSN: 18752292     EISSN: 18752284     Source Type: Journal    
DOI: 10.1007/s12307-010-0057-0     Document Type: Review
Times cited : (39)

References (125)
  • 1
    • 0033804943 scopus 로고    scopus 로고
    • Extracellular matrix moieties, cytokines, and enzymes: Dynamic effects on immune cell behavior and inflammation
    • Vaday GG, Lider O (2000) Extracellular matrix moieties, cytokines, and enzymes: dynamic effects on immune cell behavior and inflammation. J Leukoc Biol 67:149-59
    • (2000) J Leukoc Biol , vol.67 , pp. 149-159
    • Vaday, G.G.1    Lider, O.2
  • 2
    • 0033056463 scopus 로고    scopus 로고
    • The cell biology of leukocytemediated proteolysis
    • Owen CA, Campbell EJ (1999) The cell biology of leukocytemediated proteolysis. J Leukoc Biol 65:137-50
    • (1999) J Leukoc Biol , vol.65 , pp. 137-150
    • Owen, C.A.1    Campbell, E.J.2
  • 6
    • 77953068069 scopus 로고    scopus 로고
    • Effects of IL-2 on MMP expression in freshly isolated human NK cells and the IL-2 independent NK cell line YT
    • Edsparr K, Speetjens FM, Mulder-Stapel A et al (2010) Effects of IL-2 on MMP expression in freshly isolated human NK cells and the IL-2 independent NK cell line YT. J Immunother 33(5):475-81
    • (2010) J Immunother , vol.33 , Issue.5 , pp. 475-481
    • Edsparr, K.1    Speetjens, F.M.2    Mulder-Stapel, A.3
  • 9
    • 0029892991 scopus 로고    scopus 로고
    • 2 receptor
    • DOI 10.1021/bi960036x
    • Zeng L, An S, Goetzl EJ (1996) Selective regulation of RNK-16 cell matrix metalloproteinases by the EP4 subtype of prostaglandin E2 receptor. Biochemistry 35:7159-64 (Pubitemid 26182107)
    • (1996) Biochemistry , vol.35 , Issue.22 , pp. 7159-7164
    • Zeng, L.1    An, S.2    Goetzl, E.J.3
  • 10
    • 0034579433 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinases and their inhibitors by rat NK cells: Inhibition of their expression by genistein
    • Kim MH, Albertsson P, Xue Y, Kitson RP, Nannmark U, Goldfarb RH (2000) Expression of matrix metalloproteinases and their inhibitors by rat NK cells: inhibition of their expression by genistein. In Vivo 14:557-64 (Pubitemid 34097516)
    • (2000) Vivo , vol.14 , Issue.5 , pp. 557-564
    • Kim, M.H.1    Albertsson, P.2    Xue, Y.3    Kitson, R.P.4    Nannmark, U.5    Goldfarb, R.H.6
  • 12
    • 0031777912 scopus 로고    scopus 로고
    • Infiltration patterns of short- and long-term cultured A-NK and T-LAK cells following adoptive immunotherapy
    • DOI 10.1046/j.1365-3083.1998.00339.x
    • Kjaergaard J, HoklandM, Nannmark U, Hokland P, Basse P (1998) Infiltration patterns of short-and long-term cultured A-NK and T-LAK cells following adoptive immunotherapy. Scand J Immunol 47:532-40 (Pubitemid 28273362)
    • (1998) Scandinavian Journal of Immunology , vol.47 , Issue.6 , pp. 532-540
    • Kjaeergaard, J.1    Hokland, M.2    Nannmark, U.3    Hokland, P.4    Basse, P.5
  • 13
    • 10844227443 scopus 로고    scopus 로고
    • Prolonged culture of vaccine-primed lymphocytes results in decreased antitumor killing and change in cytokine secretion
    • DOI 10.1158/0008-5472.CAN-03-0376
    • Sussman JJ, Parihar R, Winstead K, Finkelman FD (2004) Prolonged culture of vaccine-primed lymphocytes results in decreased antitumor killing and change in cytokine secretion. Cancer Res 64:9124-30 (Pubitemid 39665526)
    • (2004) Cancer Research , vol.64 , Issue.24 , pp. 9124-9130
    • Sussman, J.J.1    Parihar, R.2    Winstead, K.3    Finkelman, F.D.4
  • 14
    • 0029041446 scopus 로고
    • T cell gelatinases mediate basement membrane transmigration in vitro
    • Leppert D, Waubant E, Galardy R, Bunnett NW, Hauser SL (1995) T cell gelatinases mediate basement membrane transmigration in vitro. J Immunol 154:4379-89
    • (1995) J Immunol , vol.154 , pp. 4379-4389
    • Leppert, D.1    Waubant, E.2    Galardy, R.3    Bunnett, N.W.4    Hauser, S.L.5
  • 15
    • 0028362088 scopus 로고
    • The induction of 72-kD gelatinase in T cells upon adhesion to endothelial cells is VCAM-1 dependent
    • DOI 10.1083/jcb.125.5.1165
    • Romanic AM, Madri JA (1994) The induction of 72-kD gelatinase in T cells upon adhesion to endothelial cells is VCAM-1 dependent. J Cell Biol 125:1165-78 (Pubitemid 24177218)
    • (1994) Journal of Cell Biology , vol.125 , Issue.5 , pp. 1165-1178
    • Romanic, A.M.1    Madri, J.A.2
  • 20
    • 0031868017 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinases by human plasma cells and B lymphocytes
    • DOI 10.1002/(SICI)1521-4141(199806)28:06<1773::AID-IMMU1773>3.0. CO;2-B
    • Di Girolamo N, Tedla N, Lloyd A, Wakefield D (1998) Expression of matrix metalloproteinases by human plasma cells and B lymphocytes. Eur J Immunol 28:1773-84 (Pubitemid 28271693)
    • (1998) European Journal of Immunology , vol.28 , Issue.6 , pp. 1773-1784
    • Di Girolamo, N.1    Tedla, N.2    Lloyd, A.3    Wakefield, D.4
  • 21
    • 0032493738 scopus 로고    scopus 로고
    • Human B lymphocytes synthesize the 92-kDa gelatinase, matrix metalloproteinase-9
    • DOI 10.1074/jbc.273.32.20677
    • Trocme C, Gaudin P, Berthier S, Barro C, Zaoui P, Morel F (1998) Human B lymphocytes synthesize the 92-kDa gelatinase, matrix metalloproteinase-9. J Biol Chem 273:20677-84 (Pubitemid 28377640)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.32 , pp. 20677-20684
    • Trocme, C.1    Gaudin, P.2    Berthier, S.3    Barro, C.4    Zaoui, P.5    Morel, F.6
  • 22
    • 77952065445 scopus 로고    scopus 로고
    • CCR5 signaling suppresses inflammation and reduces adverse remodeling of the infarcted heart, mediating recruitment of regulatory T cells
    • Dobaczewski M, Xia Y, Bujak M, Gonzalez-Quesada C, Frangogiannis NG (2010) CCR5 signaling suppresses inflammation and reduces adverse remodeling of the infarcted heart, mediating recruitment of regulatory T cells. Am J Pathol 176:2177-87
    • (2010) Am J Pathol , vol.176 , pp. 2177-2187
    • Dobaczewski, M.1    Xia, Y.2    Bujak, M.3    Gonzalez-Quesada, C.4    Frangogiannis, N.G.5
  • 23
    • 0028860849 scopus 로고
    • Stimulation of matrix metalloproteinase-dependent migration of T cells by eicosanoids
    • Leppert D, Hauser SL, Kishiyama JL, An S, Zeng L, Goetzl EJ (1995) Stimulation of matrix metalloproteinase-dependent migration of T cells by eicosanoids. Faseb J 9:1473-81
    • (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
  • 26
    • 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
    • DOI 10.1002/ana.410400606
    • Leppert D, Waubant E, Burk MR, Oksenberg JR, Hauser SL (1996) 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 40:846-52 (Pubitemid 27044602)
    • (1996) Annals of Neurology , vol.40 , Issue.6 , pp. 846-852
    • Leppert, D.1    Waubant, E.2    Burk, M.R.3    Oksenberg, J.R.4    Hauser, S.L.5
  • 27
    • 0030498666 scopus 로고    scopus 로고
    • Interferon β-1b decreases the migration of T lymphocytes in vitro: Effects on matrix metalloproteinase-9
    • DOI 10.1002/ana.410400607
    • Stuve O, Dooley NP, Uhm JH et al (1996) Interferon beta-1b decreases the migration of T lymphocytes in vitro: effects on matrix metalloproteinase-9. Ann Neurol 40:853-63 (Pubitemid 27044603)
    • (1996) Annals of Neurology , vol.40 , Issue.6 , pp. 853-863
    • Stuve, O.1    Dooley, N.P.2    Uhm, J.H.3    Antel, J.P.4    Francis, G.S.5    Williams, G.6    Yong, V.W.7
  • 29
    • 4444226050 scopus 로고    scopus 로고
    • Inhibition of MMP-dependent chemotaxis and amelioration of experimental autoimmune uveitis with a selective metalloproteinase-2 and -9 inhibitor
    • DOI 10.1016/j.jneuroim.2004.05.010, PII S0165572804001687
    • El-Shabrawi Y, Walch A, Hermann J, Egger G, Foster CS (2004) Inhibition of MMP-dependent chemotaxis and amelioration of experimental autoimmune uvei tis with a selective metalloproteinase-2 and -9 inhibitor. J Neuroimmunol 155:13-20 (Pubitemid 39165773)
    • (2004) Journal of Neuroimmunology , vol.155 , Issue.1-2 , pp. 13-20
    • El-Shabrawi, Y.1    Walch, A.2    Hermann, J.3    Egger, G.4    Foster, C.S.5
  • 31
    • 0141958125 scopus 로고    scopus 로고
    • Up-regulation of matrix metalloproteinase-9 in T lymphocytes of mammary tumor bearers: Role of vascular endothelial growth factor
    • Owen JL, Iragavarapu-Charyulu V, Gunja-Smith Z, Herbert LM, Grosso JF, Lopez DM (2003) Up-regulation of matrix metalloproteinase-9 in T lymphocytes of mammary tumor bearers: role of vascular endothelial growth factor. J Immunol 171:4340-51 (Pubitemid 37238712)
    • (2003) Journal of Immunology , vol.171 , Issue.8 , pp. 4340-4351
    • Owen, J.L.1    Iragavarapu-Charyulu, V.2    Gunja-Smith, Z.3    Herbert, L.M.4    Grosso, J.F.5    Lopez, D.M.6
  • 32
    • 0036901565 scopus 로고    scopus 로고
    • Rapid trafficking of membrane type 1-matrix metalloproteinase to the cell surface regulates progelatinase A activation
    • Zucker S, Hymowitz M, Conner CE, DiYanni EA, Cao J (2002) Rapid trafficking of membrane type 1-matrix metalloproteinase to the cell surface regulates progelatinase a activation. Lab Invest 82:1673-84 (Pubitemid 35462980)
    • (2002) Laboratory Investigation , vol.82 , Issue.12 , pp. 1673-1684
    • Zucker, S.1    Hymowitz, M.2    Conner, C.E.3    DiYanni, E.A.4    Cao, J.5
  • 33
    • 0025897141 scopus 로고
    • Mobilization of gelatinase-rich granules as a regulatory mechanism of early functional responses in human neutrophils
    • Mollinedo F, Pulido R, Lacal PM, Sanchez-Madrid F (1991) Mobilization of gelatinase-rich granules as a regulatory mechanism of early functional responses in human neutrophils. Scand J Immunol 34:33-43
    • (1991) Scand J Immunol , vol.34 , pp. 33-43
    • Mollinedo, F.1    Pulido, R.2    Lacal, P.M.3    Sanchez-Madrid, F.4
  • 34
    • 2942536116 scopus 로고    scopus 로고
    • Membrane-bound matrix metalloproteinase-8 on activated polymorphonuclear cells is a potent, tissue inhibitor of metalloproteinase-resistant collagenase and serpinase
    • Owen CA, Hu Z, Lopez-Otin C, Shapiro SD (2004) Membranebound matrix metalloproteinase-8 on activated polymorphonuclear cells is a potent, tissue inhibitor of metalloproteinaseresistant collagenase and serpinase. J Immunol 172:7791-803 (Pubitemid 38747647)
    • (2004) Journal of Immunology , vol.172 , Issue.12 , pp. 7791-7803
    • Owen, C.A.1    Hu, Z.2    Lopez-Otin, C.3    Shapiro, S.D.4
  • 35
    • 0042330309 scopus 로고    scopus 로고
    • Inducible expression of tissue inhibitor of metalloproteinases-resistant matrix metalloproteinase-9 on the cell surface of neutrophils
    • DOI 10.1165/rcmb.2003-0034OC
    • Owen CA, Hu Z, Barrick B, Shapiro SD (2003) Inducible expression of tissue inhibitor of metalloproteinases-resistant matrix metalloproteinase-9 on the cell surface of neutrophils. Am J Respir Cell Mol Biol 29:283-94 (Pubitemid 37093986)
    • (2003) American Journal of Respiratory Cell and Molecular Biology , vol.29 , Issue.3 , pp. 283-294
    • Owen, C.A.1    Hu, Z.2    Barrick, B.3    Shapiro, S.D.4
  • 39
    • 0032926177 scopus 로고    scopus 로고
    • Localization of matrix metalloproteinase 9 to the cell surface provides a mechanism for CD44-mediated tumor invasion
    • Yu Q, Stamenkovic I (1999) Localization of matrix metalloproteinase 9 to the cell surface provides a mechanism for CD44-mediated tumor invasion. Genes Dev 13:35-48 (Pubitemid 29045114)
    • (1999) Genes and Development , vol.13 , Issue.1 , pp. 35-48
    • Yu, Q.1    Stamenkovic, I.2
  • 40
    • 0034635483 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans as extracellular docking molecules for matrilysin (matrix metalloproteinase 7)
    • DOI 10.1074/jbc.275.6.4183
    • Yu WH, Woessner JF Jr (2000) Heparan sulfate proteoglycans as extracellular docking molecules for matrilysin (matrix metalloproteinase 7). J Biol Chem 275:4183-91 (Pubitemid 30094653)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.6 , pp. 4183-4191
    • Yu, W.-H.1    Woessner Jr., J.F.2
  • 41
    • 0032820711 scopus 로고    scopus 로고
    • Proteolysis and cell migration: Creating a path?
    • DOI 10.1016/S0955-0674(99)00022-8
    • Murphy G, Gavrilovic J (1999) Proteolysis and cell migration: creating a path? Curr Opin Cell Biol 11:614-21 (Pubitemid 29460404)
    • (1999) Current Opinion in Cell Biology , vol.11 , Issue.5 , pp. 614-621
    • Murphy, G.1    Gavrilovic, J.2
  • 42
    • 0032850365 scopus 로고    scopus 로고
    • Matrix metalloproteinases in tumour invasion and metastasis
    • DOI 10.1002/(SICI)1096-9896(199911)189:3<300::AID-PATH456>3.0.CO;2- C
    • Curran S, Murray GI (1999) Matrix metalloproteinases in tumour invasion and metastasis. J Pathol 189:300-8 (Pubitemid 29489213)
    • (1999) Journal of Pathology , vol.189 , Issue.3 , pp. 300-308
    • Curran, S.1    Murray, G.I.2
  • 44
    • 0034579833 scopus 로고    scopus 로고
    • Cooperation of urokinase plasminogen activator and matrix metalloproteinases in NK cell invasion
    • Al-Atrash G, Kitson RP, Xue Y, Goldfarb RH (2000) Cooperation of urokinase plasminogen activator and matrix metalloproteinases in NK cell invasion. In Vivo 14:565-70 (Pubitemid 34097517)
    • (2000) Vivo , vol.14 , Issue.5 , pp. 565-570
    • Al-Atrash, G.1    Kitson, R.P.2    Xue, Y.3    Goldfarb, R.H.4
  • 45
    • 0035059626 scopus 로고    scopus 로고
    • Expression of neutrophil collagenase (MMP-8) in Jurkat T leukemia cells and its role in invasion
    • Kim MH, Albertsson P, Xue Y, Nannmark U, Kitson RP, Goldfarb RH (2001) Expression of neutrophil collagenase (MMP-8) in Jurkat T leukemia cells and its role in invasion. Anticancer Res 21:45-50 (Pubitemid 32267623)
    • (2001) Anticancer Research , vol.21 , Issue.1 A , pp. 45-50
    • Kim, M.H.1    Albertsson, P.2    Xue, Y.3    Nannmark, U.4    Kitson, R.P.5    Goldfarb, R.H.6
  • 46
    • 50549091849 scopus 로고    scopus 로고
    • Collagen i but not Matrigel matrices provide an MMP-dependent barrier to ovarian cancer cell penetration
    • Sodek KL, Brown TJ, Ringuette MJ (2008) Collagen I but not Matrigel matrices provide an MMP-dependent barrier to ovarian cancer cell penetration. BMC Cancer 8:223
    • (2008) BMC Cancer , vol.8 , pp. 223
    • Sodek, K.L.1    Brown, T.J.2    Ringuette, M.J.3
  • 47
    • 0026011134 scopus 로고
    • Invasion of reconstituted basement membrane matrix is not correlated to the malignant metastatic cell phenotype
    • Noel AC, Calle A, Emonard HP et al (1991) Invasion of reconstituted basement membrane matrix is not correlated to the malignant metastatic cell phenotype. Cancer Res 51:405-14
    • (1991) Cancer Res , vol.51 , pp. 405-414
    • Noel, A.C.1    Calle, A.2    Emonard, H.P.3
  • 48
    • 0030001675 scopus 로고    scopus 로고
    • Lymphocyte homing and homeostasis
    • Butcher EC, Picker LJ (1996) Lymphocyte homing and homeostasis. Science 272:60-6 (Pubitemid 26110755)
    • (1996) Science , vol.272 , Issue.5258 , pp. 60-66
    • Butcher, E.C.1    Picker, L.J.2
  • 50
    • 0031903617 scopus 로고    scopus 로고
    • + T lymphocytes migrating in three-dimensional collagen lattices lack focal adhesions and utilize β1 integrin-independent strategies for polarization, interaction with collagen fibers and locomotion
    • DOI 10.1002/(SICI)1521-4141(199808)28:08<2331::AID-IMMU2331>3.0. CO;2-C
    • Friedl P, Entschladen F, Conrad C, Niggemann B, Zanker KS (1998) CD4+ T lymphocytes migrating in three-dimensional collagen lattices lack focal adhesions and utilize beta1 integrinindependent strategies for polarization, interaction with collagen fibers and locomotion. Eur J Immunol 28:2331-43 (Pubitemid 28362708)
    • (1998) European Journal of Immunology , vol.28 , Issue.8 , pp. 2331-2343
    • Friedl, P.1    Entschladen, F.2    Conrad, C.3    Niggemann, B.4    Zanker, K.S.5
  • 51
    • 0033769059 scopus 로고    scopus 로고
    • T cell migration in threedimensional extracellular matrix: Guidance by polarity and sensations
    • Friedl P, Brocker EB (2000) T cell migration in threedimensional extracellular matrix: guidance by polarity and sensations. Dev Immunol 7:249-66
    • (2000) Dev Immunol , vol.7 , pp. 249-266
    • Friedl, P.1    Brocker, E.B.2
  • 52
    • 0029522229 scopus 로고
    • T lymphocyte migration: The influence of interactions via adhesion molecules, the T cell receptor, and cytokines
    • Hauzenberger D, Klominek J, Bergstrom SE, Sundqvist KG (1995) T lymphocyte migration: the influence of interactions via adhesion molecules, the T cell receptor, and cytokines. Crit Rev Immunol 15:285-316 (Pubitemid 26259133)
    • (1995) Critical Reviews in Immunology , vol.15 , Issue.3-4 , pp. 285-316
    • Hauzenberger, D.1    Klominek, J.2    Bergstrom, S.-E.3    Sundqvist, K.-G.4
  • 53
    • 72449188591 scopus 로고    scopus 로고
    • Interstitial cell migration: Integrindependent and alternative adhesion mechanisms
    • Schmidt S, Friedl P (2009) Interstitial cell migration: integrindependent and alternative adhesion mechanisms. Cell Tissue Res 339(1):83-92
    • (2009) Cell Tissue Res , vol.339 , Issue.1 , pp. 83-92
    • Schmidt, S.1    Friedl, P.2
  • 54
    • 75749146306 scopus 로고    scopus 로고
    • Plasticity of cell migration: A multiscale tuning model
    • Friedl P, Wolf K (2010) Plasticity of cell migration: a multiscale tuning model. J Cell Biol 188:11-9
    • (2010) J Cell Biol , vol.188 , pp. 11-19
    • Friedl, P.1    Wolf, K.2
  • 55
    • 70349314647 scopus 로고    scopus 로고
    • Mechanical modes of 'amoeboid' cell migration
    • Lammermann T, Sixt M (2009) Mechanical modes of 'amoeboid' cell migration. Curr Opin Cell Biol 21:636-44
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 636-644
    • Lammermann, T.1    Sixt, M.2
  • 56
    • 0025770432 scopus 로고
    • Establishment of cell-to-cell contact by adoptively transferred adherent lymphokine-activated killer cells with metastatic murine melanoma cells
    • Basse PH, Nannmark U, Johansson BR, Herberman RB, Goldfarb RH (1991) Establishment of cell-to-cell contact by adoptively transferred adherent lymphokine-activated killer cells with metastatic murine melanoma cells. J Natl Cancer Inst 83:944-50
    • (1991) J Natl Cancer Inst , vol.83 , pp. 944-950
    • Basse, P.H.1    Nannmark, U.2    Johansson, B.R.3    Herberman, R.B.4    Goldfarb, R.H.5
  • 57
    • 0028788455 scopus 로고
    • Microvessel origin and distribution in pulmonary metastases of B16 melanoma: Implication for adoptive immunotherapy
    • Nannmark U, Johansson BR, Bryant JL et al (1995) Microvessel origin and distribution in pulmonary metastases of B16 melanoma: implication for adoptive immunotherapy. Cancer Res 55:4627-32
    • (1995) Cancer Res , vol.55 , pp. 4627-4632
    • Nannmark, U.1    Johansson, B.R.2    Bryant, J.L.3
  • 59
    • 69049090790 scopus 로고    scopus 로고
    • Human NK cell lines migrate differentially in vitro related to matrix interaction and MMP expression
    • Edsparr K, Johansson BR, Goldfarb RH et al (2009) Human NK cell lines migrate differentially in vitro related to matrix interaction and MMP expression. Immunol Cell Biol 87(6):489-95
    • (2009) Immunol Cell Biol , vol.87 , Issue.6 , pp. 489-495
    • Edsparr, K.1    Johansson, B.R.2    Goldfarb, R.H.3
  • 61
    • 0023809479 scopus 로고
    • Tumor invasion: A consequence of destructive and compositional matrix alterations
    • Pauli BU, Knudson W (1988) Tumor invasion: a consequence of destructive and compositional matrix alterations. Hum Pathol 19:628-39
    • (1988) Hum Pathol , vol.19 , pp. 628-639
    • Pauli, B.U.1    Knudson, W.2
  • 62
    • 0002064476 scopus 로고
    • Glycosaminoglycans in morphogenesis
    • Hay ED (ed), Plenum, New York
    • Toole BP (1981) Glycosaminoglycans in morphogenesis. In: Hay ED (ed) Cell biology of the extracellular matrix. Plenum, New York, pp 259-94
    • (1981) Cell Biology of the Extracellular Matrix , pp. 259-94
    • Toole, B.P.1
  • 63
    • 36048982445 scopus 로고    scopus 로고
    • Tumor blood vessels, a difficult hurdle for infiltrating leukocytes
    • DOI 10.1016/j.bbcan.2007.07.005, PII S0304419X07000261
    • Castermans K, Griffioen AW (2007) Tumor blood vessels, a difficult hurdle for infiltrating leukocytes. Biochim Biophys Acta 1776:160-74 (Pubitemid 350081058)
    • (2007) Biochimica et Biophysica Acta - Reviews on Cancer , vol.1776 , Issue.2 , pp. 160-174
    • Castermans, K.1    Griffioen, A.W.2
  • 65
    • 0142245603 scopus 로고    scopus 로고
    • Amoeboid shape change and contact guidance: T-lymphocyte crawling through fibrillar collagen is independent of matrix remodeling by MMPs and other proteases
    • DOI 10.1182/blood-2002-12-3791
    • Wolf K, Muller R, Borgmann S, Brocker EB, Friedl P (2003) Amoeboid shape change and contact guidance: T-lymphocyte crawling through fibrillar collagen is independent of matrix remodeling by MMPs and other proteases. Blood 102:3262-9 (Pubitemid 37314765)
    • (2003) Blood , vol.102 , Issue.9 , pp. 3262-3269
    • Wolf, K.1    Muller, R.2    Borgmann, S.3    Brocker, E.-B.4    Friedl, P.5
  • 66
    • 1542495339 scopus 로고    scopus 로고
    • Proteolytic and non-proteolytic migration of tumour cells and leucocytes
    • Friedl P, Wolf K (2003) Proteolytic and non-proteolytic migration of tumour cells and leucocytes. Biochem Soc Symp 70:277-85 (Pubitemid 38497233)
    • (2003) Biochemical Society Symposium , Issue.70 , pp. 277-285
    • Friedl, P.1    Wolf, K.2
  • 68
    • 65249155429 scopus 로고    scopus 로고
    • Protease-dependent versus -independent cancer cell invasion programs: Threedimensional amoeboid movement revisited
    • Sabeh F, Shimizu-Hirota R, Weiss SJ (2009) Protease-dependent versus -independent cancer cell invasion programs: threedimensional amoeboid movement revisited. J Cell Biol 185:11-9
    • (2009) J Cell Biol , vol.185 , pp. 11-19
    • Sabeh, F.1    Shimizu-Hirota, R.2    Weiss, S.J.3
  • 70
    • 0028349554 scopus 로고
    • The infiltration of experimentally induced lung metastases of colon carcinoma CC531 by adoptively transferred interleukin-2-activated natural killer cells in Wag rats
    • Kuppen PJ, Basse PH, Goldfarb RH, Van De Velde CJ, Fleuren GJ, Eggermont AM (1994) The infiltration of experimentally induced lung metastases of colon carcinoma CC531 by adoptively transferred interleukin-2-activated natural killer cells in Wag rats. Int J Cancer 56:574-9 (Pubitemid 24094410)
    • (1994) International Journal of Cancer , vol.56 , Issue.4 , pp. 574-579
    • Kuppen, P.J.K.1    Basse, P.H.2    Goldfarb, R.H.3    Van De Velde, C.J.H.4    Fleuren, G.J.5    Eggermont, A.M.M.6
  • 72
    • 0030002909 scopus 로고    scopus 로고
    • Elimination of established liver metastases by human interleukin 2-activated natural killer cells after locoregional or systemic adoptive transfer
    • Okada K, Nannmark U, Vujanovic NL et al (1996) Elimination of established liver metastases by human interleukin 2-activated natural killer cells after locoregional or systemic adoptive transfer. Cancer Res 56:1599-608
    • (1996) Cancer Res , vol.56 , pp. 1599-608
    • Okada, K.1    Nannmark, U.2    Vujanovic, N.L.3
  • 73
    • 33644590238 scopus 로고    scopus 로고
    • Morphological appearance, content of extracellular matrix and vascular density of lung metastases predicts permissiveness to infiltration by adoptively transferred natural killer and T cells
    • Yang Q, Goding S, Hagenaars M et al (2006) Morphological appearance, content of extracellular matrix and vascular density of lung metastases predicts permissiveness to infiltration by adoptively transferred natural killer and T cells. Cancer Immunol Immunother 55:699-707
    • (2006) Cancer Immunol Immunother , vol.55 , pp. 699-707
    • Yang, Q.1    Goding, S.2    Hagenaars, M.3
  • 76
    • 0028040310 scopus 로고
    • Expression of laminin, collagen IV, fibronectin, and type IV collagenase in gastric carcinoma: An immunohistochemical study of 87 patients
    • David L, Nesland JM, Holm R, Sobrinho-Simoes M (1994) Expression of laminin, collagen IV, fibronectin, and type IV collagenase in gastric carcinoma. An immunohistochemical study of 87 patients. Cancer 73:518-27 (Pubitemid 24046588)
    • (1994) Cancer , vol.73 , Issue.3 , pp. 518-527
    • David, L.1    Nesland, J.M.2    Holm, R.3    Sobrinho-Simoes, M.4
  • 77
    • 0028111297 scopus 로고
    • The extracellular matrix in hepatocellular carcinoma shows different localization patterns depending on the differentiation and the histological pattern of tumors: Immunohistochemical analysis
    • DOI 10.1016/S0168-8278(94)80134-7
    • Torimura T, Ueno T, Inuzuka S et al (1994) The extracellular matrix in hepatocellular carcinoma shows different localization patterns depending on the differentiation and the histological pattern of tumors: immunohistochemical analysis. J Hepatol 21:37-46 (Pubitemid 24236678)
    • (1994) Journal of Hepatology , vol.21 , Issue.1 , pp. 37-46
    • Torimura, T.1    Ueno, T.2    Inuzuka, S.3    Kin, M.4    Ohira, H.5    Kimura, Y.6    Majima, Y.7    Sata, M.8    Abe, H.9    Tanikawa, K.10
  • 78
    • 70449133451 scopus 로고    scopus 로고
    • Collagen-based cell migration models in vitro and in vivo
    • Wolf K, Alexander S, Schacht Vet al (2009) Collagen-based cell migration models in vitro and in vivo. Semin Cell Dev Biol 20:931-41
    • (2009) Semin Cell Dev Biol , vol.20 , pp. 931-941
    • Wolf, K.1    Al Vet Schacht, A.S.2
  • 79
    • 0024708518 scopus 로고
    • The distribution of secondary growths in cancer of the breast
    • Paget S (1989) The distribution of secondary growths in cancer of the breast. Cancer Metastasis Rev 8:98-101
    • (1989) Cancer Metastasis Rev , vol.8 , pp. 98-101
    • Paget, S.1
  • 81
    • 0026723832 scopus 로고
    • Migration of recombinant IL-2-activated T and natural killer cells in the intercellular space of human H-2 glioma spheroids in vitro. A study on adhesion molecules involved
    • Jaaskelainen J, Maenpaa A, Patarroyo M et al (1992) Migration of recombinant IL-2-activated T and natural killer cells in the intercellular space of human H-2 glioma spheroids in vitro. A study on adhesion molecules involved. J Immunol 149:260-8
    • (1992) J Immunol , vol.149 , pp. 260-268
    • Jaaskelainen, J.1    Maenpaa, A.2    Patarroyo, M.3
  • 82
    • 37049020929 scopus 로고    scopus 로고
    • Differing phenotypes between intraepithelial and stromal lymphocytes in early-stage tongue cancer
    • DOI 10.1158/0008-5472.CAN-07-2637
    • Katou F, Ohtani H, Watanabe Y, Nakayama T, Yoshie O, Hashimoto K (2007) Differing phenotypes between intraepithelial and stromal lymphocytes in early-stage tongue cancer. Cancer Res 67:11195-201 (Pubitemid 350248544)
    • (2007) Cancer Research , vol.67 , Issue.23 , pp. 11195-11201
    • Katou, F.1    Ohtani, H.2    Watanabe, Y.3    Nakayama, T.4    Yoshie, O.5    Hashimoto, K.6
  • 83
    • 42049094657 scopus 로고    scopus 로고
    • Innate lymphocyte and dendritic cell cross-talk: A key factor in the regulation of the immune response
    • DOI 10.1111/j.1365-2249.2008.03624.x
    • Reschner A, Hubert P, Delvenne P, Boniver J, Jacobs N (2008) Innate lymphocyte and dendritic cell cross-talk: a key factor in the regulation of the immune response. Clin Exp Immunol 152:219-26 (Pubitemid 351520908)
    • (2008) Clinical and Experimental Immunology , vol.152 , Issue.2 , pp. 219-226
    • Reschner, A.1    Hubert, P.2    Delvenne, P.3    Boniver, J.4    Jacobs, N.5
  • 84
    • 33847020733 scopus 로고    scopus 로고
    • Intracellular targets of matrix metalloproteinase-2 in cardiac disease: Rationale and therapeutic approaches
    • Schulz R (2007) Intracellular targets of matrix metalloproteinase-2 in cardiac disease: rationale and therapeutic approaches. Annu Rev Pharmacol Toxicol 47:211-42
    • (2007) Annu Rev Pharmacol Toxicol , vol.47 , pp. 211-242
    • Schulz, R.1
  • 86
    • 0035071662 scopus 로고    scopus 로고
    • The effects of extracellular pH on immune function
    • Lardner A (2001) The effects of extracellular pH on immune function. J Leukoc Biol 69:522-30 (Pubitemid 32294836)
    • (2001) Journal of Leukocyte Biology , vol.69 , Issue.4 , pp. 522-530
    • Lardner, A.1
  • 87
    • 0026573007 scopus 로고
    • Motility of IL-2-stimulated lymphocytes in neutral and acidified extracellular matrix
    • Ratner S (1992) Motility of IL-2-stimulated lymphocytes in neutral and acidified extracellular matrix. Cell Immunol 139:399-410
    • (1992) Cell Immunol , vol.139 , pp. 399-410
    • Ratner, S.1
  • 88
    • 52749091889 scopus 로고    scopus 로고
    • Monocytes and dendritic cells in a hypoxic environment: Spotlights on chemotaxis and migration
    • Bosco MC, Puppo M, Blengio F et al (2008) Monocytes and dendritic cells in a hypoxic environment: spotlights on chemotaxis and migration. Immunobiology 213:733-49
    • (2008) Immunobiology , vol.213 , pp. 733-749
    • Bosco, M.C.1    Puppo, M.2    Blengio, F.3
  • 89
    • 40149095229 scopus 로고    scopus 로고
    • Hypoxia suppresses the production of MMP-9 by human monocyte-derived dendritic cells and requires activation of adenosine receptor A2b via cAMP/PKA signaling pathway
    • Zhao P, Li XG, Yang M et al (2008) Hypoxia suppresses the production of MMP-9 by human monocyte-derived dendritic cells and requires activation of adenosine receptor A2b via cAMP/PKA signaling pathway. Mol Immunol 45:2187-95
    • (2008) Mol Immunol , vol.45 , pp. 2187-2195
    • Zhao, P.1    Li, X.G.2    Yang, M.3
  • 90
    • 33746442968 scopus 로고    scopus 로고
    • Hypoxia reduces the output of matrix metalloproteinase-9 (MMP-9) in monocytes by inhibiting its secretion and elevating membranal association
    • DOI 10.1189/jlb.0605302
    • Rahat MA, Marom B, Bitterman H, Weiss-Cerem L, Kinarty A, Lahat N (2006) Hypoxia reduces the output of matrix metalloproteinase-9 (MMP-9) in monocytes by inhibiting its secretion and elevating membranal association. J Leukoc Biol 79:706-18 (Pubitemid 44835603)
    • (2006) Journal of Leukocyte Biology , vol.79 , Issue.4 , pp. 706-718
    • Rahat, M.A.1    Marom, B.2    Bitterman, H.3    Weiss-Cerem, L.4    Kinarty, A.5    Lahat, N.6
  • 91
    • 33646593786 scopus 로고    scopus 로고
    • Modifying the soil to affect the seed: Role of stromal-derived matrix metalloproteinases in cancer progression
    • DOI 10.1007/s10555-006-7887-8, Metalloproteinases and Cancer
    • Jodele S, Blavier L, Yoon JM, DeClerck YA (2006) Modifying the soil to affect the seed: role of stromal-derived matrix metalloproteinases in cancer progression. Cancer Metastasis Rev 25:35-43 (Pubitemid 43723980)
    • (2006) Cancer and Metastasis Reviews , vol.25 , Issue.1 , pp. 35-43
    • Jodele, S.1    Blavier, L.2    Yoon, J.M.3    DeClerck, Y.A.4
  • 93
    • 0028900052 scopus 로고
    • Immobilized anti-CD3 antibody activates T cell clones to induce the production of interstitial collagenase, but not tissue inhibitor of metalloproteinases, in monocytic THP-1 cells and dermal fibroblasts
    • Miltenburg AM, Lacraz S, Welgus HG, Dayer JM (1995) Immobilized anti-CD3 antibody activates T cell clones to induce the production of interstitial collagenase, but not tissue inhibitor of metalloproteinases, in monocytic THP-1 cells and dermal fibroblasts. J Immunol 154:2655-67
    • (1995) J Immunol , vol.154 , pp. 2655-2667
    • Miltenburg, A.M.1    Lacraz, S.2    Welgus, H.G.3    Dayer, J.M.4
  • 94
    • 1842415400 scopus 로고    scopus 로고
    • Gelatinase B (MMP-9) production and expression by stromal cells in the normal and adult thymus and experimental thymic lymphoma
    • DOI 10.1002/(SICI)1097-0215(19970328)71:1<71::AID-IJC13>3.0.CO;2-C
    • Aoudjit F, Esteve PO, Desrosiers M, Potworowski EF, St-Pierre Y (1997) Gelatinase B (MMP-9) production and expression by stromal cells in the normal and adult thymus and experimental thymic lymphoma. Int J Cancer 71:71-8 (Pubitemid 27158412)
    • (1997) International Journal of Cancer , vol.71 , Issue.1 , pp. 71-78
    • Aoudjit, F.1    Esteve, P.-O.2    Desrosiers, M.3    Potworowski, E.F.4    St-Pierre, Y.5
  • 95
    • 68449097391 scopus 로고    scopus 로고
    • Human T-leukemia and T-lymphoma express glutamate receptor AMPA GluR3, and the neurotransmitter glutamate elevates the cancer-related matrix-metalloproteinases inducer CD147/EMMPRIN, MMP-9 secretion and engraftment of Tleukemia in vivo
    • Ganor Y, Grinberg I, Reis A, Cooper I, Goldstein RS, Levite M (2009) Human T-leukemia and T-lymphoma express glutamate receptor AMPA GluR3, and the neurotransmitter glutamate elevates the cancer-related matrix-metalloproteinases inducer CD147/EMMPRIN, MMP-9 secretion and engraftment of Tleukemia in vivo. Leuk Lymphoma 50:985-97
    • (2009) Leuk Lymphoma , vol.50 , pp. 985-997
    • Ganor, Y.1    Grinberg, I.2    Reis, A.3    Cooper, I.4    Goldstein, R.S.5    Levite, M.6
  • 97
    • 0002606253 scopus 로고    scopus 로고
    • The urokinase plasminogen activator system in cancer: Implications for tumor angiogenesis and metastasis
    • Mazar AP, Henkin J, Goldfarb RH (1999) The urokinase plasminogen activator system in cancer: implications for tumor angiogenesis and metastasis. Angiogenesis 3:15-32 (Pubitemid 129644777)
    • (1999) Angiogenesis , vol.3 , Issue.1 , pp. 15-32
    • Mazar, A.P.1    Henkin, J.2    Goldfarb, R.H.3
  • 98
    • 0022501236 scopus 로고
    • Identification and localization of urokinase-type plasminogen activator in human NK-cells
    • Carpen O, Saksela O, Saksela E (1986) Identification and localization of urokinase-type plasminogen activator in human NK-cells. Int J Cancer 38:355-60 (Pubitemid 16022317)
    • (1986) International Journal of Cancer , vol.38 , Issue.3 , pp. 355-360
    • Carpen, O.1    Saksela, O.2    Saksela, E.3
  • 99
    • 0021368504 scopus 로고
    • Production of plasminogen activator by human natural killer cells. Large granular lymphocytes
    • DOI 10.1084/jem.159.3.935
    • Goldfarb RH, Timonen T, Herberman RB (1984) Production of plasminogen activator by human natural killer cells. Large granular lymphocytes. J Exp Med 159:935-51 (Pubitemid 14159268)
    • (1984) Journal of Experimental Medicine , vol.159 , Issue.3 , pp. 935-951
    • Goldfarb, R.H.1    Timonen, T.2    Herberman, R.B.3
  • 101
    • 0028067871 scopus 로고
    • Urokinase-type plasminogen activator enhances invasion of human T cells (Jurkat) into a fibrin matrix
    • Kramer MD, Spring H, Todd RF, Vettel U (1994) Urokinase-type plasminogen activator enhances invasion of human T cells (Jurkat) into a fibrin matrix. J Leukoc Biol 56:110-6 (Pubitemid 24270490)
    • (1994) Journal of Leukocyte Biology , vol.56 , Issue.2 , pp. 110-116
    • Kramer, M.D.1    Spring, H.2    Todd, R.F.3    Vettel, U.4
  • 103
    • 0038372578 scopus 로고    scopus 로고
    • Urokinase-type plasminogen activator receptor crosslinking in an NK cell line increases integrin surface expression by the MAP kinase/ERK 1/2 signaling pathway
    • DOI 10.1002/jcb.10512
    • Gellert GC, Kitson RP, Goldfarb RH (2003) Urokinase-type plasminogen activator receptor crosslinking in an NK cell line increases integrin surface expression by the MAP kinase/ERK 1/2 signaling pathway. J Cell Biochem 89:279-88 (Pubitemid 36547262)
    • (2003) Journal of Cellular Biochemistry , vol.89 , Issue.2 , pp. 279-288
    • Gellert, G.C.1    Kitson, R.P.2    Goldfarb, R.H.3
  • 105
    • 0026722647 scopus 로고
    • Expression of heparanase by platelets and circulating cells of the immune system: Possible involvement in diapedesis and extravasation
    • Vlodavsky I, Eldor A, Haimovitz-Friedman A et al (1992) Expression of heparanase by platelets and circulating cells of the immune system: possible involvement in diapedesis and extravasation. Invasion Metastasis 12:112-27
    • (1992) Invasion Metastasis , vol.12 , pp. 112-127
    • Vlodavsky, I.1    Eldor, A.2    Haimovitz-Friedman, A.3
  • 106
    • 57749101252 scopus 로고    scopus 로고
    • Heparanase stimulation of protease expression implicates it as a master regulator of the aggressive tumor phenotype in myeloma
    • Purushothaman A, Chen L, Yang Y, Sanderson RD (2008) Heparanase stimulation of protease expression implicates it as a master regulator of the aggressive tumor phenotype in myeloma. J Biol Chem 283:32628-36
    • (2008) J Biol Chem , vol.283 , pp. 32628-32636
    • Purushothaman, A.1    Chen, L.2    Yang, Y.3    Sanderson, R.D.4
  • 107
    • 65249103282 scopus 로고    scopus 로고
    • Newly generated heparanase knock-out mice unravel co-regulation of heparanase and matrix metalloproteinases
    • Zcharia E, Jia J, Zhang X et al (2009) Newly generated heparanase knock-out mice unravel co-regulation of heparanase and matrix metalloproteinases. PLoS One 4:e5181
    • (2009) PLoS One , vol.4
    • Zcharia, E.1    Jia, J.2    Zhang, X.3
  • 108
    • 53149100519 scopus 로고    scopus 로고
    • Seprase: An overview of an important matrix serine protease
    • O'Brien P, O'Connor BF (2008) Seprase: an overview of an important matrix serine protease. Biochim Biophys Acta 1784:1130-45
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 1130-1145
    • O'brien, P.1    O'connor, B.F.2
  • 112
    • 33846643454 scopus 로고    scopus 로고
    • Cysteine cathepsins and the cutting edge of cancer invasion
    • Gocheva V, Joyce JA (2007) Cysteine cathepsins and the cutting edge of cancer invasion. Cell Cycle 6:60-4 (Pubitemid 46173882)
    • (2007) Cell Cycle , vol.6 , Issue.1 , pp. 60-64
    • Gocheva, V.1    Joyce, J.A.2
  • 113
    • 0025044550 scopus 로고
    • Mechanism of L-leucyl-L-leucine methyl ester-mediated killing of cytotoxic lymphocytes: Dependence on a lysosomal thiol protease, dipeptidyl peptidase I, that is enriched in these cells
    • Thiele DL, Lipsky PE (1990) Mechanism of L-leucyl-L-leucine methyl ester-mediated killing of cytotoxic lymphocytes: dependence on a lysosomal thiol protease, dipeptidyl peptidase I, that is enriched in these cells. Proc Natl Acad Sci U S A 87:83-7
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 83-87
    • Thiele, D.L.1    Lipsky, P.E.2
  • 116
    • 0027136685 scopus 로고
    • Human granzyme B degrades aggrecan proteoglycan in matrix synthesized by chondrocytes
    • Froelich CJ, Zhang X, Turbov J, Hudig D, Winkler U, Hanna WL (1993) Human granzyme B degrades aggrecan proteoglycan in matrix synthesized by chondrocytes. J Immunol 151:7161-71 (Pubitemid 24001090)
    • (1993) Journal of Immunology , vol.151 , Issue.12 , pp. 7161-7171
    • Froelich, C.J.1    Zhang, X.2    Turbov, J.3    Hudig, D.4    Winkler, U.5    Hanna, W.L.6
  • 117
    • 36049005089 scopus 로고    scopus 로고
    • Chemokine and cytokine processing by matrix metalloproteinases and its effect on leukocyte migration and inflammation
    • DOI 10.1189/jlb.0607338
    • Van Lint P, Libert C (2007) Chemokine and cytokine processing by matrix metalloproteinases and its effect on leukocyte migration and inflammation. J Leukoc Biol 82:1375-81 (Pubitemid 350276947)
    • (2007) Journal of Leukocyte Biology , vol.82 , Issue.6 , pp. 1375-1381
    • Van Lint, P.1    Libert, C.2
  • 118
    • 34250312341 scopus 로고    scopus 로고
    • The biochemical, biological, and pathological kaleidoscope of cell surface substrates processed by matrix metalloproteinases
    • DOI 10.1080/10409230701340019, PII 779481892
    • Cauwe B, Van den Steen PE, Opdenakker G (2007) The biochemical, biological, and pathological kaleidoscope of cell surface substrates processed by matrix metalloproteinases. Crit Rev Biochem Mol Biol 42:113-85 (Pubitemid 46911962)
    • (2007) Critical Reviews in Biochemistry and Molecular Biology , vol.42 , Issue.3 , pp. 113-185
    • Cauwe, B.1    Steen, P.E.V.D.2    Opdenakker, G.3
  • 119
    • 0035479845 scopus 로고    scopus 로고
    • Matrix metalloproteinases: They're not just for matrix anymore!
    • DOI 10.1016/S0955-0674(00)00248-9
    • McCawley LJ, Matrisian LM (2001) Matrix metalloproteinases: they're not just for matrix anymore! Curr Opin Cell Biol 13:534-40 (Pubitemid 32817010)
    • (2001) Current Opinion in Cell Biology , vol.13 , Issue.5 , pp. 534-540
    • McCawley, L.J.1    Matrisian, L.M.2
  • 120
    • 4444304939 scopus 로고    scopus 로고
    • Regulation of matrix biology by matrix metalloproteinases
    • DOI 10.1016/j.ceb.2004.07.010, PII S0955067404001097
    • Mott JD, Werb Z (2004) Regulation of matrix biology by matrix metalloproteinases. Curr Opin Cell Biol 16:558-64 (Pubitemid 39201241)
    • (2004) Current Opinion in Cell Biology , vol.16 , Issue.5 , pp. 558-564
    • Mott, J.D.1    Werb, Z.2
  • 123
    • 0029069565 scopus 로고
    • Matrix metalloproteinases and processing of pro-TNF-alpha
    • Gearing AJ, Beckett P, Christodoulou M et al (1995) Matrix metalloproteinases and processing of pro-TNF-alpha. J Leukoc Biol 57:774-7
    • (1995) J Leukoc Biol , vol.57 , pp. 774-777
    • Gearing, A.J.1    Beckett, P.2    Christodoulou, M.3
  • 124
    • 44649155073 scopus 로고    scopus 로고
    • Disentanglement of protease substrate repertoires
    • DOI 10.1515/BC.2008.043
    • Van Damme P, Vandekerckhove J, Gevaert K (2008) Disentanglement of protease substrate repertoires. Biol Chem 389:371-81 (Pubitemid 351773913)
    • (2008) Biological Chemistry , vol.389 , Issue.4 , pp. 371-381
    • Van Damme, P.1    Vandekerckhove, J.2    Gevaert, K.3
  • 125
    • 77949730265 scopus 로고    scopus 로고
    • MS-driven protease substrate degradomics
    • Impens F, Colaert N, Helsens K et al (2010) MS-driven protease substrate degradomics. Proteomics 10:1284-96
    • (2010) Proteomics , vol.10 , pp. 1284-1296
    • Impens, F.1    Colaert, N.2    Helsens, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.