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Volumn 98, Issue 3, 2001, Pages 688-695

Transendothelial migration of lymphocytes across high endothelial venules into lymph nodes is affected by metalloproteinases

Author keywords

[No Author keywords available]

Indexed keywords

L SELECTIN; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE INHIBITOR; N1 [2,2 DIMETHYL 1 [(METHYLAMINO)CARBONYL]PROPYL] N4 HYDROXY 2 (2 METHYLPROPYL)BUTANEDIAMIDE;

EID: 0035437168     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.V98.3.688     Document Type: Article
Times cited : (109)

References (57)
  • 1
    • 0030001675 scopus 로고    scopus 로고
    • Lymphocyte homing and homeostasis
    • Butcher EC, Picker LJ. Lymphocyte homing and homeostasis. Science. 1996;272:60-66.
    • (1996) Science , vol.272 , pp. 60-66
    • Butcher, E.C.1    Picker, L.J.2
  • 2
    • 0000768235 scopus 로고
    • The route of recirculation of lymphocytes in the rat
    • Gowans JL, Knight EJ. The route of recirculation of lymphocytes in the rat. Proc Roy Soc Series B. 1964;159:257-282.
    • (1964) Proc Roy Soc Series B , vol.159 , pp. 257-282
    • Gowans, J.L.1    Knight, E.J.2
  • 3
    • 0031965102 scopus 로고    scopus 로고
    • Molecular mechanisms of lymphocyte homing to peripheral lymph nodes
    • Wamock RA, Askari S, Butcher EC, von Andrian UH. Molecular mechanisms of lymphocyte homing to peripheral lymph nodes. J Exp Med. 1998;187:205-216.
    • (1998) J Exp Med , vol.187 , pp. 205-216
    • Wamock, R.A.1    Askari, S.2    Butcher, E.C.3    Von Andrian, U.H.4
  • 4
    • 17144442408 scopus 로고    scopus 로고
    • The CC chemokine thymus-derived chemotactic agent 4 (TCA-4, secondary lymphoid tissue chemokine, 6Ckine, exodus-2) triggers lymphocyte function-associated antigen 1-mediated arrest of rolling T lymphocytes in peripheral lymph node high endothelial venules
    • Stein JV, Rot A, Luo Y, et al. The CC chemokine thymus-derived chemotactic agent 4 (TCA-4, secondary lymphoid tissue chemokine, 6Ckine, exodus-2) triggers lymphocyte function-associated antigen 1-mediated arrest of rolling T lymphocytes in peripheral lymph node high endothelial venules. J Exp Med 2000;191:61-76.
    • (2000) J Exp Med , vol.191 , pp. 61-76
    • Stein, J.V.1    Rot, A.2    Luo, Y.3
  • 5
    • 0033214348 scopus 로고    scopus 로고
    • CCR7 coordinates the primary immune response by establishing functional microenvironments in secondary lymphoid organs
    • Forster R, Schubel A, Breitfeld D, et al. CCR7 coordinates the primary immune response by establishing functional microenvironments in secondary lymphoid organs. Cell. 1999;99:23-33.
    • (1999) Cell , vol.99 , pp. 23-33
    • Forster, R.1    Schubel, A.2    Breitfeld, D.3
  • 6
    • 0022768886 scopus 로고
    • The structure of the basement membrane of human lymph node high endothelial venules: An ultrastructural, histochemical and immunocytochemical study
    • Freemont AJ, Stoddart RW, Steven F, Jones CJ, Matthews S. The structure of the basement membrane of human lymph node high endothelial venules: an ultrastructural, histochemical and immunocytochemical study. Histochem J. 1986;18:421-428.
    • (1986) Histochem J , vol.18 , pp. 421-428
    • Freemont, A.J.1    Stoddart, R.W.2    Steven, F.3    Jones, C.J.4    Matthews, S.5
  • 7
    • 0029153736 scopus 로고
    • High endothelial venules (HEVs): Specialized endothelium for lymphocyte migration
    • Girard JP, Springer TA. High endothelial venules (HEVs): specialized endothelium for lymphocyte migration. Immunol Today. 1995;16:449-457.
    • (1995) Immunol Today , vol.16 , pp. 449-457
    • Girard, J.P.1    Springer, T.A.2
  • 8
    • 0032493871 scopus 로고    scopus 로고
    • Requirement for specific proteases in cancer cell intravasation as revealed by a novel semiquantitative PCR-based assay
    • Kim J, Yu W, Kovalski K, Ossowski L. Requirement for specific proteases in cancer cell intravasation as revealed by a novel semiquantitative PCR-based assay. Cell. 1998;94:353-362.
    • (1998) Cell , vol.94 , pp. 353-362
    • Kim, J.1    Yu, W.2    Kovalski, K.3    Ossowski, L.4
  • 9
    • 0029041446 scopus 로고
    • T cell gelatinases mediate basement membrane transmigration in vitro
    • Leppert D, Waubant E, Galardy R, Bunnett NW, Hauser SL. T cell gelatinases mediate basement membrane transmigration in vitro. J Immunol. 1995;154:4379-4389.
    • (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
  • 11
    • 0034634006 scopus 로고    scopus 로고
    • Differential induction of gelatinase B (MMP-9) and gelatinase A (MMP-2) in T lymphocytes upon VLA-4 mediated adhesion to VCAM-1 and the CS-1 peptide of fibronectin
    • Yakubenko VP, Lobb RR, Plow EF, Ugarova TP. Differential induction of gelatinase B (MMP-9) and gelatinase A (MMP-2) in T lymphocytes upon VLA-4 mediated adhesion to VCAM-1 and the CS-1 peptide of fibronectin. Exp Cell Res. 2000;260:73-84.
    • (2000) Exp Cell Res , vol.260 , pp. 73-84
    • Yakubenko, V.P.1    Lobb, R.R.2    Plow, E.F.3    Ugarova, T.P.4
  • 12
    • 0028362088 scopus 로고
    • The induction of 72-kD gelatinase in T cells upon adhesion to endothelial cells is VCAM-1 dependent
    • Romanic AM, Madri JA. The induction of 72-kD gelatinase in T cells upon adhesion to endothelial cells is VCAM-1 dependent. J Cell Biol. 1994;125:1165-1178.
    • (1994) J Cell Biol , vol.125 , pp. 1165-1178
    • Romanic, A.M.1    Madri, J.A.2
  • 13
    • 0032883939 scopus 로고    scopus 로고
    • Fibronectin upregulates gelatinase B (MMP-9) and induces coordinated expression of gelatinase A (MMP-2) and its activator MT1-MMP (MMP-14) by human T lymphocyte cell lines. A process repressed through RAS/MAP kinase signaling pathways
    • Esparza J, Vilardell C, Calvo J, et al. Fibronectin upregulates gelatinase B (MMP-9) and induces coordinated expression of gelatinase A (MMP-2) and its activator MT1-MMP (MMP-14) by human T lymphocyte cell lines. A process repressed through RAS/MAP kinase signaling pathways. Blood. 1999;94:2754-2766.
    • (1999) Blood , vol.94 , pp. 2754-2766
    • Esparza, J.1    Vilardell, C.2    Calvo, J.3
  • 14
    • 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 EF, 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. 1998;160:2967-2973.
    • (1998) J Immunol , vol.160 , pp. 2967-2973
    • Aoudjit, F.1    Potworowski, E.F.2    St-Pierre, Y.3
  • 15
    • 0032515018 scopus 로고    scopus 로고
    • An essential role for ectodomain shedding in mammalian development
    • Peschon JJ, Slack JL, Reddy P, et al. An essential role for ectodomain shedding in mammalian development. Science. 1998;282:1281-1284.
    • (1998) Science , vol.282 , pp. 1281-1284
    • Peschon, J.J.1    Slack, J.L.2    Reddy, P.3
  • 16
    • 0033613949 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinases-3 inhibits shedding of L-selectin from leukocytes
    • Borland G, Murphy G, Ager A. Tissue inhibitor of metalloproteinases-3 inhibits shedding of L-selectin from leukocytes. J Biol Chem 1999;274:2810-2815.
    • (1999) J Biol Chem , vol.274 , pp. 2810-2815
    • Borland, G.1    Murphy, G.2    Ager, A.3
  • 17
    • 11544252167 scopus 로고    scopus 로고
    • Neutrophil rolling altered by inhibition of L-selectin shedding in vitro
    • Walcheck B, Kahn J, Fisher JM, et al. Neutrophil rolling altered by inhibition of L-selectin shedding in vitro. Nature. 1996;380:720-723.
    • (1996) Nature , vol.380 , pp. 720-723
    • Walcheck, B.1    Kahn, J.2    Fisher, J.M.3
  • 18
    • 0345196534 scopus 로고    scopus 로고
    • Relevance of L-selectin shedding for leukocyte rolling in vivo
    • Hafezi-Moghadam A, Ley K. Relevance of L-selectin shedding for leukocyte rolling in vivo. J Exp Med. 1999;189:939-948.
    • (1999) J Exp Med , vol.189 , pp. 939-948
    • Hafezi-Moghadam, A.1    Ley, K.2
  • 19
    • 0029022713 scopus 로고
    • Tissue inhibitors of matrix metalloendopeptidases
    • Murphy G, Willenbrock F. Tissue inhibitors of matrix metalloendopeptidases. Methods Enzymol. 1995;248:496-510.
    • (1995) Methods Enzymol , vol.248 , pp. 496-510
    • Murphy, G.1    Willenbrock, F.2
  • 20
    • 0030016342 scopus 로고    scopus 로고
    • The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation. Regulation by TIMP-2 and TIMP-3
    • Will H, Atkinson SJ, Butler GS, Smith B, Murphy G. The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation. Regulation by TIMP-2 and TIMP-3. J Biol Chem. 1996;271:17119-17123.
    • (1996) J Biol Chem , vol.271 , pp. 17119-17123
    • Will, H.1    Atkinson, S.J.2    Butler, G.S.3    Smith, B.4    Murphy, G.5
  • 21
    • 0034640282 scopus 로고    scopus 로고
    • Membrane type 4 matrix metalloproteinase (MMP17) has tumour necrosis factor-alpha convertase activity but does not activate pro-MMP2
    • English WR, Puente XS, Freije JMP, et al. Membrane type 4 matrix metalloproteinase (MMP17) has tumour necrosis factor-alpha convertase activity but does not activate pro-MMP2. J Biol Chem. 2000;275:14046-14055.
    • (2000) J Biol Chem , vol.275 , pp. 14046-14055
    • English, W.R.1    Puente, X.S.2    Freije, J.M.P.3
  • 22
    • 0032508675 scopus 로고    scopus 로고
    • TNF-alpha converting enzyme (TACE) is inhibited by TIMP-3
    • Amour A, Slocombe PM, Webster A, et al. TNF-alpha converting enzyme (TACE) is inhibited by TIMP-3. FEBS Lett. 1998;435:39-44.
    • (1998) FEBS Lett , vol.435 , pp. 39-44
    • Amour, A.1    Slocombe, P.M.2    Webster, A.3
  • 23
    • 0028969678 scopus 로고
    • The metzincins-topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases
    • Stocker W, Grams F, Baumann U, et al. The metzincins-topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases. Protein Sci. 1995;4:823-840.
    • (1995) Protein Sci , vol.4 , pp. 823-840
    • Stocker, W.1    Grams, F.2    Baumann, U.3
  • 25
    • 0029586589 scopus 로고
    • Matrix metalloproteinase inhibition: A review of anti-tumour activity
    • Brown PD, Giavazzi R. Matrix metalloproteinase inhibition: a review of anti-tumour activity. Ann Oncol. 1995;6:967-974.
    • (1995) Ann Oncol , vol.6 , pp. 967-974
    • Brown, P.D.1    Giavazzi, R.2
  • 26
    • 0029934985 scopus 로고    scopus 로고
    • Control of lymphatic and hematogenous metastasis of a rat mammary carcinoma by the matrix metalloproteinase inhibitor batimastat (BB-94)
    • Eccies SA, Box GM, Court WJ, Bone EA, Thomas W, Brown PD. Control of lymphatic and hematogenous metastasis of a rat mammary carcinoma by the matrix metalloproteinase inhibitor batimastat (BB-94). Cancer Res. 1996;56:2815-2282.
    • (1996) Cancer Res , vol.56 , pp. 2815-2282
    • Eccies, S.A.1    Box, G.M.2    Court, W.J.3    Bone, E.A.4    Thomas, W.5    Brown, P.D.6
  • 27
    • 0000278421 scopus 로고    scopus 로고
    • Differing effects of endogenous and synthetic inhibitors of metalloproteinases on intestinal tumorigenesis
    • Goss KJ, Brown PD, Matrisian LM. Differing effects of endogenous and synthetic inhibitors of metalloproteinases on intestinal tumorigenesis. Int J Cancer. 1998;78:629-635.
    • (1998) Int J Cancer , vol.78 , pp. 629-635
    • Goss, K.J.1    Brown, P.D.2    Matrisian, L.M.3
  • 28
    • 0030839472 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibition as a novel anticancer strategy: A review with special focus on batimastat and marimastat
    • Rasmussen HS, McCann PP. Matrix metalloproteinase inhibition as a novel anticancer strategy: a review with special focus on batimastat and marimastat. Pharmacol Ther. 1997;75:69-75.
    • (1997) Pharmacol Ther , vol.75 , pp. 69-75
    • Rasmussen, H.S.1    McCann, P.P.2
  • 29
    • 0033120966 scopus 로고    scopus 로고
    • Inhibition of matrix metalloproteinases prevents allergen-induced airway inflammation in a murine model of asthma
    • Kumagai K, Ohno I, Okada S, et al. Inhibition of matrix metalloproteinases prevents allergen-induced airway inflammation in a murine model of asthma. J Immunol. 1999;162:4212-4219.
    • (1999) J Immunol , vol.162 , pp. 4212-4219
    • Kumagai, K.1    Ohno, I.2    Okada, S.3
  • 30
    • 0025944065 scopus 로고
    • The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity
    • Murphy G, Houbrechts A, Cockett MI, Williamson RA, O'Shea M, Docherty AJ. The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity. Biochemistry. 1991;30:8097-8102.
    • (1991) Biochemistry , vol.30 , pp. 8097-8102
    • Murphy, G.1    Houbrechts, A.2    Cockett, M.I.3    Williamson, R.A.4    O'Shea, M.5    Docherty, A.J.6
  • 31
    • 17544382630 scopus 로고    scopus 로고
    • Metalloproteinase-mediated regulation of L-selectin levels on leucocytes
    • Preece G, Murphy G, Ager A. Metalloproteinase-mediated regulation of L-selectin levels on leucocytes. J Biol Chem. 1996;271:11634-11640.
    • (1996) J Biol Chem , vol.271 , pp. 11634-11640
    • Preece, G.1    Murphy, G.2    Ager, A.3
  • 32
    • 0018398672 scopus 로고
    • A continuous spectrophotometric assay for angiotensin converting enzyme
    • Holmquist B, Bunning P, Riordan JF. A continuous spectrophotometric assay for angiotensin converting enzyme. Analyt Biochem. 1979;95:540-548.
    • (1979) Analyt Biochem , vol.95 , pp. 540-548
    • Holmquist, B.1    Bunning, P.2    Riordan, J.F.3
  • 33
    • 0025153163 scopus 로고
    • New fluorescent dyes for lymphocyte migration studies. Analysis by flow cytometry and fluorescence microscopy
    • Weston SA, Parish CR. New fluorescent dyes for lymphocyte migration studies. Analysis by flow cytometry and fluorescence microscopy. J Immunol Methods. 1990;133:87-97.
    • (1990) J Immunol Methods , vol.133 , pp. 87-97
    • Weston, S.A.1    Parish, C.R.2
  • 34
    • 0033216536 scopus 로고    scopus 로고
    • Laminin and beta1 integrins are crucial for normal mammary gland development in the mouse
    • Klinowska TC, Soriano JV, Edwards GM, et al. Laminin and beta1 integrins are crucial for normal mammary gland development in the mouse. Dev Biol. 1999;215:13-32.
    • (1999) Dev Biol , vol.215 , pp. 13-32
    • Klinowska, T.C.1    Soriano, J.V.2    Edwards, G.M.3
  • 35
    • 0026674635 scopus 로고
    • Sialoadhesin on macrophages: Its identification as a lymphocyte adhesion molecule
    • van den Berg TK, Breve JJ, Damoiseaux JG, et al. Sialoadhesin on macrophages: its identification as a lymphocyte adhesion molecule. J Exp Med. 1992;176:647-655.
    • (1992) J Exp Med , vol.176 , pp. 647-655
    • Van den Berg, T.K.1    Breve, J.J.2    Damoiseaux, J.G.3
  • 36
    • 0030896096 scopus 로고    scopus 로고
    • Inhibition of bovine nasal cartilage degradation by selective matrix metalloproteinase inhibitors
    • Bottomley KM, Borkakoti N, Bradshaw D, et al. Inhibition of bovine nasal cartilage degradation by selective matrix metalloproteinase inhibitors. Biochem J. 1997;323:483-488.
    • (1997) Biochem J , vol.323 , pp. 483-488
    • Bottomley, K.M.1    Borkakoti, N.2    Bradshaw, D.3
  • 37
    • 0032499266 scopus 로고    scopus 로고
    • Inhibition of membrane-type 1 matrix metalloproteinase by hydroxamate inhibitors: An examination of the subsite pocket
    • Yamamoto M, Tsujishita H, Hori N, et al. Inhibition of membrane-type 1 matrix metalloproteinase by hydroxamate inhibitors: an examination of the subsite pocket. J Med Chem. 1998;41:1209-1217.
    • (1998) J Med Chem , vol.41 , pp. 1209-1217
    • Yamamoto, M.1    Tsujishita, H.2    Hori, N.3
  • 38
    • 0029616228 scopus 로고
    • Homing of lymphocytes into islets of Langerhans in prediabetic non-obese diabetic mice is not restricted to autoreactive T cells
    • Faveeuw C, Gagnerault MC, Kraal G, Lepault F. Homing of lymphocytes into islets of Langerhans in prediabetic non-obese diabetic mice is not restricted to autoreactive T cells. Int Immunol. 1995;7:1905-1913.
    • (1995) Int Immunol , vol.7 , pp. 1905-1913
    • Faveeuw, C.1    Gagnerault, M.C.2    Kraal, G.3    Lepault, F.4
  • 39
    • 0032820124 scopus 로고    scopus 로고
    • Painful stimulation suppresses joint inflammation by inducing shedding of L-selectin from neutrophils
    • Strausbaugh HJ, Green PG, Lo E, et al. Painful stimulation suppresses joint inflammation by inducing shedding of L-selectin from neutrophils. Nat Med. 1999;5:1057-1061.
    • (1999) Nat Med , vol.5 , pp. 1057-1061
    • Strausbaugh, H.J.1    Green, P.G.2    Lo, E.3
  • 40
    • 0032524941 scopus 로고    scopus 로고
    • Intrinsic differences in L-selectin expression levels affect T and B lymphocyte subset-specific recirculation pathways
    • Tang ML, Steeber DA, Zhang XQ, Tedder TF. Intrinsic differences in L-selectin expression levels affect T and B lymphocyte subset-specific recirculation pathways. J Immunol. 1998;160:5113-5121.
    • (1998) J Immunol , vol.160 , pp. 5113-5121
    • Tang, M.L.1    Steeber, D.A.2    Zhang, X.Q.3    Tedder, T.F.4
  • 41
    • 0024109988 scopus 로고
    • Immunohistologic and functional characterization of a vascular addressin involved in lymphocyte homing into peripheral lymph nodes
    • Streeter PR, Rouse BT, Butcher EC. Immunohistologic and functional characterization of a vascular addressin involved in lymphocyte homing into peripheral lymph nodes. J Cell Biol. 1988;107:1853-1862.
    • (1988) J Cell Biol , vol.107 , pp. 1853-1862
    • Streeter, P.R.1    Rouse, B.T.2    Butcher, E.C.3
  • 42
    • 78651149825 scopus 로고
    • The migration of lymphocytes through the endothelium of venules in lymph nodes: An electron microscope study
    • Marchesi VT, Gowans JL. The migration of lymphocytes through the endothelium of venules in lymph nodes: an electron microscope study. Proc Roy Soc Series B. 1964;159:283-290.
    • (1964) Proc Roy Soc Series B , vol.159 , pp. 283-290
    • Marchesi, V.T.1    Gowans, J.L.2
  • 43
    • 0033832622 scopus 로고    scopus 로고
    • Design and synthesis of acidic dipeptide hydroxamate inhibitors of procollagen C-proteinase
    • Ovens A, Joule JA, Kadler KE. Design and synthesis of acidic dipeptide hydroxamate inhibitors of procollagen C-proteinase. J Peptide Sci. 2000;6:489-495.
    • (2000) J Peptide Sci , vol.6 , pp. 489-495
    • Ovens, A.1    Joule, J.A.2    Kadler, K.E.3
  • 44
    • 0026599715 scopus 로고
    • Metalloproteinases mediate extracellular matrix degradation by cells from mouse blastocyst outgrowths
    • Behrendtsen O, Alexander CM, Werb Z. Metalloproteinases mediate extracellular matrix degradation by cells from mouse blastocyst outgrowths. Development. 1992;114:447-456.
    • (1992) Development , vol.114 , pp. 447-456
    • Behrendtsen, O.1    Alexander, C.M.2    Werb, Z.3
  • 45
    • 0022969477 scopus 로고
    • Tumor invasion through the human amniotic membrane: Requirement for a proteinase cascade
    • Mignatti P, Robbins E, Rifkin DB. Tumor invasion through the human amniotic membrane: requirement for a proteinase cascade. Cell. 1986;47:487-498.
    • (1986) Cell , vol.47 , pp. 487-498
    • Mignatti, P.1    Robbins, E.2    Rifkin, D.B.3
  • 46
    • 0023696675 scopus 로고
    • Inhibition by human recombinant tissue inhibitor of metalloproteinases of human amnion invasion and lung colonization by murine B16-F10 melanoma cells
    • Schultz RM, Silberman S, Persky B, Bajkowski AS, Carmichael DF. Inhibition by human recombinant tissue inhibitor of metalloproteinases of human amnion invasion and lung colonization by murine B16-F10 melanoma cells. Cancer Res. 1988;48:5539-5545.
    • (1988) Cancer Res , vol.48 , pp. 5539-5545
    • Schultz, R.M.1    Silberman, S.2    Persky, B.3    Bajkowski, A.S.4    Carmichael, D.F.5
  • 47
    • 0034703180 scopus 로고    scopus 로고
    • Distinct roles for matrix metalloproteinase-2 and alpha4 integrin in autoimmune T cell extravasation and residency in brain parenchyma during experimental autoimmune encephalomyelitis
    • Graesser D, Mahooti S, Madri JA. Distinct roles for matrix metalloproteinase-2 and alpha4 integrin in autoimmune T cell extravasation and residency in brain parenchyma during experimental autoimmune encephalomyelitis. J Neuroimmunol. 2000;109:121-131.
    • (2000) J Neuroimmunol , vol.109 , pp. 121-131
    • Graesser, D.1    Mahooti, S.2    Madri, J.A.3
  • 48
    • 0031596366 scopus 로고    scopus 로고
    • The interrelationship of alpha4 integrin and matrix metalloproteinase-2 in the pathogenesis of experimental autoimmune encephalomyelitis
    • Graesser D, Mahooti S, Haas T, Davis S, Clark RB, Madri JA. The interrelationship of alpha4 integrin and matrix metalloproteinase-2 in the pathogenesis of experimental autoimmune encephalomyelitis. Lab Invest. 1998;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
  • 49
    • 0020580587 scopus 로고
    • The recirculating lymphocyte pool of the rat: A systematic description of the migratory behaviour of recirculating lymphocytes
    • Smith ME, Ford WL. The recirculating lymphocyte pool of the rat: a systematic description of the migratory behaviour of recirculating lymphocytes. Immunology. 1983;49:83-94.
    • (1983) Immunology , vol.49 , pp. 83-94
    • Smith, M.E.1    Ford, W.L.2
  • 50
    • 0021058847 scopus 로고
    • Intercellular contacts of lymphocytes during migration across high-endothelial venules of lymph nodes. An electron microscopic study
    • Campbell FR. Intercellular contacts of lymphocytes during migration across high-endothelial venules of lymph nodes. An electron microscopic study. Anat Rec. 1983;207:643-652.
    • (1983) Anat Rec , vol.207 , pp. 643-652
    • Campbell, F.R.1
  • 51
    • 0030671306 scopus 로고    scopus 로고
    • Production of a DPP activity gradient in the early Drosophila embryo through the opposing actions of the SOG and TLD proteins
    • Marques G, Musacchio M, Shimell MJ, Wunnenberg-Stapleton K, Cho KW, O'Connor MB. Production of a DPP activity gradient in the early Drosophila embryo through the opposing actions of the SOG and TLD proteins. Cell. 1997;91:417-426.
    • (1997) Cell , vol.91 , pp. 417-426
    • Marques, G.1    Musacchio, M.2    Shimell, M.J.3    Wunnenberg-Stapleton, K.4    Cho, K.W.5    O'Connor, M.B.6
  • 52
    • 0034627829 scopus 로고    scopus 로고
    • Monocytes induce reversible focal changes in vascular endothelial cadherin complex during transendothelial migration under flow
    • Allport JR, Muller WA, Luscinskas FW. Monocytes induce reversible focal changes in vascular endothelial cadherin complex during transendothelial migration under flow. J Cell Biol. 2000;148:203-216.
    • (2000) J Cell Biol , vol.148 , pp. 203-216
    • Allport, J.R.1    Muller, W.A.2    Luscinskas, F.W.3
  • 53
    • 0030806173 scopus 로고    scopus 로고
    • Changing views of the role of matrix metalloproteinases in metastasis
    • Chambers AF, Matrisian LM. Changing views of the role of matrix metalloproteinases in metastasis. J Natl Cancer Inst. 1997;89:1260-1270.
    • (1997) J Natl Cancer Inst , vol.89 , pp. 1260-1270
    • Chambers, A.F.1    Matrisian, L.M.2
  • 54
    • 0028140295 scopus 로고
    • Suppression of the tumorigenic and metastatic abilities of murine B16-F10 melanoma cells in vivo by the overexpression of the tissue inhibitor of the metalloproteinases-1
    • Khokha R. Suppression of the tumorigenic and metastatic abilities of murine B16-F10 melanoma cells in vivo by the overexpression of the tissue inhibitor of the metalloproteinases-1. J Natl Cancer Inst. 1994;86:299-304.
    • (1994) J Natl Cancer Inst , vol.86 , pp. 299-304
    • Khokha, R.1
  • 55
    • 0026499369 scopus 로고
    • Upregulation of TIMP1 expression in B16-F10 melanoma cells suppresses their metastatic ability in chick embryo
    • Khokha R, Zimmer MJ, Wilson SM, Chambers AF. Upregulation of TIMP1 expression in B16-F10 melanoma cells suppresses their metastatic ability in chick embryo. Clin Exp Metastasis. 1992;10:365-370.
    • (1992) Clin Exp Metastasis , vol.10 , pp. 365-370
    • Khokha, R.1    Zimmer, M.J.2    Wilson, S.M.3    Chambers, A.F.4
  • 56
    • 0028129494 scopus 로고
    • Overexpression of metalloproteinase inhibitor in B16F10 cells does not affect extravasation but reduces tumor growth
    • Koop S, Khokha R, Schmidt EE, et al. Overexpression of metalloproteinase inhibitor in B16F10 cells does not affect extravasation but reduces tumor growth. Cancer Res. 1994;54:4791-4797.
    • (1994) Cancer Res , vol.54 , pp. 4791-4797
    • Koop, S.1    Khokha, R.2    Schmidt, E.E.3
  • 57
    • 0032782424 scopus 로고    scopus 로고
    • The matrix metalloproteinase inhibitor batimastat inhibits angiognesis in liver metastases of B16F1 melanoma cells
    • Wylie S, MacDonald IC, Varghese HJ. The matrix metalloproteinase inhibitor batimastat inhibits angiognesis in liver metastases of B16F1 melanoma cells. Clin Exp Metastasis. 1999;17:111-117.
    • (1999) Clin Exp Metastasis , vol.17 , pp. 111-117
    • Wylie, S.1    MacDonald, I.C.2    Varghese, H.J.3


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