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Volumn 70, Issue 17, 2010, Pages 6978-6987

Matrix metalloproteinase-9 is upregulated in nucleophosmin-anaplastic lymphoma kinase-positive anaplastic lymphomas and activated at the cell surface by the chaperone heat shock protein 90 to promote cell invasion

Author keywords

[No Author keywords available]

Indexed keywords

ANAPLASTIC LYMPHOMA KINASE; ENZYME ANTIBODY; GELATINASE B; HEAT SHOCK PROTEIN 90; HERMES ANTIGEN; ILOMASTAT; NUCLEOPHOSMIN; RAC1 PROTEIN; CD44 PROTEIN, HUMAN; DIPEPTIDE; ENZYME PRECURSOR; MATRIX METALLOPROTEINASE INHIBITOR; N-(2(R)-2-(HYDROXAMIDOCARBONYLMETHYL)-4-METHYLPENTANOYL)-L-TRYPTOPHAN METHYLAMIDE; P80(NPM-ALK) PROTEIN; PRO-MATRIX METALLOPROTEINASE 9; PROTEIN TYROSINE KINASE; RAC1 PROTEIN, HUMAN;

EID: 77956294299     PISSN: 00085472     EISSN: 15387445     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-10-0861     Document Type: Article
Times cited : (48)

References (44)
  • 1
    • 0030034745 scopus 로고    scopus 로고
    • High incidence of the t(2;5) (p23;q35) translocation in anaplastic large cell lymphoma and its lack of detection in Hodgkin's disease. Comparison of cytogenetic analysis, reverse transcriptase-polymerase chain reaction, and P-80 immunostaining
    • Lamant L, Meggetto F, al Saati T, et al. High incidence of the t(2;5) (p23;q35) translocation in anaplastic large cell lymphoma and its lack of detection in Hodgkin's disease. Comparison of cytogenetic analysis, reverse transcriptase-polymerase chain reaction, and P-80 immunostaining. Blood 1996;87:284-91.
    • (1996) Blood , vol.87 , pp. 284-291
    • Lamant, L.1    Meggetto, F.2    Al Saati, T.3
  • 2
    • 77956280939 scopus 로고    scopus 로고
    • What have we learnt from mouse models of NPM-ALK-induced lymphomagenesis?
    • Turner SD, Alexander DR. What have we learnt from mouse models of NPM-ALK-induced lymphomagenesis? Leukemia 2005;20:572-82.
    • (2005) Leukemia , vol.20 , pp. 572-582
    • Turner, S.D.1    Alexander, D.R.2
  • 3
    • 33744503924 scopus 로고    scopus 로고
    • Proteomic analysis of anaplastic lymphoma cell lines: Identification of potential tumour markers
    • Cussac D, Pichereaux C, Colomba A, et al. Proteomic analysis of anaplastic lymphoma cell lines: identification of potential tumour markers. Proteomics 2006;6:3210-22.
    • (2006) Proteomics , vol.6 , pp. 3210-3222
    • Cussac, D.1    Pichereaux, C.2    Colomba, A.3
  • 4
    • 2342516776 scopus 로고    scopus 로고
    • Identification of NPM-ALK interacting proteins by tandem mass spectrometry
    • Crockett DK, Lin Z, Elenitoba-Johnson KS, Lim MS. Identification of NPM-ALK interacting proteins by tandem mass spectrometry. Oncogene 2004;23:2617-29.
    • (2004) Oncogene , vol.23 , pp. 2617-2629
    • Crockett, D.K.1    Lin, Z.2    Elenitoba-Johnson, K.S.3    Lim, M.S.4
  • 6
    • 34948834758 scopus 로고    scopus 로고
    • + anaplastic large-cell lymphoma
    • + anaplastic large-cell lymphoma. Blood 2007;110:2259-67.
    • (2007) Blood , vol.110 , pp. 2259-2267
    • Amin, H.M.1    Lai, R.2
  • 7
    • 28444462500 scopus 로고    scopus 로고
    • P130Cas mediates the transforming properties of the anaplastic lymphoma kinase
    • Ambrogio C, Voena C, Manazza AD, et al. p130Cas mediates the transforming properties of the anaplastic lymphoma kinase. Blood 2005;106:3907-16.
    • (2005) Blood , vol.106 , pp. 3907-3916
    • Ambrogio, C.1    Voena, C.2    Manazza, A.D.3
  • 8
    • 42549168106 scopus 로고    scopus 로고
    • Activation of Rac1 and the exchange factor Vav3 are involved in NPM-ALK signaling in anaplastic large cell lymphomas
    • Colomba A, Courilleau D, Ramel D, et al. Activation of Rac1 and the exchange factor Vav3 are involved in NPM-ALK signaling in anaplastic large cell lymphomas. Oncogene 2008;27:2728-36.
    • (2008) Oncogene , vol.27 , pp. 2728-2736
    • Colomba, A.1    Courilleau, D.2    Ramel, D.3
  • 9
    • 4444319567 scopus 로고    scopus 로고
    • Differential effects of X-ALK fusion proteins on proliferation, transformation, and invasion properties of NIH3T3 cells
    • Armstrong F, Duplantier MM, Trempat P, et al. Differential effects of X-ALK fusion proteins on proliferation, transformation, and invasion properties of NIH3T3 cells. Oncogene 2004;23:6071-82.
    • (2004) Oncogene , vol.23 , pp. 6071-6082
    • Armstrong, F.1    Duplantier, M.M.2    Trempat, P.3
  • 10
    • 0842264006 scopus 로고    scopus 로고
    • Nucleophosmin-anaplastic lymphoma kinase of anaplastic large-cell lymphoma recruits, activates, and uses pp60c-src to mediate its mitogenicity
    • Cussac D, Greenland C, Roche S, et al. Nucleophosmin-anaplastic lymphoma kinase of anaplastic large-cell lymphoma recruits, activates, and uses pp60c-src to mediate its mitogenicity. Blood 2004; 103:1464-71.
    • (2004) Blood , vol.103 , pp. 1464-1471
    • Cussac, D.1    Greenland, C.2    Roche, S.3
  • 12
    • 0038575443 scopus 로고    scopus 로고
    • Extracellular matrix remodelling: The role of matrix metalloproteinases
    • Stamenkovic I. Extracellular matrix remodelling: the role of matrix metalloproteinases. J Pathol 2003;200:448-64.
    • (2003) J Pathol , vol.200 , pp. 448-464
    • Stamenkovic, I.1
  • 13
    • 0035479845 scopus 로고    scopus 로고
    • Matrix metalloproteinases: They're not for matrix anymore!
    • McCawley LJ, Matrisian LM. Matrix metalloproteinases: they're not for matrix anymore!. Curr Opin Cell Biol 2001;13:534-40.
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 534-540
    • McCawley, L.J.1    Matrisian, L.M.2
  • 14
    • 19344366798 scopus 로고    scopus 로고
    • Gelatinase-mediated migration and invasion of cancer cells
    • Björklund M, Koivunen E. Gelatinase-mediated migration and invasion of cancer cells. Biochim Biophys Acta 2005;1755:37-69.
    • (2005) Biochim Biophys Acta , vol.1755 , pp. 37-69
    • Björklund, M.1    Koivunen, E.2
  • 15
    • 6344261567 scopus 로고    scopus 로고
    • The membrane form of the DNA repair protein Ku interacts at the cell surface with metalloproteinase 9
    • Monferran S, Paupert J, Dauvillier S, Salles B, Muller C. The membrane form of the DNA repair protein Ku interacts at the cell surface with metalloproteinase 9. EMBO J 2004;23:3758-68.
    • (2004) EMBO J , vol.23 , pp. 3758-3768
    • Monferran, S.1    Paupert, J.2    Dauvillier, S.3    Salles, B.4    Muller, C.5
  • 16
    • 47249093296 scopus 로고    scopus 로고
    • 1 Integrin and 190-kDa CD44v constitute a cell surface docking complex for gelatinase B/MMP-9 in chronic leukemic but not normal B cells
    • 1 Integrin and 190-kDa CD44v constitute a cell surface docking complex for gelatinase B/MMP-9 in chronic leukemic but not normal B cells. Blood 2008;112:169-78.
    • (2008) Blood , vol.112 , pp. 169-178
    • Redondo-Munoz, J.1    Ugarte-Berzal, E.2    Garcia-Marco, J.A.3
  • 17
    • 43549115238 scopus 로고    scopus 로고
    • Cell-surface MMP-9 regulates the invasive capacity of leukemia blast cells with monocytic features
    • Paupert J, Mansat-De Mas V, Demur C, Salles B, Muller C. Cell-surface MMP-9 regulates the invasive capacity of leukemia blast cells with monocytic features. Cell Cycle 2008;7:1047-53.
    • (2008) Cell Cycle , vol.7 , pp. 1047-1053
    • Paupert, J.1    Mansat-De Mas, V.2    Demur, C.3    Salles, B.4    Muller, C.5
  • 18
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • Egebald M, Werb Z. New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer 2002;2:161-74.
    • (2002) Nat Rev Cancer , vol.2 , pp. 161-174
    • Egebald, M.1    Werb, Z.2
  • 19
    • 0033567964 scopus 로고    scopus 로고
    • Interleukine-6 regulation of matrix mettalloproteinase (MMP-2 and MMP-9) and tissue inhibitors of metalloproteinase (TIMP-1) expression in malignant non-Hodgkin's lymphomas
    • Kossakowska AE, Edwards DR, Prusinkiewicz C, Zhang MC, Guo D, Urbanski SJ. Interleukine-6 regulation of matrix mettalloproteinase (MMP-2 and MMP-9) and tissue inhibitors of metalloproteinase (TIMP-1) expression in malignant non-Hodgkin's lymphomas. Blood 1999;94:2080-89.
    • (1999) Blood , vol.94 , pp. 2080-2089
    • Kossakowska, A.E.1    Edwards, D.R.2    Prusinkiewicz, C.3    Zhang, M.C.4    Guo, D.5    Urbanski, S.J.6
  • 20
    • 0036105592 scopus 로고    scopus 로고
    • Production of matrix metalloproteinase-9 in early stage B-CLL: Suppression by interferons
    • Bauvois B, Dumont J, Mathiot C, Kolb JP. Production of matrix metalloproteinase-9 in early stage B-CLL: suppression by interferons. Leukemia 2002;16:791-98.
    • (2002) Leukemia , vol.16 , pp. 791-798
    • Bauvois, B.1    Dumont, J.2    Mathiot, C.3    Kolb, J.P.4
  • 21
    • 58549119944 scopus 로고    scopus 로고
    • Secretion of MMP-2 and MMP- 9 induced VEGF autocrine loop correlates with clinical features in childhood acute lymphoblastic leukemia
    • Poyer F, Coquerel B, Pegahi R, et al. Secretion of MMP-2 and MMP- 9 induced VEGF autocrine loop correlates with clinical features in childhood acute lymphoblastic leukemia. Leuk Res 2009;33:407-17.
    • (2009) Leuk Res , vol.33 , pp. 407-417
    • Poyer, F.1    Coquerel, B.2    Pegahi, R.3
  • 22
    • 6344278652 scopus 로고    scopus 로고
    • Establishment of a novel anaplastic large-cell lymphoma-cell line (COST) from a "small-cell variant" of ALCL
    • Lamant L, Espinos E, Duplantier M, et al. Establishment of a novel anaplastic large-cell lymphoma-cell line (COST) from a "small-cell variant" of ALCL. Leukemia 2004;18:1693-98.
    • (2004) Leukemia , vol.18 , pp. 1693-1698
    • Lamant, L.1    Espinos, E.2    Duplantier, M.3
  • 23
    • 33646540436 scopus 로고    scopus 로고
    • SHP1 tyrosine phosphatase negatively regulates NPM-ALK tyrosine kinase signaling
    • Honorat JF, Ragab A, Lamant L, Delsol G, Ragab-Thomas J. SHP1 tyrosine phosphatase negatively regulates NPM-ALK tyrosine kinase signaling. Blood 2006;107:4130-38.
    • (2006) Blood , vol.107 , pp. 4130-4138
    • Honorat, J.F.1    Ragab, A.2    Lamant, L.3    Delsol, G.4    Ragab-Thomas, J.5
  • 24
    • 0035227262 scopus 로고    scopus 로고
    • Invadopodia: Unique methods for measurement of extracellular matrix degradation in vitro
    • Bowden ET, Coopman PJ, Mueller SC. Invadopodia: unique methods for measurement of extracellular matrix degradation in vitro. Methods Cell Biol 2001;63:613-27.
    • (2001) Methods Cell Biol , vol.63 , pp. 613-627
    • Bowden, E.T.1    Coopman, P.J.2    Mueller, S.C.3
  • 25
    • 22644439354 scopus 로고    scopus 로고
    • TIMP-1 expression in anaplastic large cell lymphoma is usually restricted to macrophages and only seldom observed in tumoral cells
    • Rust R, Blokzijl T, Harms G, et al. TIMP-1 expression in anaplastic large cell lymphoma is usually restricted to macrophages and only seldom observed in tumoral cells. J Pathol 2005;206:445-50.
    • (2005) J Pathol , vol.206 , pp. 445-450
    • Rust, R.1    Blokzijl, T.2    Harms, G.3
  • 27
    • 0032926177 scopus 로고    scopus 로고
    • Localization of matrix metalloproteinase 9 to the cell surface provides a mechanism for CD44-mediated tumor invasion
    • Yu A, Stamenkovic I. Localization of matrix metalloproteinase 9 to the cell surface provides a mechanism for CD44-mediated tumor invasion. Genes Dev 1999;13:35-48.
    • (1999) Genes Dev , vol.13 , pp. 35-48
    • Yu, A.1    Stamenkovic, I.2
  • 28
    • 33847343034 scopus 로고    scopus 로고
    • The matrix corroded: Podosomes and invadopodia in extracellular matrix degradation
    • Linder S. The matrix corroded: podosomes and invadopodia in extracellular matrix degradation. Trends Cell Biol 2007;17:107-17.
    • (2007) Trends Cell Biol , vol.17 , pp. 107-117
    • Linder, S.1
  • 29
    • 2442664118 scopus 로고    scopus 로고
    • Rational design and characterization of a Rac GTPase-specific small molecule inhibitor
    • Gao Y, Dickerson JB, Guo F, Zheng J, Zheng Y. Rational design and characterization of a Rac GTPase-specific small molecule inhibitor. Proc Natl Acad Sci U S A 2004;101:7618-23.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 7618-7623
    • Gao, Y.1    Dickerson, J.B.2    Guo, F.3    Zheng, J.4    Zheng, Y.5
  • 30
    • 2942716692 scopus 로고    scopus 로고
    • Functional proteomic screens reveal an essential extracellular role for hsp90α in cancer cell invasiveness
    • Eustace BD, Sakurai T, Stewart JK, et al. Functional proteomic screens reveal an essential extracellular role for hsp90α in cancer cell invasiveness. Nat Cell Biol 2004;6:507-14.
    • (2004) Nat Cell Biol , vol.6 , pp. 507-514
    • Eustace, B.D.1    Sakurai, T.2    Stewart, J.K.3
  • 31
    • 0036494113 scopus 로고    scopus 로고
    • Nucleophosmin-anaplastic lymphoma kinase (NPM-ALK), a novel Hsp90-client tyrosine kinase: Down-regulation of NPM-ALK expression and tyrosine phosphorylation in ALK(+) CD30(+) lymphoma cells by the Hsp90 antagonist 17-allylamino,17-demethoxygeldanamycin
    • Bonvini P, Gastaldi T, Falini B, Rosolen A. Nucleophosmin-anaplastic lymphoma kinase (NPM-ALK), a novel Hsp90-client tyrosine kinase: down-regulation of NPM-ALK expression and tyrosine phosphorylation in ALK(+) CD30(+) lymphoma cells by the Hsp90 antagonist 17-allylamino,17-demethoxygeldanamycin. Cancer Res 2002;62: 1559-66.
    • (2002) Cancer Res , vol.62 , pp. 1559-1566
    • Bonvini, P.1    Gastaldi, T.2    Falini, B.3    Rosolen, A.4
  • 32
    • 0141484615 scopus 로고    scopus 로고
    • A high-affinity conformation of hsp90 confers tumour selectivity on Hsp90 inhibitors
    • Kamal A, Thao L, Sensintaffar J, et al. A high-affinity conformation of hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature 2003; 425:407-10.
    • (2003) Nature , vol.425 , pp. 407-410
    • Kamal, A.1    Thao, L.2    Sensintaffar, J.3
  • 33
  • 34
    • 0031028979 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases in reactive and neoplastic lymphoid cells
    • Stetler-Stevenson M, Mansoor A, Lim M, et al. Expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases in reactive and neoplastic lymphoid cells. Blood 1997;89:1708-15.
    • (1997) Blood , vol.89 , pp. 1708-1715
    • Stetler-Stevenson, M.1    Mansoor, A.2    Lim, M.3
  • 36
    • 2042545418 scopus 로고    scopus 로고
    • The role of matrix metalloproteinase 9 in the pathogenesis of chronic lymphocytic leukaemia
    • Kamiguti AS, Lee ES, Till KJ, et al. The role of matrix metalloproteinase 9 in the pathogenesis of chronic lymphocytic leukaemia. Br J Haematol 2004;125:128-40.
    • (2004) Br J Haematol , vol.125 , pp. 128-140
    • Kamiguti, A.S.1    Lee, E.S.2    Till, K.J.3
  • 37
    • 0024538886 scopus 로고
    • Expression of lymphocyte homing receptor as a mechanism of dissemination in non-Hodgkin's lymphoma
    • Pals ST, Horst E, Ossekoppele GJ, Figdor CG, Scheper RJ, Meijer CJLM. Expression of lymphocyte homing receptor as a mechanism of dissemination in non-Hodgkin's lymphoma. Blood 1989; 73:885-88.
    • (1989) Blood , vol.73 , pp. 885-888
    • Pals, S.T.1    Horst, E.2    Ossekoppele, G.J.3    Figdor, C.G.4    Scheper, R.J.5    Meijer, C.J.L.M.6
  • 38
    • 0025004303 scopus 로고
    • Adhesion molecules in the prognosis of diffuse large-cell lymphoma: Expression of a lymphocyte homing receptor (CD44), LFA-1 (CD11a/18), and ICAM-1 (CD54)
    • Horst E, Meijer CJ, Radaszkiewicz T, Ossekoppele GJ, Van Krieken JH, Pals ST. Adhesion molecules in the prognosis of diffuse large-cell lymphoma: expression of a lymphocyte homing receptor (CD44), LFA-1 (CD11a/18), and ICAM-1 (CD54). Leukemia 1990;4:595-99.
    • (1990) Leukemia , vol.4 , pp. 595-599
    • Horst, E.1    Meijer, C.J.2    Radaszkiewicz, T.3    Ossekoppele, G.J.4    Van Krieken, J.H.5    Pals, S.T.6
  • 39
    • 0034650486 scopus 로고    scopus 로고
    • Cell surface-localized matrix metalloproteinase- 9 proteolytically activates TGF-β and promotes tumor invasion and angiogenesis
    • Yu Q, Stamenkovic I. Cell surface-localized matrix metalloproteinase- 9 proteolytically activates TGF-β and promotes tumor invasion and angiogenesis. Genes Dev 2000;14:163-76.
    • (2000) Genes Dev , vol.14 , pp. 163-176
    • Yu, Q.1    Stamenkovic, I.2
  • 40
    • 55349097094 scopus 로고    scopus 로고
    • The anaplastic lymphoma kinase controls cell shape and growth of anaplastic large cell lymphoma through Cdc42 activation
    • Ambrogio C, Voena C, Manazza AD, et al. The anaplastic lymphoma kinase controls cell shape and growth of anaplastic large cell lymphoma through Cdc42 activation. Cancer Res 2008;68: 8899-907.
    • (2008) Cancer Res , vol.68 , pp. 8899-8907
    • Ambrogio, C.1    Voena, C.2    Manazza, A.D.3
  • 41
    • 0038556694 scopus 로고    scopus 로고
    • Tumor progression: Small GTPases and loss of cell-cell adhesion
    • Lozano E, Betson M, Braga VM. Tumor progression: small GTPases and loss of cell-cell adhesion. BioEssays 2003;25:452-63.
    • (2003) BioEssays , vol.25 , pp. 452-463
    • Lozano, E.1    Betson, M.2    Braga, V.M.3
  • 42
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPases in cell biology
    • Etienne-Maneville S, Hall A. Rho GTPases in cell biology. Nature 2002;420:629-35.
    • (2002) Nature , vol.420 , pp. 629-635
    • Etienne-Maneville, S.1    Hall, A.2
  • 43
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • Whitesell L, Lindquist SL. HSP90 and the chaperoning of cancer. Nat Rev Cancer 2005;5:761-72.
    • (2005) Nat Rev Cancer , vol.5 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 44
    • 49649108912 scopus 로고    scopus 로고
    • Role of acetylation and extracellular location of heat shock protein 90aα in tumor cell invasion
    • Yang Y, Rao R, Shen J, et al. Role of acetylation and extracellular location of heat shock protein 90aα in tumor cell invasion. Cancer Res 2008;68:4833-42.
    • (2008) Cancer Res , vol.68 , pp. 4833-4842
    • Yang, Y.1    Rao, R.2    Shen, J.3


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