메뉴 건너뛰기




Volumn 3, Issue 3, 2010, Pages 288-302

Culture of K562 human myeloid leukemia cells in presence of fibronectin expresses and secretes MMP-9 in serum free culture medium

Author keywords

5 1 integrin; FAK; Fibronectin; MMP 9; NF B

Indexed keywords

FIBRONECTIN; FOCAL ADHESION KINASE; GELATINASE B; INTEGRIN; LAMININ; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATIDYLINOSITOL 3 KINASE; TISSUE INHIBITOR OF METALLOPROTEINASE 1;

EID: 77953473407     PISSN: None     EISSN: 19362625     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (15)

References (39)
  • 2
    • 0028987190 scopus 로고
    • Cooperative signaling by alpha 5 beta 1 and alpha 4 beta 1 integrins regulates metalloproteinase gene expression in fibroblasts adhering to fibronectin
    • Huhtala P, Humphries MJ, McCarthy JB, Tremble PM, Werb Z, Damsky CH. Cooperative signaling by alpha 5 beta 1 and alpha 4 beta 1 integrins regulates metalloproteinase gene expression in fibroblasts adhering to fibronectin. J Cell Biol 1995;129(3):867-79
    • (1995) J Cell Biol , vol.129 , Issue.3 , pp. 867-879
    • Huhtala, P.1    Humphries, M.J.2    McCarthy, J.B.3    Tremble, P.M.4    Werb, Z.5    Damsky, C.H.6
  • 3
    • 1542269303 scopus 로고    scopus 로고
    • Integrins. roles in cancer development and as treatment targets
    • Jin H, Varner J. Integrins. roles in cancer development and as treatment targets. Br J Cancer 2004;90(3):561-5.
    • (2004) Br J Cancer , vol.90 , Issue.3 , pp. 561-565
    • Jin, H.1    Varner, J.2
  • 4
    • 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, Juan M, Vives J, Urbano-Márquez A, Yagüe J, Cid MC. 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(8):2754-66
    • (1999) Blood , vol.94 , Issue.8 , pp. 2754-2766
    • Esparza, J.1    Vilardell, C.2    Calvo, J.3    Juan, M.4    Vives, J.5    Urbano-Márquez, A.6    Yagüe, J.7    Cid, M.C.8
  • 5
    • 33748189347 scopus 로고    scopus 로고
    • Cell-surface association between matrix metalloproteinases and integrins: Role of the complexes in leukocyte migration and cancer progression
    • Stefanidakis M, Koivunen E. Cell-surface association between matrix metalloproteinases and integrins: Role of the complexes in leukocyte migration and cancer progression. Blood 2006;108(5):1441-50.
    • (2006) Blood , vol.108 , Issue.5 , pp. 1441-1450
    • Stefanidakis, M.1    Koivunen, E.2
  • 8
    • 0032578007 scopus 로고    scopus 로고
    • Complementary roles for receptor clustering and conformational change in the adhesive and signaling functions of integrin alphaIIb beta3
    • Hato T, Pampori N, Shattil SJ. Complementary roles for receptor clustering and conformational change in the adhesive and signaling functions of integrin alphaIIb beta3. J Cell Biol 1998;141 (7):1685-95.
    • (1998) J Cell Biol , vol.141 , Issue.7 , pp. 1685-1695
    • Hato, T.1    Pampori, N.2    Shattil, S.J.3
  • 9
    • 77956036906 scopus 로고
    • Fibronectin; New York Sringer Verlag
    • Hynes RO. Fibronectin; New York Sringer Verlag (1990).
    • (1990)
    • Hynes, R.O.1
  • 10
    • 10244272938 scopus 로고    scopus 로고
    • Non-collagenous matrix proteins
    • W. E. Comper, ed., 1 ed, Amsterdam: Harwood academic publishers
    • Johansson S. Non-collagenous matrix proteins, In: W. E. Comper, ed. Extracellular matrix, 1 ed, vol 2, Amsterdam: Harwood academic publishers; 68-94 (1996).
    • (1996) Extracellular matrix , vol.2 , pp. 68-94
    • Johansson, S.1
  • 11
    • 0032926793 scopus 로고    scopus 로고
    • Fibronectin and its integrin receptors in cancer
    • Ruoslahti E. Fibronectin and its integrin receptors in cancer. Adv Cancer Res. 1999;76:1-20.
    • (1999) Adv Cancer Res , vol.76 , pp. 1-20
    • Ruoslahti, E.1
  • 12
    • 0025313097 scopus 로고
    • Cheresh DA Interaction of integrins alpha v beta 3 and glycoprotein IIb-IIIa with fibrinogen Differential peptide recognition accounts for distinct binding sites
    • Smith JW, Ruggeri ZM, Kunicki TJ, Cheresh DA Interaction of integrins alpha v beta 3 and glycoprotein IIb-IIIa with fibrinogen. Differential peptide recognition accounts for distinct binding sites. J Biol Chem 1990;265(21):12267-71
    • (1990) J Biol Chem , vol.265 , Issue.21 , pp. 12267-12271
    • Smith, J.W.1    Ruggeri, Z.M.2    Kunicki, T.J.3
  • 13
    • 0027267959 scopus 로고
    • Selection of peptides binding to the alpha 5 beta 1 integrin from phage display library
    • Koivunen E, Gay DA, Ruoslahti E. Selection of peptides binding to the alpha 5 beta 1 integrin from phage display library. J Biol Chem. 1993;268; 20205-10
    • (1993) J Biol Chem , vol.268 , pp. 20205-20210
    • Koivunen, E.1    Gay, D.A.2    Ruoslahti, E.3
  • 14
    • 0021271957 scopus 로고
    • Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
    • Pierschbacher MD, Ruoslahti E. Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature 1984;309(5963):30-3.
    • (1984) Nature , vol.309 , Issue.5963 , pp. 30-33
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 15
    • 0027055575 scopus 로고
    • Cell adhesion or integrin clustering increases phosphorylation of a focal adhesionassociated tyrosine kinase
    • Kornberg L, Earp HS, Parsons JT, Schaller M, Juliano RL. Cell adhesion or integrin clustering increases phosphorylation of a focal adhesionassociated tyrosine kinase, J Biol Chem. 1992;267(33):23439-42.
    • (1992) J Biol Chem , vol.267 , Issue.33 , pp. 23439-23442
    • Kornberg, L.1    Earp, H.S.2    Parsons, J.T.3    Schaller, M.4    Juliano, R.L.5
  • 16
    • 0036178447 scopus 로고    scopus 로고
    • Signal transduction by cell adhesion receptors and the cytoskeleton: Functions of integrins, cadherins, selectins, and immunoglobulin-superfamily members
    • Juliano RL. Signal transduction by cell adhesion receptors and the cytoskeleton: functions of integrins, cadherins, selectins, and immunoglobulin-superfamily members, Annu Rev Pharmacol Toxicol. 2002;42:283-323.
    • (2002) Annu Rev Pharmacol Toxicol , vol.42 , pp. 283-323
    • Juliano, R.L.1
  • 17
    • 2442421050 scopus 로고    scopus 로고
    • Dual regulation of MMP-2 expression by the type 1 insulin-like growth factor receptor: The phosphatidylinositol 3-kinase/Akt and Raf/ERK pathways transmit opposing signals
    • Zhang D, Bar-Eli M, Meloche S, Brodt P. Dual regulation of MMP-2 expression by the type 1 insulin-like growth factor receptor: The phosphatidylinositol 3-kinase/Akt and Raf/ERK pathways transmit opposing signals. J Biol Chem 2004;279(19):19683-90.
    • (2004) J Biol Chem , vol.279 , Issue.19 , pp. 19683-19690
    • Zhang, D.1    Bar-Eli, M.2    Meloche, S.3    Brodt, P.4
  • 19
    • 0034044418 scopus 로고    scopus 로고
    • Expression of integrin alpha (v)beta(3) correlates with activation of membrane-type matrix metalloproteinase-1 (MT1-MMP) and matrix metalloproteinase-2 (MMP-2) in human melanoma cells in vitro and in vivo
    • Hofmann UB, Westphal JR, Van Kraats AA, Ruiter DJ, Van Muijen GN. Expression of integrin alpha (v)beta(3) correlates with activation of membrane-type matrix metalloproteinase-1 (MT1-MMP) and matrix metalloproteinase-2 (MMP-2) in human melanoma cells in vitro and in vivo. Int J Cancer 2000;87(1):12-9.
    • (2000) Int J Cancer , vol.87 , Issue.1 , pp. 12-19
    • Hofmann, U.B.1    Westphal, J.R.2    Van Kraats, A.A.3    Ruiter, D.J.4    Van Muijen, G.N.5
  • 21
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • Egeblad M, Werb Z. New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer 2002;2(3):161-74.
    • (2002) Nat Rev Cancer , vol.2 , Issue.3 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 22
    • 2442462505 scopus 로고    scopus 로고
    • The possible role of matrix metalloproteinase (MMP)-2 and MMP-9 in cancer, e.g. acute leukemia
    • Klein G, Vellenga E, Fraaije MW, Kamps WA, de Bont ES. The possible role of matrix metalloproteinase (MMP)-2 and MMP-9 in cancer, e.g. acute leukemia, Crit Rev Oncol Hematol 2004;50(2):87-100.
    • (2004) Crit Rev Oncol Hematol , vol.50 , Issue.2 , pp. 87-100
    • Klein, G.1    Vellenga, E.2    Fraaije, M.W.3    Kamps, W.A.4    de Bont, E.S.5
  • 23
    • 3242704308 scopus 로고    scopus 로고
    • Binding of alpha2 monoclonal antibody to human cervical tumor cell (SiHa) surface alpha2beta1 integrin modulates MMP-2 activity
    • Mitra A, Chakrabarti J, Banerji A, Chatterjee A. Binding of alpha2 monoclonal antibody to human cervical tumor cell (SiHa) surface alpha2beta1 integrin modulates MMP-2 activity. Gynecol Oncol. 2004; 94(1):33-9.
    • (2004) Gynecol Oncol , vol.94 , Issue.1 , pp. 33-39
    • Mitra, A.1    Chakrabarti, J.2    Banerji, A.3    Chatterjee, A.4
  • 24
    • 33745295151 scopus 로고    scopus 로고
    • Culture of human cervical cells in presence of fibronectin activated MMP-2
    • Mitra A, Banerji A, Das S, Chatterjee A. Culture of human cervical cells in presence of fibronectin activated MMP-2. J Can Res Clin Oncol 2006;132 (8):505-13.
    • (2006) J Can Res Clin Oncol , vol.132 , Issue.8 , pp. 505-513
    • Mitra, A.1    Banerji, A.2    Das, S.3    Chatterjee, A.4
  • 25
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
    • Dignam JD, Lebovitz RM, Roeder RG. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acid Res 1983; 11 (5): 1475-1489.
    • (1983) Nucleic Acid Res , vol.11 , Issue.5 , pp. 1475-1489
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.G.3
  • 26
    • 3242882629 scopus 로고    scopus 로고
    • Fibronectin stimulates human lung carcinoma cell growth by inducing cyclooxygenase-2 (COX-2) expression
    • Han S, Sidell A, Roser-Page S, Roman J. Fibronectin stimulates human lung carcinoma cell growth by inducing cyclooxygenase-2 (COX-2) expression. Int J cancer 2004;111:322-331.
    • (2004) Int J cancer , vol.111 , pp. 322-331
    • Han, S.1    Sidell, A.2    Roser-Page, S.3    Roman, J.4
  • 28
    • 0035318252 scopus 로고    scopus 로고
    • All-trans Retinoic acid selectively down regulates matrix metalloproteinase-9 (MMP-9) and up-regulates tissue inhibitor of metalloproteinase-1 (TIMP-1) in human bronchoalveolar lavage cells
    • Frankenberger M, Hanck RW, Frankenberger B, Häu Binger K, Maier KL. All-trans Retinoic acid selectively down regulates matrix metalloproteinase-9 (MMP-9) and up-regulates tissue inhibitor of metalloproteinase-1 (TIMP-1) in human bronchoalveolar lavage cells. Molecular medicine 2001;7(4):263-270.
    • (2001) Molecular medicine , vol.7 , Issue.4 , pp. 263-270
    • Frankenberger, M.1    Hanck, R.W.2    Frankenberger, B.3    Häu Binger, K.4    Maier, K.L.5
  • 29
    • 0030272101 scopus 로고    scopus 로고
    • Integrin activation: the link between ligand binding and signal transduction
    • Humphries MJ. Integrin activation: the link between ligand binding and signal transduction. Curr Opin Cell Biol 1996;8:632-640.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 632-640
    • Humphries, M.J.1
  • 30
    • 0027982876 scopus 로고
    • Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigm
    • Springer TA. Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigm. Cell 1994;76, 301-314.
    • (1994) Cell , vol.76 , pp. 301-314
    • Springer, T.A.1
  • 35
    • 0033623969 scopus 로고    scopus 로고
    • Integrin alpha5 Beta1 mediates fibronectin dependent epithelial cell proliferation through epithelial growth factor receptor activation
    • Scott K, Integrin alpha5 Beta1 mediates fibronectin dependent epithelial cell proliferation through epithelial growth factor receptor activation, Mol Biol Cell, 2000;11:2485-96
    • (2000) Mol Biol Cell , vol.11 , pp. 2485-2496
    • Scott, K.1
  • 37
    • 39149084984 scopus 로고    scopus 로고
    • Rapid expression and activation of matrix metalloproteinase-2 and -9 upon exposure of human breast cancer cells (MCF-7) to fibronectin in serum free culture medium
    • Das S, Banerji A, Frie E, Chatterjee A. Rapid expression and activation of matrix metalloproteinase-2 and -9 upon exposure of human breast cancer cells (MCF-7) to fibronectin in serum free culture medium, Life Sci 2008, 82:467-76.
    • (2008) Life Sci , vol.82 , pp. 467-476
    • Das, S.1    Banerji, A.2    Frie, E.3    Chatterjee, A.4
  • 38
    • 0025226540 scopus 로고
    • Positive and Negative Transcriptional Elements of the Human Type IV Collagenase Gene
    • Frisch SM, Morisaki JH. Positive and Negative Transcriptional Elements of the Human Type IV Collagenase Gene. Mol Cell Biol 1990;10 (12):6524.
    • (1990) Mol Cell Biol , vol.10 , Issue.12 , pp. 6524
    • Frisch, S.M.1    Morisaki, J.H.2
  • 39
    • 0032584221 scopus 로고    scopus 로고
    • The expression of matrix metalloproteinase 9 is enhanced by Epstein-Barr virus latent membrane protein 1
    • Yoshizaki T, Sato H, Furukawa M, Pagano JS. The expression of matrix metalloproteinase 9 is enhanced by Epstein-Barr virus latent membrane protein 1. Proc Natl Acad Sci 1998;95:3621.
    • (1998) Proc Natl Acad Sci , vol.95 , pp. 3621
    • Yoshizaki, T.1    Sato, H.2    Furukawa, M.3    Pagano, J.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.