메뉴 건너뛰기




Volumn 17, Issue 2, 2013, Pages 203-216

Matrix metalloproteinase-2 as a target for head and neck cancer therapy

Author keywords

Head and neck cancer; MMP 2; Molecular target; Signaling networks

Indexed keywords

2 [N (4 METHOXYSULFONYL)(3 PYRIDINYLMETHYL)AMINO] 3 METHYLBUTYROHYDROXAMIC ACID; AE 941; ALPHA INTERFERON; BATIMASTAT; BISPHOSPHONIC ACID DERIVATIVE; CARBOPLATIN; CISPLATIN; CYTOTOXIC AGENT; DOXYCYCLINE; ETOPOSIDE; FLUOROURACIL; FOLINIC ACID; GELATINASE A; GEMCITABINE; INCYCLINIDE; MARIMASTAT; MATRIX METALLOPROTEINASE INHIBITOR; MEMBRANE PROTEIN; OSTHOLE; PACLITAXEL; PEPTIDOMIMETIC AGENT; PRINOMASTAT; REBIMASTAT; SILIBININ; SOLIMASTAT; TANOMASTAT; TETRACYCLINE DERIVATIVE; TISSUE INHIBITOR OF METALLOPROTEINASE 2; ZOLEDRONIC ACID;

EID: 84872240151     PISSN: 14728222     EISSN: 17447631     Source Type: Journal    
DOI: 10.1517/14728222.2013.740012     Document Type: Review
Times cited : (82)

References (126)
  • 1
    • 0035892919 scopus 로고    scopus 로고
    • Extracapsular spread: A significant predictor of treatment failure in patients with squamous cell carcinoma of the tongue
    • DOI 10.1002/1097-0142(20011215)92:12<3030::AID-CNCR10148>3.0.CO;2-P
    • Myers JN, Greenberg JS, Mo V, et al. Extracapsular spread. A significant predictor of treatment failure in patients with squamous cell carcinoma of the tongue. Cancer 2001;92:3030-6 (Pubitemid 33136197)
    • (2001) Cancer , vol.92 , Issue.12 , pp. 3030-3036
    • Myers, J.N.1    Greenberg, J.S.2    Mo, V.3    Roberts, D.4
  • 2
    • 0030769477 scopus 로고    scopus 로고
    • General mechanisms of metastasis
    • Woodhouse EC, Chuaqui RF, Liotta LA. General mechanisms of metastasis. Cancer 1997;80:1529-37 (Pubitemid 27444024)
    • (1997) Cancer , vol.80 , Issue.8 , pp. 1529-1537
    • Woodhouse, E.C.1    Chuaqui, R.F.2    Liotta, L.A.3
  • 3
    • 0022656975 scopus 로고
    • Tumor invasion and metastases - Role of the extracellular matrix: Rhoads Memorial Award Lecture
    • Liotta LA. Tumor invasion and metastases-role of the extracellular matrix: Rhoads Memorial Award lecture. Cancer Res 1986;46:1-7 (Pubitemid 16189019)
    • (1986) Cancer Research , vol.46 , Issue.1 , pp. 1-7
    • Liotta, L.A.1
  • 4
    • 33947636758 scopus 로고    scopus 로고
    • Clinicopathological significance of MMP-2 and TIMP-2 genotypes in gastric cancer
    • Wu CY, Wu MS, Chen YJ, et al. Clinicopathological significance of MMP-2 and TIMP-2 genotypes in gastric cancer. Eur J Cancer 2007;43:799-808
    • (2007) Eur J Cancer , vol.43 , pp. 799-808
    • Wu, C.Y.1    Wu, M.S.2    Chen, Y.J.3
  • 5
    • 5644232084 scopus 로고    scopus 로고
    • Functional haplotypes in the promoter of matrix metalloproteinase-2 predict risk of the occurrence and metastasis of esophageal cancer
    • DOI 10.1158/0008-5472.CAN-04-1521
    • Yu C, Zhou Y, Miao X, et al. Functional haplotypes in the promoter of matrix metalloproteinase-2 predict risk of the occurrence and metastasis of esophageal cancer. Cancer Res 2004;64:7622-8 (Pubitemid 39372109)
    • (2004) Cancer Research , vol.64 , Issue.20 , pp. 7622-7628
    • Yu, C.1    Zhou, Y.2    Miao, X.3    Xiong, P.4    Tan, W.5    Lin, D.6
  • 6
    • 0032737415 scopus 로고    scopus 로고
    • Matrix metalloproteinases expressed in squamous cell carcinoma of the oral cavity: Correlation with clinicopathologic features and neo-adjuvant chemotherapy response
    • Arenas-Huertero FJ, Herrera-Goepfert R Delgado-Chavez R, et al. Matrix metalloproteinases expressed in squamous cell carcinoma of the oral cavity: Correlation with clinicopathologic features and neo-adjuvant chemotherapy response. J Exp Clin Cancer Res 1999;18:279-84
    • (1999) J Exp Clin Cancer Res , vol.18 , pp. 279-284
    • Arenas-Huertero, F.J.1    Herrera-Goepfert, R.2    Delgado-Chavez, R.3
  • 7
    • 0034934654 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinases and their inhibitors correlates with invasion and metastasis in squamous cell carcinoma of the head and neck
    • O-Charoenrat P, Rhys-Evans PH Eccles SA. Expression of matrix metalloproteinases and their inhibitors correlates with invasion and metastasis in squamous cell carcinoma of the head and neck. Arch Otolaryngol Head Neck Surg 2001;127:813-20 (Pubitemid 32619361)
    • (2001) Archives of Otolaryngology - Head and Neck Surgery , vol.127 , Issue.7 , pp. 813-820
    • Ocharoenrat, P.1    Rhys-Evans, P.H.2    Eccles, S.A.3
  • 9
    • 78650107988 scopus 로고    scopus 로고
    • Immunoexpression of matrix metalloproteinase-2 and matrix metalloproteinase-9 in the metastasis of squamous cell carcinoma of the human tongue
    • Zhou CX, Gao Y, Johnson NW, et al. Immunoexpression of matrix metalloproteinase-2 and matrix metalloproteinase-9 in the metastasis of squamous cell carcinoma of the human tongue. Aust Dent J 2010;55:385-9
    • (2010) Aust Dent J , vol.55 , pp. 385-389
    • Zhou, C.X.1    Gao, Y.2    Johnson, N.W.3
  • 10
    • 63449131596 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 involvement in breast cancer progression: A mini-review
    • Jezierska A, Motyl T. Matrix metalloproteinase-2 involvement in breast cancer progression: A mini-review. Med Sci Monit 2009;15:RA32-40
    • (2009) Med Sci Monit , vol.15
    • Jezierska, A.1    Motyl, T.2
  • 11
    • 74249098410 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 and myocardial oxidative stress injury: Beyond the matrix
    • Kandasamy AD, Chow AK, Ali MA et al. Matrix metalloproteinase-2 and myocardial oxidative stress injury: Beyond the matrix. Cardiovasc Res 2010;85:413-23
    • (2010) Cardiovasc Res , vol.85 , pp. 413-423
    • Kandasamy, A.D.1    Chow, A.K.2    Ali, M.A.3
  • 12
    • 0020623038 scopus 로고
    • Purification and characterization of a murine basement membrane collagen-degrading enzyme secreted by metastatic tumor cells
    • Salo T, Liotta LA, Tryggvason K. Purification and characterization of a murine basement membrane collagen-degrading enzyme secreted by metastatic tumor cells. J Biol Chem 1983;258:3058-63 (Pubitemid 13130228)
    • (1983) Journal of Biological Chemistry , vol.258 , Issue.5 , pp. 3058-3063
    • Salo, T.1    Liotta, L.A.2    Tryggvason, K.3
  • 13
    • 0023916537 scopus 로고
    • Monoclonal antibodies to type IV collagenase recognize a protein with limited sequence homology to interstitial collagenase and stromelysin
    • Hoyhtya M, Turpeenniemi-Hujanen T Stetler-Stevenson W, et al. Monoclonal antibodies to type IV collagenase recognize a protein with limited sequence homology to interstitial collagenase and stromelysin. FEBS Lett 1988;233:109-13
    • (1988) FEBS Lett , vol.233 , pp. 109-113
    • Hoyhtya, M.1    Turpeenniemi-Hujanen, T.2    Stetler-Stevenson, W.3
  • 14
    • 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;2:161-74 (Pubitemid 37328786)
    • (2002) Nature Reviews Cancer , vol.2 , Issue.3 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 16
    • 0030826510 scopus 로고    scopus 로고
    • Transcriptional activation by p53 of the human type IV collagenase (gelatinase A or matrix metalloproteinase 2) promoter
    • Bian J, Sun Y. Transcriptional activation by p53 of the human type IV collagenase (gelatinase A or matrix metalloproteinase 2) promoter. Mol Cell Biol 1997;17:6330-8 (Pubitemid 27451177)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.11 , pp. 6330-6338
    • Bian, J.1    Sun, Y.2
  • 17
    • 0032857460 scopus 로고    scopus 로고
    • The transcription factors Sp1, Sp3, and AP-2 are required for constitutive matrix metalloproteinase-2 gene expression in astroglioma cells
    • Qin H, Sun Y, Benveniste EN. The transcription factors Sp1, Sp3, and AP-2 are required for constitutive matrix metalloproteinase-2 gene expression in astroglioma cells. J Biol Chem 1999;274:29130-7
    • (1999) J Biol Chem , vol.274 , pp. 29130-7
    • Qin, H.1    Sun, Y.2    Benveniste, E.N.3
  • 18
    • 0035831536 scopus 로고    scopus 로고
    • Identification of novel, functional genetic variants in the human matrix metalloproteinase-2 gene: Role of Sp1 in allele-specific transcriptional regulation
    • Price SJ, Greaves DR, Watkins H. Identification of novel, functional genetic variants in the human matrix metalloproteinase-2 gene: Role of Sp1 in allele-specific transcriptional regulation. J Biol Chem 2001;276:7549-58
    • (2001) J Biol Chem , vol.276 , pp. 7549-7558
    • Price, S.J.1    Greaves, D.R.2    Watkins, H.3
  • 19
    • 3342955556 scopus 로고    scopus 로고
    • Functional genotype in matrix metalloproteinases-2 promoter is a risk factor for oral carcinogenesis
    • Lin SC, Lo SS, Liu CJ, et al. Functional genotype in matrix metalloproteinases-2 promoter is a risk factor for oral carcinogenesis. J Oral Pathol Med 2004;33:405-9
    • (2004) J Oral Pathol Med , vol.33 , pp. 405-409
    • Lin, S.C.1    Lo, S.S.2    Liu, C.J.3
  • 20
    • 0032227612 scopus 로고    scopus 로고
    • Role of matrix proteases in processing enamel proteins
    • discussion 141-149
    • Woessner JF Jr. Role of matrix proteases in processing enamel proteins. Connect Tissue Res 1998;39:69-73; discussion 141-149
    • (1998) Connect Tissue Res , vol.39 , pp. 69-73
    • Woessner Jr., J.F.1
  • 21
    • 0035800858 scopus 로고    scopus 로고
    • Activation of matrix metalloproteinases by peroxynitrite-induced protein S-glutathiolation via disulfide S-oxide formation
    • Okamoto T, Akaike T, Sawa T, et al. Activation of matrix metalloproteinases by peroxynitrite-induced protein S-glutathiolation via disulfide S-oxide formation. J Biol Chem 2001;276:29596-602
    • (2001) J Biol Chem , vol.276 , pp. 29596-29602
    • Okamoto, T.1    Akaike, T.2    Sawa, T.3
  • 23
    • 0037205286 scopus 로고    scopus 로고
    • Factor Xa releases matrix metalloproteinase-2 (MMP-2) from human vascular smooth muscle cells and stimulates the conversion of pro-MMP-2 to MMP-2: Role of MMP-2 in factor Xa-induced DNA synthesis and matrix invasion
    • DOI 10.1161/01.RES.0000019240.72809.76
    • Rauch BH, Bretschneider E, Braun M et al. Factor Xa releases matrix metalloproteinase-2 (MMP-2) from human vascular smooth muscle cells and stimulates the conversion of pro-MMP-2 to MMP-2: Role of MMP-2 in factor Xa-induced DNA synthesis and matrix invasion. Circ Res 2002;90:1122-7 (Pubitemid 34627912)
    • (2002) Circulation Research , vol.90 , Issue.10 , pp. 1122-1127
    • Rauch, B.H.1    Bretschneider, E.2    Braun, M.3    Schror, K.4
  • 24
    • 0028804964 scopus 로고
    • Thrombin induces the activation of progelatinase A in vascular endothelial cells. Physiologic regulation of angiogenesis
    • Zucker S, Conner C, DiMassmo BI et al. Thrombin induces the activation of progelatinase A in vascular endothelial cells. Physiologic regulation of angiogenesis. J Biol Chem 1995;270:23730-8
    • (1995) J Biol Chem , vol.270 , pp. 23730-8
    • Zucker, S.1    Conner, C.2    DiMassmo, B.I.3
  • 25
    • 0028924956 scopus 로고
    • The C-terminal region of membrane type matrix metalloproteinase is a functional transmembrane domain required for pro-gelatinase A activation
    • Cao J, Sato H, Takino T, et al. The C-terminal region of membrane type matrix metalloproteinase is a functional transmembrane domain required for pro-gelatinase A activation. J Biol Chem 1995;270:801-5
    • (1995) J Biol Chem , vol.270 , pp. 801-805
    • Cao, J.1    Sato, H.2    Takino, T.3
  • 26
    • 0142169378 scopus 로고    scopus 로고
    • Selective involvement of TIMP-2 in the second activational cleavage of pro-MMP-2: Refinement of the pro-MMP-2 activation mechanism
    • DOI 10.1016/S0014-5793(03)01094-9
    • Lafleur MA, Tester AM, Thompson EW. Selective involvement of TIMP-2 in the second activational cleavage of pro-MMP-2: Refinement of the pro-MMP-2 activation mechanism. FEBS Lett 2003;553:457-63 (Pubitemid 37315649)
    • (2003) FEBS Letters , vol.553 , Issue.3 , pp. 457-463
    • Lafleur, M.A.1    Tester, A.M.2    Thompson, E.W.3
  • 28
    • 25144509494 scopus 로고    scopus 로고
    • Inhibition of basigin expression in glioblastoma cell line via antisense RNA reduces tumor cell invasion and angiogenesis
    • Liang Q, Xiong H, Gao G, et al. Inhibition of basigin expression in glioblastoma cell line via antisense RNA reduces tumor cell invasion and angiogenesis. Cancer Biol Ther 2005;4:759-62 (Pubitemid 41351176)
    • (2005) Cancer Biology and Therapy , vol.4 , Issue.7 , pp. 759-762
    • Liang, Q.1    Xiong, H.2    Gao, G.3    Xiong, K.4    Wang, X.5    Zhao, Z.6    Zhang, H.7    Li, Y.8
  • 29
    • 0041622766 scopus 로고    scopus 로고
    • Expression of extracellular matrix metalloprotease inducer in laryngeal squamous cell carcinoma
    • DOI 10.1097/00005537-200308000-00027
    • Rosenthal EL, Shreenivas S, Peters GE et al. Expression of extracellular matrix metalloprotease inducer in laryngeal squamous cell carcinoma. Laryngoscope 2003;113:1406-10 (Pubitemid 36944687)
    • (2003) Laryngoscope , vol.113 , Issue.8 , pp. 1406-1410
    • Rosenthal, E.L.1    Shreenivas, S.2    Peters, G.E.3    Grizzle, W.E.4    Desmond, R.5    Gladson, C.L.6
  • 30
    • 84863014455 scopus 로고    scopus 로고
    • EMMPRIN contributes to the in vitro invasion of human salivary adenoid cystic carcinoma cells
    • Yang X, Zhang P, Ma Q, et al. EMMPRIN contributes to the in vitro invasion of human salivary adenoid cystic carcinoma cells. Oncol Rep 2012;27:1123-7
    • (2012) Oncol Rep , vol.27 , pp. 1123-1127
    • Yang, X.1    Zhang, P.2    Ma, Q.3
  • 31
    • 33644500747 scopus 로고    scopus 로고
    • Increased EMMPRIN (CD 147) expression during oral carcinogenesis
    • Vigneswaran N, Beckers S, Waigel S et al. Increased EMMPRIN (CD 147) expression during oral carcinogenesis. Exp Mol Pathol 2006;80:147-59
    • (2006) Exp Mol Pathol , vol.80 , pp. 147-159
    • Vigneswaran, N.1    Beckers, S.2    Waigel, S.3
  • 32
    • 84858717758 scopus 로고    scopus 로고
    • EMMPRIN/CD147 up-regulates urokinase-type plasminogen activator: Implications in oral tumor progression
    • Lescaille G, Menashi S Cavelier-Balloy B, et al. EMMPRIN/CD147 up-regulates urokinase-type plasminogen activator: implications in oral tumor progression. BMC Cancer 2012;12:115
    • (2012) BMC Cancer , vol.12 , pp. 115
    • Lescaille, G.1    Menashi, S.2    Cavelier-Balloy, B.3
  • 33
    • 49049093408 scopus 로고    scopus 로고
    • EMMPRIN modulates migration and deposition of TN-C in oral squamous carcinoma
    • Dang D, Atakilit A, Ramos DM. EMMPRIN modulates migration and deposition of TN-C in oral squamous carcinoma. Anticancer Res 2008;28:2049-54
    • (2008) Anticancer Res , vol.28 , pp. 2049-2054
    • Dang, D.1    Atakilit, A.2    Ramos, D.M.3
  • 34
    • 84863067484 scopus 로고    scopus 로고
    • EMMPRIN silencing inhibits proliferation and perineural invasion of human salivary adenoid cystic carcinoma cells in vitro and in vivo
    • Yang X, Zhang P, Ma Q, et al. EMMPRIN silencing inhibits proliferation and perineural invasion of human salivary adenoid cystic carcinoma cells in vitro and in vivo. Cancer Biol Ther 2012;13:85-91
    • (2012) Cancer Biol Ther , vol.13 , pp. 85-91
    • Yang, X.1    Zhang, P.2    Ma, Q.3
  • 35
    • 77950931419 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Regulators of the tumor microenvironment
    • Kessenbrock K, Plaks V, Werb Z. Matrix metalloproteinases: Regulators of the tumor microenvironment. Cell 2010;141:52-67
    • (2010) Cell , vol.141 , pp. 52-67
    • Kessenbrock, K.1    Plaks, V.2    Werb, Z.3
  • 36
    • 79960226262 scopus 로고    scopus 로고
    • Physiology and pathophysiology of matrix metalloproteases
    • Klein T, Bischoff R. Physiology and pathophysiology of matrix metalloproteases. Amino Acids 2011;41:271-90
    • (2011) Amino Acids , vol.41 , pp. 271-290
    • Klein, T.1    Bischoff, R.2
  • 37
    • 70449732503 scopus 로고    scopus 로고
    • Matrix metalloproteinases as novel biomarkers and potential therapeutic targets in human cancer
    • Roy R, Yang J, Moses MA. Matrix metalloproteinases as novel biomarkers and potential therapeutic targets in human cancer. J Clin Oncol 2009;27:5287-97
    • (2009) J Clin Oncol , vol.27 , pp. 5287-5297
    • Roy, R.1    Yang, J.2    Moses, M.A.3
  • 38
    • 77149164774 scopus 로고    scopus 로고
    • Matrix metalloproteinases: What do they not do? new substrates and biological roles identified by murine models and proteomics
    • Rodriguez D, Morrison CJ, Overall CM. Matrix metalloproteinases: what do they not do? New substrates and biological roles identified by murine models and proteomics. Biochim Biophys Acta 2010;1803:39-54
    • (2010) Biochim Biophys Acta , vol.1803 , pp. 39-54
    • Rodriguez, D.1    Morrison, C.J.2    Overall, C.M.3
  • 39
    • 77049108176 scopus 로고    scopus 로고
    • Pleiotropic roles of matrix metalloproteinases in tumor angiogenesis: Contrasting overlapping and compensatory functions
    • Deryugina EI, Quigley JP. Pleiotropic roles of matrix metalloproteinases in tumor angiogenesis: Contrasting overlapping and compensatory functions. Biochim Biophys Acta 2010;1803:103-20
    • (2010) Biochim Biophys Acta , vol.1803 , pp. 103-120
    • Deryugina, E.I.1    Quigley, J.P.2
  • 41
    • 33749350351 scopus 로고    scopus 로고
    • A cancer cell metalloprotease triad regulates the basement membrane transmigration program
    • DOI 10.1101/gad.1451806
    • Hotary K, Li XY, Allen E, et al. A cancer cell metalloprotease triad regulates the basement membrane transmigration program. Genes Dev 2006;20:2673-86 (Pubitemid 44498378)
    • (2006) Genes and Development , vol.20 , Issue.19 , pp. 2673-2686
    • Hotary, K.1    Li, X.-Y.2    Allen, E.3    Stevens, S.L.4    Weiss, S.J.5
  • 42
    • 69249156451 scopus 로고    scopus 로고
    • Secreted versus membrane-anchored collagenases: Relative roles in fibroblast-dependent collagenolysis and invasion
    • Sabeh F, Li XY, Saunders TL, et al. Secreted versus membrane-anchored collagenases: Relative roles in fibroblast-dependent collagenolysis and invasion. J Biol Chem 2009;284:23001-11
    • (2009) J Biol Chem , vol.284 , pp. 23001-23011
    • Sabeh, F.1    Li, X.Y.2    Saunders, T.L.3
  • 44
    • 47949096781 scopus 로고    scopus 로고
    • Cancer-related inflammation
    • Mantovani A, Allavena P, Sica A, et al. Cancer-related inflammation. Nature 2008;454:436-44
    • (2008) Nature , vol.454 , pp. 436-444
    • Mantovani, A.1    Allavena, P.2    Sica, A.3
  • 45
    • 79952706985 scopus 로고    scopus 로고
    • Transforming growth factor-beta and the hallmarks of cancer
    • Tian M, Neil JR, Schiemann WP. Transforming growth factor-beta and the hallmarks of cancer. Cell Signal 2011;23:951-62
    • (2011) Cell Signal , vol.23 , pp. 951-962
    • Tian, M.1    Neil, J.R.2    Schiemann, W.P.3
  • 47
    • 78650695157 scopus 로고    scopus 로고
    • The crosstalk between the matrix metalloprotease system and the chemokine network in acute myeloid leukemia
    • Hatfield KJ, Reikvam H, Bruserud O. The crosstalk between the matrix metalloprotease system and the chemokine network in acute myeloid leukemia. Curr Med Chem 2010;17:4448-61
    • (2010) Curr Med Chem , vol.17 , pp. 4448-4461
    • Hatfield, K.J.1    Reikvam, H.2    Bruserud, O.3
  • 48
    • 19344366798 scopus 로고    scopus 로고
    • Gelatinase-mediated migration and invasion of cancer cells
    • DOI 10.1016/j.bbcan.2005.03.001, PII S0304419X05000077
    • Bjorklund M, Koivunen E. Gelatinase-mediated migration and invasion of cancer cells. Biochim Biophys Acta 2005;1755:37-69 (Pubitemid 40720240)
    • (2005) Biochimica et Biophysica Acta - Reviews on Cancer , vol.1755 , Issue.1 , pp. 37-69
    • Bjorklund, M.1    Koivunen, E.2
  • 49
    • 0034682885 scopus 로고    scopus 로고
    • Inflammation dampened by gelatinase a cleavage of monocyte chemoattractant protein-3
    • DOI 10.1126/science.289.5482.1202
    • McQuibban GA, Gong JH, Tam EM et al. Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3. Science 2000;289:1202-6 (Pubitemid 30650734)
    • (2000) Science , vol.289 , Issue.5482 , pp. 1202-1206
    • McQuibban, G.A.1    Gong, J.-H.2    Tam, E.M.3    McCulloch, C.A.G.4    Clark-Lewis, I.5    Overall, C.M.6
  • 50
    • 15244357105 scopus 로고    scopus 로고
    • Role of matrix metalloproteinases in melanoma cell invasion
    • DOI 10.1016/j.biochi.2005.01.013
    • Hofmann UB, Houben R, Brocker EB et al. Role of matrix metalloproteinases in melanoma cell invasion. Biochimie 2005;87:307-14 (Pubitemid 40387609)
    • (2005) Biochimie , vol.87 , Issue.3 , pp. 307-314
    • Hofmann, U.B.1    Houben, R.2    Brocker, E.-B.3    Becker, J.C.4
  • 51
    • 33748189347 scopus 로고    scopus 로고
    • Cell-surface association between matrix metalloproteinases and integrins: Role of the complexes in leukocyte migration and cancer progression
    • DOI 10.1182/blood-2006-02-005363
    • Stefanidakis M, Koivunen E. Cell-surface association between matrix metalloproteinases and integrins: Role of the complexes in leukocyte migration and cancer progression. Blood 2006;108:1441-50 (Pubitemid 44316107)
    • (2006) Blood , vol.108 , Issue.5 , pp. 1441-1450
    • Stefanidakis, M.1    Koivunen, E.2
  • 52
    • 0035805530 scopus 로고    scopus 로고
    • The low density lipoprotein receptor-related protein modulates levels of matrix metalloproteinase 9 (MMP-9) by mediating its cellular catabolism
    • Hahn-Dantona E, Ruiz JF, Bornstein P et al. The low density lipoprotein receptor-related protein modulates levels of matrix metalloproteinase 9 (MMP-9) by mediating its cellular catabolism. J Biol Chem 2001;276:15498-503
    • (2001) J Biol Chem , vol.276 , pp. 15498-15503
    • Hahn-Dantona, E.1    Ruiz, J.F.2    Bornstein, P.3
  • 53
    • 0035896646 scopus 로고    scopus 로고
    • Extracellular matrix metalloproteinase 2 levels are regulated by the low density lipoprotein-related scavenger receptor and thrombospondin 2
    • Yang Z, Strickland DK, Bornstein P. Extracellular matrix metalloproteinase 2 levels are regulated by the low density lipoprotein-related scavenger receptor and thrombospondin 2. J Biol Chem 2001;276:8403-8
    • (2001) J Biol Chem , vol.276 , pp. 8403-8408
    • Yang, Z.1    Strickland, D.K.2    Bornstein, P.3
  • 55
    • 0032545758 scopus 로고    scopus 로고
    • Density-dependent regulation of cell-surface association of matrix metalloproteinase-2 (MMP-2) in breast-carcinoma cells
    • DOI 10.1002/(SICI)1097-0215(19980119)75:2<259::AID-IJC15>3.0.CO;2-8
    • Menashi S, Dehem M, Souliac I, et al. Density-dependent regulation of cell-surface association of matrix metalloproteinase-2 (MMP-2) in breast-carcinoma cells. Int J Cancer 1998;75:259-65 (Pubitemid 28100068)
    • (1998) International Journal of Cancer , vol.75 , Issue.2 , pp. 259-265
    • Menashi, S.1    Dehem, M.2    Souliac, I.3    Legrand, Y.4    Fridman, R.5
  • 56
    • 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, et al. 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;87:12-19
    • (2000) Int J Cancer , pp. 8712-8719
    • Hofmann, U.B.1    Westphal, J.R.2    Van Kraats, A.A.3
  • 59
    • 12244295145 scopus 로고    scopus 로고
    • Activation of metalloproteinases and their association with integrins: An auxillary apoptotic pathway in human endothelial cells
    • DOI 10.1038/sj.cdd.4401106
    • Levkau B, Kenagy RD, Karsan A, et al. Activation of metalloproteinases and their association with integrins: An auxiliary apoptotic pathway in human endothelial cells. Cell Death Differ 2002;9:1360-7 (Pubitemid 36097706)
    • (2002) Cell Death and Differentiation , vol.9 , Issue.12 , pp. 1360-1367
    • Levkau, B.1    Kenagy, R.D.2    Karsan, A.3    Weitkamp, B.4    Clowes, A.W.5    Ross, R.6    Raines, E.W.7
  • 60
    • 59449108662 scopus 로고    scopus 로고
    • Matrix metalloproteinase 2-integrin alpha v)beta3 binding is required for mesenchymal cell invasive activity but not epithelial locomotion: A computational time-lapse study
    • Rupp PA, Visconti RP, Czirok A, et al. Matrix metalloproteinase 2-integrin alpha (v)beta3 binding is required for mesenchymal cell invasive activity but not epithelial locomotion: A computational time-lapse study. Mol Biol Cell 2008;19:5529-40
    • (2008) Mol Biol Cell , vol.19 , pp. 5529-40
    • Rupp, P.A.1    Visconti, R.P.2    Czirok, A.3
  • 61
    • 77955496933 scopus 로고    scopus 로고
    • MMP-2 alters VEGF expression via alphaVbeta3 integrin-mediated PI3K/AKT signaling in A549 lung cancer cells
    • Chetty C, Lakka SS, Bhoopathi P, et al. MMP-2 alters VEGF expression via alphaVbeta3 integrin-mediated PI3K/AKT signaling in A549 lung cancer cells. Int J Cancer 2010;127:1081-95
    • (2010) Int J Cancer , vol.127 , pp. 1081-1095
    • Chetty, C.1    Lakka, S.S.2    Bhoopathi, P.3
  • 62
    • 4444282869 scopus 로고    scopus 로고
    • Tumor markers in cancer patients. An update of their prognostic significance. Part II
    • Agnantis NJ, Goussia AC, Batistatou A et al. Tumor markers in cancer patients. an update of their prognostic significance. Part II. In Vivo 2004;18:481-8 (Pubitemid 39199996)
    • (2004) Vivo , vol.18 , Issue.4 , pp. 481-488
    • Agnantis, N.J.1    Goussia, A.C.2    Batistatou, A.3    Stefanou, D.4
  • 63
    • 24744440612 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinases (MMPs) in cultured hepatocellular carcinoma (HCC) cells and surgically resected HCC tissues
    • Ogasawara S, Yano H, Momosaki S et al. Expression of matrix metalloproteinases (MMPs) in cultured hepatocellular carcinoma (HCC) cells and surgically resected HCC tissues. Oncol Rep 2005;13:1043-8
    • (2005) Oncol Rep , vol.13 , pp. 1043-1048
    • Ogasawara, S.1    Yano, H.2    Momosaki, S.3
  • 64
    • 0242266487 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 (MMP-2) is associated with survival in breast carcinoma
    • DOI 10.1038/sj.bjc.6601238
    • Talvensaari-Mattila A, Paakko P Turpeenniemi-Hujanen T. Matrix metalloproteinase-2 (MMP-2) is associated with survival in breast carcinoma. Br J Cancer 2003;89:1270-5 (Pubitemid 37363416)
    • (2003) British Journal of Cancer , vol.89 , Issue.7 , pp. 1270-1275
    • Talvensaari-Mattila, A.1    Paakko, P.2    Turpeenniemi-Hujanen, T.3
  • 65
    • 21444441146 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 and matrix metalloproteinase-9 type IV collagenases in serum of patients with pleural effusions
    • Di Carlo A, Terracciano D, Mariano A et al. Matrix metalloproteinase-2 and matrix metalloproteinase-9 type IV collagenases in serum of patients with pleural effusions. Int J Oncol 2005;26:1363-8
    • (2005) Int J Oncol , vol.26 , pp. 1363-1368
    • Di Carlo, A.1    Terracciano, D.2    Mariano, A.3
  • 66
    • 10044271232 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinases in supraglottic carcinoma and its clinical implication for estimating lymph node metastases
    • DOI 10.1097/01.mlg.0000149467.18822.59
    • Xie M, Sun Y, Li Y. Expression of matrix metalloproteinases in supraglottic carcinoma and its clinical implication for estimating lymph node metastases. Laryngoscope 2004;114:2243-8 (Pubitemid 39602498)
    • (2004) Laryngoscope , vol.114 , Issue.12 , pp. 2243-2248
    • Xie, M.1    Sun, Y.2    Li, Y.3
  • 67
    • 0842311599 scopus 로고    scopus 로고
    • Expressions of Matrix Metalloproteinases in Early-Stage Oral Squamous Cell Carcinoma as Predictive Indicators for Tumor Metastases and Prognosis
    • DOI 10.1158/1078-0432.CCR-0864-02
    • Katayama A, Bandoh N, Kishibe K et al. Expressions of matrix metalloproteinases in early-stage oral squamous cell carcinoma as predictive indicators for tumor metastases and prognosis. Clin Cancer Res 2004;10:634-40 (Pubitemid 38174003)
    • (2004) Clinical Cancer Research , vol.10 , Issue.2 , pp. 634-640
    • Katayama, A.1    Bandoh, N.2    Kishibe, K.3    Takahara, M.4    Ogino, T.5    Nonaka, S.6    Harabuchi, Y.7
  • 70
    • 0036134183 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 and -9 activities correlate with the disease-free survival of oral squamous cell carcinoma patients
    • Yorioka CW, Coletta RD, Alves F, et al. Matrix metalloproteinase-2 and -9 activities correlate with the disease-free survival of oral squamous cell carcinoma patients. Int J Oncol 2002;20:189-94
    • (2002) Int J Oncol , vol.20 , pp. 189-194
    • Yorioka, C.W.1    Coletta, R.D.2    Alves, F.3
  • 71
    • 0035109581 scopus 로고    scopus 로고
    • Enhanced production and activation of progelatinase A mediated by membrane-type 1 matrix metalloproteinase in human oral squamous cell carcinomas: Implications for lymph node metastasis
    • DOI 10.1023/A:1006749501682
    • Shimada T, Nakamura H, Yamashita K et al. Enhanced production and activation of progelatinase A mediated by membrane-type 1 matrix metalloproteinase in human oral squamous cell carcinomas: implications for lymph node metastasis. Clin Exp Metastasis 2000;18:179-88 (Pubitemid 32165252)
    • (2000) Clinical and Experimental Metastasis , vol.18 , Issue.2 , pp. 179-188
    • Shimada, T.1    Nakamura, H.2    Yamashita, K.3    Kawata, R.4    Murakami, Y.5    Fujimoto, N.6    Sato, H.7    Seiki, M.8    Okada, Y.9
  • 72
    • 0028291737 scopus 로고
    • A matrix metalloproteinase expressed on the surface of invasive tumour cells
    • DOI 10.1038/370061a0
    • Sato H, Takino T, Okada Y, et al. A matrix metalloproteinase expressed on the surface of invasive tumour cells. Nature 1994;370:61-5 (Pubitemid 24216953)
    • (1994) Nature , vol.370 , Issue.6484 , pp. 61-65
    • Sato, H.1    Takino, T.2    Okada, Y.3    Cao, J.4    Shinagawa, A.5    Yamamoto, E.6    Seiki, M.7
  • 73
    • 0028935326 scopus 로고
    • Membrane-type matrix metalloproteinase (MT-MMP) gene is expressed in stromal cells of human colon, breast, and head and neck carcinomas
    • Okada A, Bellocq JP, Rouyer N, et al. Membrane-type matrix metalloproteinase (MT-MMP) gene is expressed in stromal cells of human colon, breast, and head and neck carcinomas. Proc Natl Acad Sci USA 1995;92:2730-4
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2730-2734
    • Okada, A.1    Bellocq, J.P.2    Rouyer, N.3
  • 74
    • 0034329334 scopus 로고    scopus 로고
    • MMP and TIMP gene expression in head and neck squamous cell carcinomas and adjacent tissues
    • Birkedal-Hansen B, Pavelic ZP Gluckman JL, et al. MMP and TIMP gene expression in head and neck squamous cell carcinomas and adjacent tissues. Oral Dis 2000;6:376-82
    • (2000) Oral Dis , vol.6 , pp. 376-382
    • Birkedal-Hansen, B.1    Pavelic, Z.P.2    Gluckman, J.L.3
  • 75
    • 0017644625 scopus 로고
    • Further studies on the activation of procollagenase, the latent precursor of bone collagenase. Effects of lysosomal cathepsin B, plasmin and kallikrein, and spontaneous activation
    • Eeckhout Y, Vaes G. Further studies on the activation of procollagenase, the latent precursor of bone collagenase. Effects of lysosomal cathepsin B, plasmin and kallikrein, and spontaneous activation. Biochem J 1977;166:21-31 (Pubitemid 8127122)
    • (1977) Biochemical Journal , vol.166 , Issue.1 , pp. 21-31
    • Eeckhout, Y.1    Vaes, G.2
  • 76
    • 0026754414 scopus 로고
    • Proteolytic processing of the 72,000-Da type IV collagenase by urokinase plasminogen activator
    • Keski-Oja J, Lohi J, Tuuttila A, et al. Proteolytic processing of the 72,000-Da type IV collagenase by urokinase plasminogen activator. Exp Cell Res 1992;202:471-6
    • (1992) Exp Cell Res , vol.202 , pp. 471-476
    • Keski-Oja, J.1    Lohi, J.2    Tuuttila, A.3
  • 77
    • 0034904245 scopus 로고    scopus 로고
    • Urokinase-type plasminogen activator expression and proliferation stimulation in head and neck squamous cell carcinoma in vitro and in situ
    • Schmidt M, Grunsfelder P. Urokinase-type plasminogen activator expression and proliferation stimulation in head and neck squamous cell carcinoma in vitro and in situ. Arch Otolaryngol Head Neck Surg 2001;127:679-82 (Pubitemid 32705874)
    • (2001) Archives of Otolaryngology - Head and Neck Surgery , vol.127 , Issue.6 , pp. 679-682
    • Schmidt, M.1    Grunsfelder, P.2
  • 78
    • 0037192458 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors and cancer: Trials and tribulations
    • DOI 10.1126/science.1067100
    • Coussens LM, Fingleton B Matrisian LM. Matrix metalloproteinase inhibitors and cancer: Trials and tribulations. Science 2002;295:2387-92 (Pubitemid 34270240)
    • (2002) Science , vol.295 , Issue.5564 , pp. 2387-2392
    • Coussens, L.M.1    Fingleton, B.2    Matrisian, L.M.3
  • 79
    • 75949098347 scopus 로고    scopus 로고
    • Vivo characterization of activatable cell penetrating peptides for targeting protease activity in cancer
    • Olson ES, Aguilera TA, Jiang T, et al. In vivo characterization of activatable cell penetrating peptides for targeting protease activity in cancer. Integr Biol (Camb) 2009;1:382-93
    • (2009) Integr Biol (Camb) , vol.1 , pp. 382-393
    • Olson, E.S.1    Aguilera, T.A.2    Jiang, T.3
  • 80
    • 79957842461 scopus 로고    scopus 로고
    • Efficient targeting of head and neck squamous cell carcinoma by systemic administration of a dual uPA and MMP-activated engineered anthrax toxin
    • Schafer JM, Peters DE, Morley T, et al. Efficient targeting of head and neck squamous cell carcinoma by systemic administration of a dual uPA and MMP-activated engineered anthrax toxin. PLoS One 2011;6:e20532
    • (2011) PLoS One , vol.6
    • Schafer, J.M.1    Peters, D.E.2    Morley, T.3
  • 81
    • 36549085160 scopus 로고    scopus 로고
    • Control of matrix metalloproteinase catalytic activity
    • DOI 10.1016/j.matbio.2007.07.001, PII S0945053X0700090X
    • Ra HJ, Parks WC. Control of matrix metalloproteinase catalytic activity. Matrix Biol 2007;26:587-96 (Pubitemid 350180394)
    • (2007) Matrix Biology , vol.26 , Issue.8 , pp. 587-596
    • Ra, H.-J.1    Parks, W.C.2
  • 82
    • 0033742833 scopus 로고    scopus 로고
    • Polymorphism in matrix metalloproteinase gene promoters: Implication in regulation of gene expression and susceptibility of various diseases
    • Ye S. Polymorphism in matrix metalloproteinase gene promoters: implication in regulation of gene expression and susceptibility of various diseases. Matrix Biol 2000;19:623-9
    • (2000) Matrix Biol , vol.19 , pp. 623-629
    • Ye, S.1
  • 83
    • 32644482152 scopus 로고    scopus 로고
    • The role of genetic polymorphisms in the promoters of the matrix metalloproteinase-2 and tissue inhibitor of metalloproteinase-2 genes in head and neck cancer
    • DOI 10.1016/j.oraloncology.2005.07.008, PII S1368837505002307
    • O-Charoenrat P, Khantapura P. The role of genetic polymorphisms in the promoters of the matrix metalloproteinase-2 and tissue inhibitor of metalloproteinase-2 genes in head and neck cancer. Oral Oncol 2006;42:257-67 (Pubitemid 43246757)
    • (2006) Oral Oncology , vol.42 , Issue.3 , pp. 257-267
    • O-Charoenrat, P.1    Khantapura, P.2
  • 84
    • 80054932238 scopus 로고    scopus 로고
    • Role of functional polymorphism of matrix metalloproteinase-2 (-1306 C/T and -168 G/T) and MMP-9 (-1562 C/T) promoter in oral submucous fibrosis and head and neck squamous cell carcinoma in an Indian population
    • Chaudhary AK, Pandya S, Mehrotra R et al. Role of functional polymorphism of matrix metalloproteinase-2 (-1306 C/T and -168 G/T) and MMP-9 (-1562 C/T) promoter in oral submucous fibrosis and head and neck squamous cell carcinoma in an Indian population. Biomarkers 2011;16:577-86
    • (2011) Biomarkers , vol.16 , pp. 577-586
    • Chaudhary, A.K.1    Pandya, S.2    Mehrotra, R.3
  • 85
    • 34249931241 scopus 로고    scopus 로고
    • Strong association of the tissue inhibitor of metalloproteinase-2 polymorphism with an increased risk of oral squamous cell carcinoma in Europeans
    • Vairaktaris E, Yapijakis C Yiannopoulos A, et al. Strong association of the tissue inhibitor of metalloproteinase-2 polymorphism with an increased risk of oral squamous cell carcinoma in Europeans. Oncol Rep 2007;17:963-8
    • (2007) Oncol Rep , vol.17 , pp. 963-968
    • Vairaktaris, E.1    Yapijakis, C.2    Yiannopoulos, A.3
  • 88
    • 0031848158 scopus 로고    scopus 로고
    • Phase I study of intraperitoneal metalloproteinase inhibitor BB94 in patients with malignant ascites
    • Beattie GJ, Smyth JF. Phase I study of intraperitoneal metalloproteinase inhibitor BB94 in patients with malignant ascites. Clin Cancer Res 1998;4:1899-902 (Pubitemid 28369173)
    • (1998) Clinical Cancer Research , vol.4 , Issue.8 , pp. 1899-1902
    • Beattie, G.J.1    Smyth, J.F.2
  • 89
    • 16544372352 scopus 로고    scopus 로고
    • Randomized phase III trial of marimastat versus placebo in patients with metastatic breast cancer who have responding or stable disease after first-line chemotherapy: Eastern Cooperative Oncology Group trial E2196
    • Sparano JA, Bernardo P, Stephenson P et al. Randomized phase III trial of marimastat versus placebo in patients with metastatic breast cancer who have responding or stable disease after first-line chemotherapy: Eastern Cooperative Oncology Group trial E2196. J Clin Oncol 2004;22:4683-90
    • (2004) J Clin Oncol , vol.22 , pp. 4683-4690
    • Sparano, J.A.1    Bernardo, P.2    Stephenson, P.3
  • 95
    • 0035819527 scopus 로고    scopus 로고
    • Development of matrix metalloproteinase inhibitors in cancer therapy
    • Hidalgo M, Eckhardt SG. Development of matrix metalloproteinase inhibitors in cancer therapy. J Natl Cancer Inst 2001;93:178-93 (Pubitemid 32166488)
    • (2001) Journal of the National Cancer Institute , vol.93 , Issue.3 , pp. 178-193
    • Hidalgo, M.1    Eckhardt, S.G.2
  • 98
    • 33645080175 scopus 로고    scopus 로고
    • A randomized phase II trial of the matrix metalloproteinase inhibitor BMS-275291 in hormone-refractory prostate cancer patients with bone metastases
    • Lara PN Jr, Stadler WM, Longmate J et al. A randomized phase II trial of the matrix metalloproteinase inhibitor BMS-275291 in hormone-refractory prostate cancer patients with bone metastases. Clin Cancer Res 2006;12:1556-63
    • (2006) Clin Cancer Res , vol.12 , pp. 1556-1563
    • Lara, P.N.1    Stadler, W.M.2    Longmate, J.3
  • 103
    • 80052296632 scopus 로고    scopus 로고
    • Silibinin inhibits the invasion and migration of renal carcinoma 786-O cells in vitro, inhibits the growth of xenografts in vivo and enhances chemosensitivity to 5-fluorouracil and paclitaxel
    • Chang HR, Chen PN, Yang SF, et al. Silibinin inhibits the invasion and migration of renal carcinoma 786-O cells in vitro, inhibits the growth of xenografts in vivo and enhances chemosensitivity to 5-fluorouracil and paclitaxel. Mol Carcinog 2011;50:811-23
    • (2011) Mol Carcinog , vol.50 , pp. 811-823
    • Chang, H.R.1    Chen, P.N.2    Yang, S.F.3
  • 104
    • 84865683855 scopus 로고    scopus 로고
    • Silibinin inhibits tumor growth in a murine orthotopic hepatocarcinoma model and activates the TRAIL apoptotic signaling pathway
    • Bousserouel S, Bour G, Kauntz H, et al. Silibinin inhibits tumor growth in a murine orthotopic hepatocarcinoma model and activates the TRAIL apoptotic signaling pathway. Anticancer Res 2012;32:2455-62
    • (2012) Anticancer Res , vol.32 , pp. 2455-2462
    • Bousserouel, S.1    Bour, G.2    Kauntz, H.3
  • 105
    • 84866736330 scopus 로고    scopus 로고
    • Therapeutic efficacy of silibinin on human neuroblastoma cells: Akt and NF-kappaB expressions may play an important role in silibinin-induced response
    • Yousefi M, Ghaffari SH, Soltani BM et al. Therapeutic efficacy of silibinin on human neuroblastoma cells: Akt and NF-kappaB expressions may play an important role in silibinin-induced response. Neurochem Res 2012;37:2053-63
    • (2012) Neurochem Res , vol.37 , pp. 2053-2063
    • Yousefi, M.1    Ghaffari, S.H.2    Soltani, B.M.3
  • 106
    • 77952317006 scopus 로고    scopus 로고
    • A study of high-dose oral silybin-phytosome followed by prostatectomy in patients with localized prostate cancer
    • Flaig TW, Glode M, Gustafson D, et al. A study of high-dose oral silybin-phytosome followed by prostatectomy in patients with localized prostate cancer. Prostate 2010;70:848-55
    • (2010) Prostate , vol.70 , pp. 848-855
    • Flaig, T.W.1    Glode, M.2    Gustafson, D.3
  • 107
    • 1242351803 scopus 로고    scopus 로고
    • Cytotoxic activity of coumarins from the fruits of Cnidium monnieri on leukemia cell lines
    • Yang LL, Wang MC, Chen LG, et al. Cytotoxic activity of coumarins from the fruits of Cnidium monnieri on leukemia cell lines. Planta Med 2003;69:1091-5
    • (2003) Planta Med , vol.69 , pp. 1091-1095
    • Yang, L.L.1    Wang, M.C.2    Chen, L.G.3
  • 108
    • 84860511960 scopus 로고    scopus 로고
    • Osthole inhibits the invasive ability of human lung adenocarcinoma cells via suppression of NF-kappaB-mediated matrix metalloproteinase-9 expression
    • Kao SJ, Su JL, Chen CK, et al. Osthole inhibits the invasive ability of human lung adenocarcinoma cells via suppression of NF-kappaB-mediated matrix metalloproteinase-9 expression. Toxicol Appl Pharmacol 2012;261:105-15
    • (2012) Toxicol Appl Pharmacol , vol.261 , pp. 105-115
    • Kao, S.J.1    Su, J.L.2    Chen, C.K.3
  • 109
    • 77955210698 scopus 로고    scopus 로고
    • Effects of osthole on migration and invasion in breast cancer cells
    • Yang D, Gu T, Wang T, et al. Effects of osthole on migration and invasion in breast cancer cells. Biosci Biotechnol Biochem 2010;74:1430-4
    • (2010) Biosci Biotechnol Biochem , vol.74 , pp. 1430-1434
    • Yang, D.1    Gu, T.2    Wang, T.3
  • 114
    • 0037051090 scopus 로고    scopus 로고
    • Inhibition of cell proliferation, invasion, tumor growth and metastasis by an oral non-antimicrobial tetracycline analog (COL-3) in a metastatic prostate cancer model
    • DOI 10.1002/ijc.10168
    • Lokeshwar BL, Selzer MG, Zhu BQ et al. Inhibition of cell proliferation invasion, tumor growth and metastasis by an oral non-antimicrobial tetracycline analog (COL-3) in a metastatic prostate cancer model. Int J Cancer 2002;98:297-309 (Pubitemid 34150817)
    • (2002) International Journal of Cancer , vol.98 , Issue.2 , pp. 297-309
    • Lokeshwar, B.L.1    Selzer, M.G.2    Zhu, B.-Q.3    Block, N.L.4    Golub, L.M.5
  • 116
    • 34250630512 scopus 로고    scopus 로고
    • A phase II and pharmacological study of the matrix metalloproteinase inhibitor (MMPI) COL-3 in patients with advanced soft tissue sarcomas
    • DOI 10.1007/s10637-006-9031-6
    • Chu QS, Forouzesh B, Syed S, et al. A phase II and pharmacological study of the matrix metalloproteinase inhibitor (MMPI) COL-3 in patients with advanced soft tissue sarcomas. Invest New Drugs 2007;25:359-67 (Pubitemid 46944843)
    • (2007) Investigational New Drugs , vol.25 , Issue.4 , pp. 359-367
    • Chu, Q.S.C.1    Forouzesh, B.2    Syed, S.3    Mita, M.4    Schwartz, G.5    Copper, J.6    Curtright, J.7    Rowinsky, E.K.8
  • 118
    • 0032527618 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase-2 protection of matrix metalloproteinase-2 from degradation by plasmin is reversed by divalent cation chelator EDTA and the bisphosphonate alendronate
    • Farina AR, Tacconelli A, Teti A, et al. Tissue inhibitor of metalloproteinase-2 protection of matrix metalloproteinase-2 from degradation by plasmin is reversed by divalent cation chelator EDTA and the bisphosphonate alendronate. Cancer Res 1998;58:2957-60 (Pubitemid 28335069)
    • (1998) Cancer Research , vol.58 , Issue.14 , pp. 2957-2960
    • Farina, A.R.1    Tacconelli, A.2    Teti, A.3    Gulino, A.4    Mackay, A.R.5
  • 119
    • 33745779881 scopus 로고    scopus 로고
    • Matrix metalloproteases in head and neck cancer
    • DOI 10.1002/hed.20365
    • Rosenthal EL, Matrisian LM. Matrix metalloproteases in head and neck cancer. Head Neck 2006;28:639-48 (Pubitemid 44025114)
    • (2006) Head and Neck , vol.28 , Issue.7 , pp. 639-648
    • Rosenthal, E.L.1    Matrisian, L.M.2
  • 120
    • 33644545381 scopus 로고    scopus 로고
    • Validating matrix metalloproteinases as drug targets and anti-targets for cancer therapy
    • DOI 10.1038/nrc1821, PII N1821
    • Overall CM, Kleifeld O. Tumour microenvironment - opinion: validating matrix metalloproteinases as drug targets and anti-targets for cancer therapy. Nat Rev Cancer 2006;6:227-39 (Pubitemid 43292566)
    • (2006) Nature Reviews Cancer , vol.6 , Issue.3 , pp. 227-239
    • Overall, C.M.1    Kleifeld, O.2
  • 121
    • 77149171184 scopus 로고    scopus 로고
    • Structural and functional bases for allosteric control of MMP activities: Can it pave the path for selective inhibition?
    • Sela-Passwell N, Rosenblum G Shoham T, et al. Structural and functional bases for allosteric control of MMP activities: Can it pave the path for selective inhibition? Biochim Biophys Acta 2010;1803:29-38
    • (2010) Biochim Biophys Acta , vol.1803 , pp. 29-38
    • Sela-Passwell, N.1    Rosenblum, G.2    Shoham, T.3
  • 122
    • 3142698646 scopus 로고    scopus 로고
    • Peptide inhibition of catalytic and noncatalytic activities of matrix metalloproteinase-9 blocks tumor cell migration and invasion
    • DOI 10.1074/jbc.M401601200
    • Bjorklund M, Heikkila P, Koivunen E. Peptide inhibition of catalytic and noncatalytic activities of matrix metalloproteinase-9 blocks tumor cell migration and invasion. J Biol Chem 2004;279:29589-97 (Pubitemid 38915841)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.28 , pp. 29589-29597
    • Bjorklund, M.1    Heikkila, P.2    Koivunen, E.3
  • 123
    • 78149231567 scopus 로고    scopus 로고
    • Role of matrix metalloproteinase-9 dimers in cell migration: Design of inhibitory peptides
    • Dufour A, Zucker S, Sampson NS, et al. Role of matrix metalloproteinase-9 dimers in cell migration: Design of inhibitory peptides. J Biol Chem 2010;285:35944-56
    • (2010) J Biol Chem , vol.285 , pp. 35944-35956
    • Dufour, A.1    Zucker, S.2    Sampson, N.S.3
  • 125
    • 78650048935 scopus 로고    scopus 로고
    • The regulatory mechanism of extracellular Hsp90{alpha} on matrix metalloproteinase-2 processing and tumor angiogenesis
    • Song X, Wang X, Zhuo W, et al. The regulatory mechanism of extracellular Hsp90{alpha} on matrix metalloproteinase-2 processing and tumor angiogenesis. J Biol Chem 2010;285:40039-49
    • (2010) J Biol Chem , vol.285 , pp. 40039-40049
    • Song, X.1    Wang, X.2    Zhuo, W.3
  • 126
    • 77955372512 scopus 로고    scopus 로고
    • Monoclonal antibody 4C5 prevents activation of MMP2 and MMP9 by disrupting their interaction with extracellular HSP90 and inhibits formation of metastatic breast cancer cell deposits
    • Stellas D, El Hamidieh A, Patsavoudi E. Monoclonal antibody 4C5 prevents activation of MMP2 and MMP9 by disrupting their interaction with extracellular HSP90 and inhibits formation of metastatic breast cancer cell deposits. BMC Cell Biol 2010;11:51
    • (2010) BMC Cell Biol , vol.11 , pp. 51
    • Stellas, D.1    El Hamidieh, A.2    Patsavoudi, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.