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

Bibliography

• Myers JN, Greenberg JS, Mo V, Extracapsular spread. A significant predictor of treatment failure in patients with squamous cell carcinoma of the tongue. Cancer 2001;92:3030-6
   PubMedGoogle Scholar
• Woodhouse EC, Chuaqui RF, Liotta LA. General mechanisms of metastasis. Cancer 1997;80:1529-37
   PubMed Web of Science ®Google Scholar
• Liotta LA. Tumor invasion and metastases–role of the extracellular matrix: rhoads Memorial Award lecture. Cancer Res 1986;46:1-7
   PubMed Web of Science ®Google Scholar
• Wu CY, Wu MS, Chen YJ, Clinicopathological significance of MMP-2 and TIMP-2 genotypes in gastric cancer. Eur J Cancer 2007;43:799-808
   Google Scholar
• Yu C, Zhou Y, Miao X, 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
   PubMed Web of Science ®Google Scholar
• Arenas-Huertero FJ, Herrera-Goepfert R, Delgado-Chavez R, 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
   Google Scholar
• 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
   PubMedGoogle Scholar
• Patel BP, Shah PM, Rawal UM, Activation of MMP-2 and MMP-9 in patients with oral squamous cell carcinoma. J Surg Oncol 2005;90:81-8
   PubMed Web of Science ®Google Scholar
• Zhou CX, Gao Y, Johnson NW, 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
   PubMed Web of Science ®Google Scholar
• Jezierska A, Motyl T. Matrix metalloproteinase-2 involvement in breast cancer progression: a mini-review. Med Sci Monit 2009;15:RA32-40
   PubMed Web of Science ®Google Scholar
• Kandasamy AD, Chow AK, Ali MA, Matrix metalloproteinase-2 and myocardial oxidative stress injury: beyond the matrix. Cardiovasc Res 2010;85:413-23
   PubMed Web of Science ®Google Scholar
• 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
   PubMed Web of Science ®Google Scholar
• Hoyhtya M, Turpeenniemi-Hujanen T, Stetler-Stevenson W, Monoclonal antibodies to type IV collagenase recognize a protein with limited sequence homology to interstitial collagenase and stromelysin. FEBS Lett 1988;233:109-13
   PubMed Web of Science ®Google Scholar
• Egeblad M, Werb Z. New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer 2002;2:161-74
   PubMed Web of Science ®Google Scholar
• Nagase H, Woessner JF Jr. Matrix metalloproteinases. J Biol Chem 1999;274:21491-4
   PubMed Web of Science ®Google Scholar
• 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
   PubMed Web of Science ®Google Scholar
• 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
   PubMed Web of Science ®Google Scholar
• 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
   PubMed Web of Science ®Google Scholar
• Lin SC, Lo SS, Liu CJ, Functional genotype in matrix metalloproteinases-2 promoter is a risk factor for oral carcinogenesis. J Oral Pathol Med 2004;33:405-9
   Web of Science ®Google Scholar
• Woessner JF Jr. Role of matrix proteases in processing enamel proteins. Connect Tissue Res 1998;39:69-73; discussion 141-9
   PubMed Web of Science ®Google Scholar
• Okamoto T, Akaike T, Sawa T, Activation of matrix metalloproteinases by peroxynitrite-induced protein S-glutathiolation via disulfide S-oxide formation. J Biol Chem 2001;276:29596-602
   PubMed Web of Science ®Google Scholar
• Morgunova E, Tuuttila A, Bergmann U, Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed. Science 1999;284:1667-70
   PubMed Web of Science ®Google Scholar
• Rauch BH, Bretschneider E, Braun M, 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
   PubMed Web of Science ®Google Scholar
• Zucker S, Conner C, DiMassmo BI, Thrombin induces the activation of progelatinase A in vascular endothelial cells. Physiologic regulation of angiogenesis. J Biol Chem 1995;270:23730-8
   PubMed Web of Science ®Google Scholar
• Cao J, Sato H, Takino T, 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
   PubMed Web of Science ®Google Scholar
• 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
   Google Scholar
• Helvering LM, Adrian MD, Geiser AG, Differential effects of estrogen and raloxifene on messenger RNA and matrix metalloproteinase 2 activity in the rat uterus. Biol Reprod 2005;72:830-41
   PubMed Web of Science ®Google Scholar
• Liang Q, Xiong H, Gao G, Inhibition of basigin expression in glioblastoma cell line via antisense RNA reduces tumor cell invasion and angiogenesis. Cancer Biol Ther 2005;4:759-62
   PubMed Web of Science ®Google Scholar
• Rosenthal EL, Shreenivas S, Peters GE, Expression of extracellular matrix metalloprotease inducer in laryngeal squamous cell carcinoma. Laryngoscope 2003;113:1406-10
   Google Scholar
• Yang X, Zhang P, Ma Q, EMMPRIN contributes to the in vitro invasion of human salivary adenoid cystic carcinoma cells. Oncol Rep 2012;27:1123-7
   Google Scholar
• Vigneswaran N, Beckers S, Waigel S, Increased EMMPRIN (CD 147) expression during oral carcinogenesis. Exp Mol Pathol 2006;80:147-59
   PubMed Web of Science ®Google Scholar
• Lescaille G, Menashi S, Cavelier-Balloy B, EMMPRIN/CD147 up-regulates urokinase-type plasminogen activator: implications in oral tumor progression. BMC Cancer 2012;12:115
   PubMed Web of Science ®Google Scholar
• Dang D, Atakilit A, Ramos DM. EMMPRIN modulates migration and deposition of TN-C in oral squamous carcinoma. Anticancer Res 2008;28:2049-54
   PubMed Web of Science ®Google Scholar
• Yang X, Zhang P, Ma Q, 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
   PubMed Web of Science ®Google Scholar
• Kessenbrock K, Plaks V, Werb Z. Matrix metalloproteinases: regulators of the tumor microenvironment. Cell 2010;141:52-67
   PubMed Web of Science ®Google Scholar
• Klein T, Bischoff R. Physiology and pathophysiology of matrix metalloproteases. Amino Acids 2011;41:271-90
   PubMed Web of Science ®Google Scholar
• 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
   PubMed Web of Science ®Google Scholar
• 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
   PubMed Web of Science ®Google Scholar
• Deryugina EI, Quigley JP. Pleiotropic roles of matrix metalloproteinases in tumor angiogenesis: contrasting, overlapping and compensatory functions. Biochim Biophys Acta 2010;1803:103-20
   PubMed Web of Science ®Google Scholar
• Baluk P, Raymond WW, Ator E, Matrix metalloproteinase-2 and -9 expression increases in Mycoplasma-infected airways but is not required for microvascular remodeling. Am J Physiol Lung Cell Mol Physiol 2004;287:L307-17
   Google Scholar
• Hotary K, Li XY, Allen E, A cancer cell metalloprotease triad regulates the basement membrane transmigration program. Genes Dev 2006;20:2673-86
   PubMed Web of Science ®Google Scholar
• Sabeh F, Li XY, Saunders TL, Secreted versus membrane-anchored collagenases: relative roles in fibroblast-dependent collagenolysis and invasion. J Biol Chem 2009;284:23001-11
   PubMedGoogle Scholar
• Giannelli G, Falk-Marzillier J, Schiraldi O, Induction of cell migration by matrix metalloprotease-2 cleavage of laminin-5. Science 1997;277:225-8
   PubMed Web of Science ®Google Scholar
• Mantovani A, Allavena P, Sica A, Cancer-related inflammation. Nature 2008;454:436-44
   PubMed Web of Science ®Google Scholar
• Tian M, Neil JR, Schiemann WP. Transforming growth factor-beta and the hallmarks of cancer. Cell Signal 2011;23:951-62
   PubMed Web of Science ®Google Scholar
• Levi E, Fridman R, Miao HQ, Matrix metalloproteinase 2 releases active soluble ectodomain of fibroblast growth factor receptor 1. Proc Natl Acad Sci USA 1996;93:7069-74
   PubMed Web of Science ®Google Scholar
• 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
   PubMed Web of Science ®Google Scholar
• Bjorklund M, Koivunen E. Gelatinase-mediated migration and invasion of cancer cells. Biochim Biophys Acta 2005;1755:37-69
   PubMed Web of Science ®Google Scholar
• McQuibban GA, Gong JH, Tam EM, Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3. Science 2000;289:1202-6
   PubMed Web of Science ®Google Scholar
• Hofmann UB, Houben R, Brocker EB, Role of matrix metalloproteinases in melanoma cell invasion. Biochimie 2005;87:307-14
   PubMed Web of Science ®Google Scholar
• 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
   PubMed Web of Science ®Google Scholar
• Hahn-Dantona E, Ruiz JF, Bornstein P, 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
   PubMed Web of Science ®Google Scholar
• 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
   PubMed Web of Science ®Google Scholar
• Brooks PC, Stromblad S, Sanders LC, Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin alpha v beta 3. Cell 1996;85:683-93
   PubMed Web of Science ®Google Scholar
• Menashi S, Dehem M, Souliac I, Density-dependent regulation of cell-surface association of matrix metalloproteinase-2 (MMP-2) in breast-carcinoma cells. Int J Cancer 1998;75:259-65
   Google Scholar
• Hofmann UB, Westphal JR, Van Kraats AA, 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
   PubMedGoogle Scholar
• Silletti S, Kessler T, Goldberg J, Disruption of matrix metalloproteinase 2 binding to integrin alpha vbeta 3 by an organic molecule inhibits angiogenesis and tumor growth in vivo. Proc Natl Acad Sci USA 2001;98:119-24
   PubMed Web of Science ®Google Scholar
• Stefanidakis M, Bjorklund M, Ihanus E, Identification of a negatively charged peptide motif within the catalytic domain of progelatinases that mediates binding to leukocyte beta 2 integrins. J Biol Chem 2003;278:34674-84
   PubMed Web of Science ®Google Scholar
• Levkau B, Kenagy RD, Karsan A, Activation of metalloproteinases and their association with integrins: an auxiliary apoptotic pathway in human endothelial cells. Cell Death Differ 2002;9:1360-7
   PubMed Web of Science ®Google Scholar
• Rupp PA, Visconti RP, Czirok A, 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
   Google Scholar
• Chetty C, Lakka SS, Bhoopathi P, MMP-2 alters VEGF expression via alphaVbeta3 integrin-mediated PI3K/AKT signaling in A549 lung cancer cells. Int J Cancer 2010;127:1081-95
   PubMed Web of Science ®Google Scholar
• Agnantis NJ, Goussia AC, Batistatou A, Tumor markers in cancer patients. an update of their prognostic significance. Part II. In Vivo 2004;18:481-8
   Google Scholar
• Ogasawara S, Yano H, Momosaki S, Expression of matrix metalloproteinases (MMPs) in cultured hepatocellular carcinoma (HCC) cells and surgically resected HCC tissues. Oncol Rep 2005;13:1043-8
   Google Scholar
• 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
   PubMed Web of Science ®Google Scholar
• Di Carlo A, Terracciano D, Mariano A, Matrix metalloproteinase-2 and matrix metalloproteinase-9 type IV collagenases in serum of patients with pleural effusions. Int J Oncol 2005;26:1363-8
   Google Scholar
• 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
   PubMed Web of Science ®Google Scholar
• Katayama A, Bandoh N, Kishibe K, 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
   PubMed Web of Science ®Google Scholar
• Chung CH, Parker JS, Karaca G, Molecular classification of head and neck squamous cell carcinomas using patterns of gene expression. Cancer Cell 2004;5:489-500
   PubMed Web of Science ®Google Scholar
• Bogusiewicz M, Stryjecka-Zimmer M, Szymanski M, Activity of matrix metalloproteinases-2 and -9 in advanced laryngeal cancer. Otolaryngol Head Neck Surg 2003;128:132-6
   Google Scholar
• Yorioka CW, Coletta RD, Alves F, 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
   PubMed Web of Science ®Google Scholar
• Shimada T, Nakamura H, Yamashita K, 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
   Google Scholar
• Sato H, Takino T, Okada Y, A matrix metalloproteinase expressed on the surface of invasive tumour cells. Nature 1994;370:61-5
   PubMed Web of Science ®Google Scholar
• Okada A, Bellocq JP, Rouyer N, 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
   PubMed Web of Science ®Google Scholar
• Birkedal-Hansen B, Pavelic ZP, Gluckman JL, MMP and TIMP gene expression in head and neck squamous cell carcinomas and adjacent tissues. Oral Dis 2000;6:376-82
   PubMedGoogle Scholar
• 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
   PubMed Web of Science ®Google Scholar
• Keski-Oja J, Lohi J, Tuuttila A, Proteolytic processing of the 72,000-Da type IV collagenase by urokinase plasminogen activator. Exp Cell Res 1992;202:471-6
   PubMed Web of Science ®Google Scholar
• 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
   Google Scholar
• Coussens LM, Fingleton B, Matrisian LM. Matrix metalloproteinase inhibitors and cancer: trials and tribulations. Science 2002;295:2387-92
   PubMed Web of Science ®Google Scholar
• Olson ES, Aguilera TA, Jiang T, In vivo characterization of activatable cell penetrating peptides for targeting protease activity in cancer. Integr Biol (Camb) 2009;1:382-93
   PubMed Web of Science ®Google Scholar
• Schafer JM, Peters DE, Morley T, 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
   Google Scholar
• Ra HJ, Parks WC. Control of matrix metalloproteinase catalytic activity. Matrix Biol 2007;26:587-96
   PubMed Web of Science ®Google Scholar
• 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
   PubMed Web of Science ®Google Scholar
• 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
   PubMed Web of Science ®Google Scholar
• Chaudhary AK, Pandya S, Mehrotra R, 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
   PubMed Web of Science ®Google Scholar
• Vairaktaris E, Yapijakis C, Yiannopoulos A, 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
   PubMed Web of Science ®Google Scholar
• Nelson AR, Fingleton B, Rothenberg ML, Matrix metalloproteinases: biologic activity and clinical implications. J Clin Oncol 2000;18:1135-49
   PubMed Web of Science ®Google Scholar
• Macaulay VM, O'Byrne KJ, Saunders MP, Phase I study of intrapleural batimastat (BB-94), a matrix metalloproteinase inhibitor, in the treatment of malignant pleural effusions. Clin Cancer Res 1999;5:513-20
   PubMed Web of Science ®Google Scholar
• Beattie GJ, Smyth JF. Phase I study of intraperitoneal metalloproteinase inhibitor BB94 in patients with malignant ascites. Clin Cancer Res 1998;4:1899-902
   PubMed Web of Science ®Google Scholar
• Sparano JA, Bernardo P, Stephenson P, 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
   PubMed Web of Science ®Google Scholar
• Tierney GM, Griffin NR, Stuart RC, A pilot study of the safety and effects of the matrix metalloproteinase inhibitor marimastat in gastric cancer. Eur J Cancer 1999;35:563-8
   PubMed Web of Science ®Google Scholar
• Shalinsky DR, Brekken J, Zou H, Broad antitumor and antiangiogenic activities of AG3340, a potent and selective MMP inhibitor undergoing advanced oncology clinical trials. Ann NY Acad Sci 1999;878:236-70
   PubMed Web of Science ®Google Scholar
• Bissett D, O'Byrne KJ, von Pawel J, Phase III study of matrix metalloproteinase inhibitor prinomastat in non-small-cell lung cancer. J Clin Oncol 2005;23:842-9
   PubMed Web of Science ®Google Scholar
• Rowinsky EK, Humphrey R, Hammond LA, Phase I and pharmacologic study of the specific matrix metalloproteinase inhibitor BAY 12-9566 on a protracted oral daily dosing schedule in patients with solid malignancies. J Clin Oncol 2000;18:178-86
   PubMed Web of Science ®Google Scholar
• Heath EI, O'Reilly S, Humphrey R, Phase I trial of the matrix metalloproteinase inhibitor BAY12-9566 in patients with advanced solid tumors. Cancer Chemother Pharmacol 2001;48:269-74
   PubMed Web of Science ®Google Scholar
• Hidalgo M, Eckhardt SG. Development of matrix metalloproteinase inhibitors in cancer therapy. J Natl Cancer Inst 2001;93:178-93
   PubMed Web of Science ®Google Scholar
• Ferrante K, Winograd B, Canetta R. Promising new developments in cancer chemotherapy. Cancer Chemother Pharmacol 1999;43(Suppl):S61-8
   Google Scholar
• Rizvi NA, Humphrey JS, Ness EA, A phase I study of oral BMS-275291, a novel nonhydroxamate sheddase-sparing matrix metalloproteinase inhibitor, in patients with advanced or metastatic cancer. Clin Cancer Res 2004;10:1963-70
   PubMed Web of Science ®Google Scholar
• Lara PN Jr, Stadler WM, Longmate J, 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
   PubMed Web of Science ®Google Scholar
• Miller KD, Saphner TJ, Waterhouse DM, A randomized phase II feasibility trial of BMS-275291 in patients with early stage breast cancer. Clin Cancer Res 2004;10:1971-5
   PubMed Web of Science ®Google Scholar
• Leighl NB, Paz-Ares L, Douillard JY, Randomized phase III study of matrix metalloproteinase inhibitor BMS-275291 in combination with paclitaxel and carboplatin in advanced non-small-cell lung cancer: national Cancer Institute of Canada-Clinical Trials Group Study BR.18. J Clin Oncol 2005;23:2831-9
   PubMed Web of Science ®Google Scholar
• Levitt NC, Eskens FA, O'Byrne KJ, Phase I and pharmacological study of the oral matrix metalloproteinase inhibitor, MMI270 (CGS27023A), in patients with advanced solid cancer. Clin Cancer Res 2001;7:1912-22
   PubMed Web of Science ®Google Scholar
• Eatock M, Cassidy J, Johnson J, A dose-finding and pharmacokinetic study of the matrix metalloproteinase inhibitor MMI270 (previously termed CGS27023A) with 5-FU and folinic acid. Cancer Chemother Pharmacol 2005;55:39-46
   PubMed Web of Science ®Google Scholar
• Chang HR, Chen PN, Yang SF, 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
   Google Scholar
• Bousserouel S, Bour G, Kauntz H, Silibinin inhibits tumor growth in a murine orthotopic hepatocarcinoma model and activates the TRAIL apoptotic signaling pathway. Anticancer Res 2012;32:2455-62
   PubMed Web of Science ®Google Scholar
• Yousefi M, Ghaffari SH, Soltani BM, 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
   Google Scholar
• Flaig TW, Glode M, Gustafson D, A study of high-dose oral silybin-phytosome followed by prostatectomy in patients with localized prostate cancer. Prostate 2010;70:848-55
   PubMed Web of Science ®Google Scholar
• Yang LL, Wang MC, Chen LG, Cytotoxic activity of coumarins from the fruits of Cnidium monnieri on leukemia cell lines. Planta Med 2003;69:1091-5
   PubMed Web of Science ®Google Scholar
• Kao SJ, Su JL, Chen CK, 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
   Google Scholar
• Yang D, Gu T, Wang T, Effects of osthole on migration and invasion in breast cancer cells. Biosci Biotechnol Biochem 2010;74:1430-4
   PubMed Web of Science ®Google Scholar
• Dredge K. AE-941 (AEterna). Curr Opin Investig Drugs 2004;5:668-77
   Google Scholar
• Dupont E, Falardeau P, Mousa SA, Antiangiogenic and antimetastatic properties of Neovastat (AE-941), an orally active extract derived from cartilage tissue. Clin Exp Metastasis 2002;19:145-53
   PubMedGoogle Scholar
• Batist G, Patenaude F, Champagne P, Neovastat (AE-941) in refractory renal cell carcinoma patients: report of a phase II trial with two dose levels. Ann Oncol 2002;13:1259-63
   PubMed Web of Science ®Google Scholar
• Latreille J, Batist G, Laberge F, Phase I/II trial of the safety and efficacy of AE-941 (Neovastat) in the treatment of non-small-cell lung cancer. Clin Lung Cancer 2003;4:231-6
   PubMedGoogle Scholar
• Lokeshwar BL, Selzer MG, Zhu BQ, 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
   PubMed Web of Science ®Google Scholar
• Cianfrocca M, Cooley TP, Lee JY, Matrix metalloproteinase inhibitor COL-3 in the treatment of AIDS-related Kaposi's sarcoma: a phase I AIDS malignancy consortium study. J Clin Oncol 2002;20:153-9
   PubMed Web of Science ®Google Scholar
• Chu QS, Forouzesh B, Syed S, 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
   PubMedGoogle Scholar
• Teronen O, Heikkila P, Konttinen YT, MMP inhibition and downregulation by bisphosphonates. Ann NY Acad Sci 1999;878:453-65
   PubMed Web of Science ®Google Scholar
• Farina AR, Tacconelli A, Teti A, 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
   PubMed Web of Science ®Google Scholar
• Rosenthal EL, Matrisian LM. Matrix metalloproteases in head and neck cancer. Head Neck 2006;28:639-48
   PubMed Web of Science ®Google Scholar
• 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
   PubMed Web of Science ®Google Scholar
• Sela-Passwell N, Rosenblum G, Shoham T, 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
   PubMed Web of Science ®Google Scholar
• 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
   PubMed Web of Science ®Google Scholar
• Dufour A, Zucker S, Sampson NS, Role of matrix metalloproteinase-9 dimers in cell migration: design of inhibitory peptides. J Biol Chem 2010;285:35944-56
   PubMed Web of Science ®Google Scholar
• Eustace BK, Sakurai T, Stewart JK, Functional proteomic screens reveal an essential extracellular role for hsp90 alpha in cancer cell invasiveness. Nat Cell Biol 2004;6:507-14
   PubMed Web of Science ®Google Scholar
• Song X, Wang X, Zhuo W, The regulatory mechanism of extracellular Hsp90{alpha} on matrix metalloproteinase-2 processing and tumor angiogenesis. J Biol Chem 2010;285:40039-49
   Web of Science ®Google Scholar
• 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
   Google Scholar