참고문헌
-
Agrez M, Chen A, Cone R I, Pytela R, Sheppard D (1994). The
${\alpha}5{\beta}6$ integrin promotes proliferation of colon carcinoma cells through a unique region of the b6 cytoplasmic domain. J Cell Biol, 127, 547-56. https://doi.org/10.1083/jcb.127.2.547 - Basbaum C B, Werb Z (1996). Focalized proteolysis: spatial and temporal regulation of extracellular matrix at the cell surface. Current Opinions in Cell Biology, 8, 731-38. https://doi.org/10.1016/S0955-0674(96)80116-5
- Benbow U, Brinckerhoff C E (1997). The AP-1 site and MMP gene regulation: what is all the fuss about? Matrix Biol, 15, 519-26. https://doi.org/10.1016/S0945-053X(97)90026-3
- Birchmeier C, Birchmeier W, Brand- saberi B (1996). Epithelialmesenchymal transition in cancer progression. ActaAnat, 156, 217-26.
- Brew K, Dinakarpandian D, Nagase H (2000).Tissue inhibitors of metalloproteinases: evolution, structure and function. Biochem Biophys Acta, 1477, 267-83.
- Cao Z G, Li C Z (2006). A single nucleotide polymorphism in the matrix metalloproteinase-1 promoter enhances oral squamous cell carcinoma susceptibility in a Chinese population. Oral Oncol, 42, 32-8. https://doi.org/10.1016/j.ooe.2005.08.006
- Chambers A F, Groom A C, Macdonald I C (2002). Dissemination and growth of cancer cells in metastatic sites. Nat Rev Cancer, 2, 563-72. https://doi.org/10.1038/nrc865
- Chambers A F, Matrisian L M (1997). Changing views of the role of matrix metalloproteinases in metastasis. J Natl Cancer Inst, 89, 1260-70. https://doi.org/10.1093/jnci/89.17.1260
- Chaudhary A K, Singh M, Bharti A C, et al (2010). Genetic polymorphism of matrix metalloproteinases and their inhibitors in potentially malignant lesions of the head and neck. J Biomed Sci, 17, 10. https://doi.org/10.1186/1423-0127-17-10
- Chen L C, Noelken M E, Nagase H(1993). Disruption of the cysteine-75 and zinc ion coordination is not sufficient to activate the precursor of human matrix metalloproteinase 3(stromelysin- 1). Biochemistry, 32, 10289-295. https://doi.org/10.1021/bi00090a003
- Choi S,Myers J N (2008). Molecular pathogenesis of oral squamous cell carcinoma: implications for Therapy. J Dent Res, 87, 14-32. https://doi.org/10.1177/154405910808700104
- Cornelius L A, et al (1998). Matrix metalloproteinases generate angiostatin: effects on neovascularisation. J Immunol, 161,6845-52.
- Curran S,Murray G I (1999). Matrix metalloproteinases in tumour invasion and metastasis. J Pathol, 189, 300-8. https://doi.org/10.1002/(SICI)1096-9896(199911)189:3<300::AID-PATH456>3.0.CO;2-C
- Denhardt D T, Feng B, Edwards D R, Cocuzzi E T, Malyanker U M (1993). Tissue inhibitor of metalloproteinases(TIMP aka EPA): structure, control of expression and biological functions. PharmacolTher, 59, 329-341.
- Eccles S A et al (1996). Control of lymphatic and hematogenous metastasis of a rat mammary carcinoma by the matrix metalloproteinase inhibitor batimastat (BB-94). Cancer Res, 56, 2815-22.
- Egeblad M ,Werb Z (2002). New function for the matrix metalloproteinases in cancer progression. Nature reviews, 2, 161-74.
- Falardeau P, Champagne P, Poyet P, Hariton C, Dupont E (2001). Neovastat, a naturally occurring multifunctional antiangiogenic drug, in phase III clinical trials. Semin Oncol, 28, 620-5. https://doi.org/10.1016/S0093-7754(01)90035-1
- Ferreras M, Felbor U, Lenhard T, Olsen B R, Delaisse J (2000). Generation and degradation of human endostatin protein by various proteinases. FEBS Lett, 486, 247-51. https://doi.org/10.1016/S0014-5793(00)02249-3
- Folgueras A R, Pendas A M, Sanchez L M, Lopez-otin C (2004). Matrix metalloproteinases in cancer: from new function to improved inhibition strategies. Int J Dev Biol, 48, 411-24. https://doi.org/10.1387/ijdb.041811af
- Ganea E, Trifan M, Laslo A C, Putina G, Cristescu C (2007). Matrix metalloproteinases: useful and deleterious. Biochem Soc Trans, 35, 689-91. https://doi.org/10.1042/BST0350689
- Gialeli C, Kletsas D, Mavroudis D, Kalofonos H P, Tzanakakis G N (2009). Targetting epidermal growth factor receptor in solid tumours: critical evaluation of the biological importance of therapeutic monoclonal antibodies. Curr Med Chem, 16, 3797-804. https://doi.org/10.2174/092986709789177984
- Gialeli C, Theocharis A D, Karamanos N K (2011). Role of matrix metalloproteinases in cancer progression and their pharmacological targeting. FEBS J, 278, 16-27. https://doi.org/10.1111/j.1742-4658.2010.07919.x
- Gorelik L, Flavell R A (2001). Immune mediated eradication of tumours through the blockage of transforming growth factor-beta signalling in T-cells. Nature Med, 7, 1118-22. https://doi.org/10.1038/nm1001-1118
- Greene J, Wang M, Liu Y E, et al (1996). Molecular cloning and characterisation of human tissue inhibitor of metalloproteinase 4. J BiolChem, 271, 30375-380.
- Hanahan D, Folkman J (1996). Patterns and emerging mechanisms of the angiogenic switch during tumorigenesis. Cell, 86, 353-64. https://doi.org/10.1016/S0092-8674(00)80108-7
- Hanahan D, Weinberg R A (2000). The hallmarks of cancer. Cell, 100, 57-70. https://doi.org/10.1016/S0092-8674(00)81683-9
- Hidalgo M, Eckhardt S G (2001). Development of matrix metalloproteinase inhibitors in cancer therapy. J Natl Cancer Inst, 93, 178-93. https://doi.org/10.1093/jnci/93.3.178
- Ikebe T, Shinohara M, Takeuchi H, et al (1999). Gelatinolytic activity of matrix metalloproteinase in tumour tissues correlates with invasiveness of oral cancer. Clin Exp Metastasis, 17, 315-23. https://doi.org/10.1023/A:1006642428826
- Illman S A, Lehti K, Keski-Oja J, Lohi J (2006). Epilysin(MMP-28) induces TGF B mediated epithelial to mesenchymal transition in lung carcinoma cells. J Cell Sci, 119, 3856-65. https://doi.org/10.1242/jcs.03157
- Jemal A, Tiwari RC, Murray T, et al (2004). Cancer statistics. CA Cancer J Clin, 54, 9-29.
- Karin M, Chang L (2001). AP-1 glucocorticoid receptor crosstalk taken to a higher level. J. Endocrinol, 169,447-51. https://doi.org/10.1677/joe.0.1690447
- Kim J, Yu W, Kovalski K, Ossowski L (1998). Requirment of specific proteases in cancer cell intravasation as revealed by a novel semiquantitative PCR based assay. Cell, 94, 353-62. https://doi.org/10.1016/S0092-8674(00)81478-6
- Koolwijk P, Sidenius N, Peters E, et al (2001). Proteolysis of the urokinase-type plasminogen activator receptor by metalloproteinase-12:implication for angiogenesis in fibrin matrices. Blood, 97, 3123-31. https://doi.org/10.1182/blood.V97.10.3123
- Kousidou O C, Mitropoulou T N, Roussidis A E, et al (2006). Genistein suppresses the invasive potential of human breast cancer cells through transcriptional regulation of metalloproteinases and their tissue inhibitors. Int J Oncol, 26, 1101-9.
- Kuga H, Morisaki T, Nakamura K, et al (2003). Interferon gama suppreses transforming growth factor beta induced invasion of gastric carcinoma cells through cross talk of Smad pathway in a three -dimensional culture model. Oncogene, 22, 7838-47. https://doi.org/10.1038/sj.onc.1207046
- Kumar V, Abbas A K, Fausto N (2004). Robbins and Cotran Pathologic basis of disease. 7thed; Philadelphia; Saunders; Elsevier Inc, 202-3.
- Leco K J, Khokha R, Pavloff N, Hawkes S P, Edwards D R (1994). Tissue inhibitors of metalloproteinases-3 (TIMP-3) is an extracellular matrix associated protein with a distinctive pattern of expression in mouse cells and tissues. J Biol Chem, 269, 9532-60.
- Lijnen H R (2001). Plasmin and matrix metalloproteinases in vascular remodelling. Thomb Haemost, 86, 324-33.
- Lockhart A C, Braun R D, Yu D, et al (2003). Reduction of wound angiogenesis in patients treated with BMS-275291, a broad spectrum matrix metalloproteinase inhibitor. Clin Cancer Res, 9, 586-93.
- Lokeshwar B L, Escatel E, Zhu B (2001). Cytotoxic activity and inhibition of tumour cell invasion by derivatives of a chemically modified tetracycline CMT-3(COL-3). Curr Med Chem, 8, 271-9. https://doi.org/10.2174/0929867013373516
- Lopez-otin C, Overall C M (2002). Protease degradomics: a new challenge for proteomics. Nat Rev Mol Cell Biol, 3, 509-19. https://doi.org/10.1038/nrm858
- Manes S, Mira E, Barbacid MM, Cipres A, et al (1997). Identification of insulin -like growth binding protein-1 as a potential physiological substrate for human stromelysins-3. J Biol Chem, 272, 25706-12. https://doi.org/10.1074/jbc.272.41.25706
- Maretzky T, Reiss K, Ludwig A, et al (2005). ADAM-10 mediates E-cadherin shedding and regulates epithelial cell-cell adhesion , migration and beta- catenin translocation. Proc Natl Acad Sci USA, 102, 9182-87. https://doi.org/10.1073/pnas.0500918102
- McCawley L J, Matrisian L M (2001). Matrix metalloproteinases: they are not just for matrix anymore! Curr. Opin. Cell Biol,13, 534-40. https://doi.org/10.1016/S0955-0674(00)00248-9
- Mitsiades N, Yu W H, Poulaki V, Tsokos M, Stamenkovic I (2001). Matrix metalloproteinase-7 mediated cleavage of Fas ligand protects tumour cells from chemotherapeutic drug toxicity. Cancer Res, 61, 577-81.
- Murphy G, Reynolds J J (1993). Extracellular matrix degradation: in connective tissue and its heritable disorders. Royce P M,Steinman B, editors. New York, Wiley-Liss 287-316.
- Murray G I, Duncan M E, O'Neil P, Melvin W T, Fothergill J E (1996). Matrix metalloproteinase-1 is associated with poor prognosis in colorectal cancer. Nat Med, 2, 461-2. https://doi.org/10.1038/nm0496-461
- Nagase H, Visse R, Murphy G (2006). Structure and function of matrix metalloproteinases and TIMPs. Cardiovascular Res, 69, 562-73. https://doi.org/10.1016/j.cardiores.2005.12.002
- Nelson A R, Fingleton B, Rotherberg M L, et al (2000). Matrix metalloproteinases: biologic activity and clinical implications. J Clin Oncol, 18, 1135-49.
- Noe V et al (2001). Release of an invasion promoter E-cadherin fragment by matrilysins and stromilysin-1. J Cell Sci, 114, 111-8.
- Overall C M (2002). Molecular determinants of metalloproteinase substrate specificity: matrix metalloproteinases and new 'intracellular substrate binding domains, modules and exosites. Mol Biotechnol Chem, 383, 1059-66.
- Overall C M, Lopez-otin C(2002). Strategies for MMP inhibition in cancer: innovations for the post-trial era. Nat Rev Cancer, 2, 657-72. https://doi.org/10.1038/nrc884
- Pendas A M, Balbin M, Llano E, Jimenez M G, Lopez-otin C (1997). Structural analysis and promoter characterization of the human collagenases-3 gene (MMP-13). Genomics, 40, 222-33. https://doi.org/10.1006/geno.1996.4554
- Peschon JJ, Slack JL, Reddy P, et al (1998). An essential role for ectodomain shedding in mammalian development. Science, 282, 1281-84. https://doi.org/10.1126/science.282.5392.1281
- Rundhaung J E. Matrix Metalloproteinases, angiogenesis and cancer (2003). Clin Cancer Res, 9, 551-54.
- Sapadin A N, Fleischmajer R (2006). Tetracyclines: nonantibiotic properties and their clinical implications. J Am Acad Dermatol, 54, 258-65. https://doi.org/10.1016/j.jaad.2005.10.004
- Sekhon BS (2010). Matrix metalloproteinases-an overview. Res Reports Biol, 1, 20.
- Sheu B C, Hsu S M, Ho H N, et al (2001). A novel role of metalloproteinase in cancer-mediated immunosuppression. Cancer Res, 61, 237-42.
- Stamenkovic I (2003). Extracellular remodelling: the role of metalloendopeptidases. J Pathol, 200, 448-64. https://doi.org/10.1002/path.1400
- Sternlicht M D, Werb Z (2001). How matrix metalloproteinase regulate cell behaviour. Annu Rev Cell Dev Biol, 17, 463-516. https://doi.org/10.1146/annurev.cellbio.17.1.463
- Stetler-Stevenson W G (1999). Matrix metalloproteinases in angiogenesis: a moving target for therapeutic intervention. J Clin Investig, 103, 1237-41. https://doi.org/10.1172/JCI6870
- Stetler-stevenson W G, Krutzsch H C, Liotta L A (1989). Tissue inhibitor of metalloproteinase (TIMP-2). J BiolChem, 264, 17374-8.
- Steward W P, Thomas A L (2000). Marimastat: the clinical development of a matrix metalloproteinase inhibitor. Expert Opin Invesig Drugs, 9, 2913-22. https://doi.org/10.1517/13543784.9.12.2913
- Strickland D K, Ashcom J D, Williams S, et al (1990). Sequence identity between the alpha 2- macroglobulin receptor and low density lipoprotein receptor related protein suggests that this molecule is a multifunctional receptor. J BiolChem, 265, 17401-4.
- Takeichi M (1991). Cadherin cell adhesion receptors as a morphogenetic regulator. Science, 251, 1451-55. https://doi.org/10.1126/science.2006419
- Thiery J P (2002). Epithelial mesenchymal transitions in tumour progression. Nat Rev Cancer, 2, 442-54. https://doi.org/10.1038/nrc822
- Thomas GT, Lewis MP, Speight PM (1999). Matrixmetalloproteinases and oral cancer. Oral Oncol, 227, 33.
- Uria J A, Ferrando A A, Velasco G, Freije J M P, Lopez-otin C (1994). Structure and expression in breast tumours of human TIMP-3, a new member of the metalloproteinase family. Cancer Res, 54, 2091-94.
- Velasco G, Pendas A M, Fueyo A ,et al (1999). Cloning and characterization of human MMP-23,a new matrix metalloproteinase predominantly expressed in reproductive tissues and lacking conserved domains in other family members. J BiolChem, 274, 4570-76.
- Vihinen P, Kahari V M (2002). Matrix metalloproteinases in cancer: prognostic markers and therapeutic targets. Int J cancer, 99, 157-66. https://doi.org/10.1002/ijc.10329
- Visse R, Nagase H (2003). Matrix metalloproteinases and tissue inhibitors of metalloproteinases: Structure, Function and Biochemistry. Circulation Research, 92,827-39. https://doi.org/10.1161/01.RES.0000070112.80711.3D
- Waldhauer I, Goehlsdorf D, Gieseke F, et al (2008). Tumour associated MICA is shed by ADAM proteases. Cancer Res, 68, 6368-76. https://doi.org/10.1158/0008-5472.CAN-07-6768
- Westermarck J, Kahari V M (1999). Regulation of matrix metalloproteinase expression in tumour invasion. FASEB J, 13, 781-92.
- Williamson R A, Marston F A, Angal S, et al (1990). Disulphide bond assignment in human tissue inhibitor of metalloproteinases(TIMP). Biochem J, 268, 267-74.
- Wojtowicz-praga S, Low J, Marshall J, et al (1996). Phase I trial of a novel matrix metalloproteinase inhibitor batimastat(BB-94) in patients with advanced cancer. Invest New Drugs, 14, 193-202.
- Zhang Y Zhang YY, Chen B, Ding YQ (2012). Metastasisassociated Factors Facilitating the Progression of Colorectal Cancer. APJCP, 13, 2436-47.
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