Membrane-type 1 matrix metalloproteinase expression is regulated by zonula occludens-1 in human breast cancer cells

Cancer Research

Volumn 65, Issue 17, 2005, Pages 7691-7698

  Polette, Myriam ^a   Gilles, Christine ^b   Nawrocki Raby, Béatrice ^a   Lohi, Jouko ^c   Hunziker, Walter ^d   Foidart, Jean Michel ^b   Birembaut, Philippe ^a  

^a HÔPITAL MAISON BLANCHE   (France)

^b UNIVERSITY OF LIÈGE   (Belgium)

^c UNIVERSITY OF HELSINKI   (Finland)

^d INSTITUTE OF MOLECULAR AND CELL BIOLOGY   (Singapore)

Author keywords

[No Author keywords available]

Indexed keywords

LUCIFERASE; MATRIX METALLOPROTEINASE 14; MESSENGER RNA; OCCLUDIN; PROTEIN; SMALL INTERFERING RNA;

ARTICLE; BREAST CANCER; CANCER CELL; CONTROLLED STUDY; ENZYME REGULATION; HUMAN; HUMAN CELL; HUMAN TISSUE; IMMUNOFLUORESCENCE; IMMUNOHISTOCHEMISTRY; NUCLEOTIDE SEQUENCE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; RNA INTERFERENCE; WESTERN BLOTTING;

BETA CATENIN; BREAST NEOPLASMS; CYTOPLASM; CYTOSKELETAL PROTEINS; DNA, COMPLEMENTARY; DOWN-REGULATION; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GENE EXPRESSION REGULATION, NEOPLASTIC; HUMANS; MATRIX METALLOPROTEINASES, MEMBRANE-ASSOCIATED; MEMBRANE PROTEINS; METALLOENDOPEPTIDASES; NEOPLASM INVASIVENESS; PHOSPHOPROTEINS; PROMOTER REGIONS (GENETICS); RNA, MESSENGER; RNA, SMALL INTERFERING; TRANS-ACTIVATION (GENETICS); TRANS-ACTIVATORS; TRANSFECTION;

EID: 24744470324     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-04-4230     Document Type: Article

References (38)

1. Conacci-Sorrell M, Zhurinsky J, Ben Ze'ev A. The cadherin-catenin adhesion system in signaling and cancer. J Clin Invest 2002;109:987-91.
2. Gonzalez-Mariscal L, Betanzos A, Nava P, Jaramillo BE. Tight junction proteins. Prog Biophys Mol Biol 2003;81:1-44.
3. Itoh M, Nagafuchi A, Yonemura S, Kitani-Yasuda T, Tsukita S, Tsukita S. The 220-kD protein colocalizing with cadherins in non-epithelial cells is identical to ZO-1, a tight junction-associated protein in epithelial cells: cDNA cloning and immunoelectron microscopy. J Cell Biol 1993;121:491-502.
4. Tsukita S, Itoh M, Nagafuchi A, Yonemura S, Tsukita S. Submembranous junctional plaque proteins include potential tumor suppressor molecules. J Cell Biol 1993;123:1049-53.
5. Hoover KB, Liao SY, Bryant PJ. Loss of the tight junction MAGUK ZO-1 in breast cancer: relationship to glandular differentiation and loss of heterozygosity. Am J Pathol 1998;153:1767-73.
6. Kaihara T, Kusaka T, Nishi M, et al. Dedifferentiation and decreased expression of adhesion molecules, E-cadherin and ZO-1, in colorectal cancer are closely related to liver metastasis. J Exp Clin Cancer Res 2003;22:117-23.
7. Martin TA, Watkins G, Mansel RE, Jiang WG. Loss of tight junction plaque molecules in breast cancer tissues is associated with a poor prognosis in patients with breast cancer. Eur J Cancer 2004;40:2717-25.
8. Kleeff J, Shi X, Bode HP, et al. Altered expression and localization of the tight junction protein ZO-1 in primary and metastatic pancreatic cancer. Pancreas 2001;23:259-65.
9. Reichert M, Muller T, Hunziker W. The PDZ domains of zonula occludens-1 induce an epithelial to mesenchymal transition of Madin-Darby canine kidney I cells. Evidence for a role of β-catenin/Tcf/Lef signaling. J Biol Chem 2000;275:9492-500.
10. Gottardi CJ, Arpin M, Fanning AS, Louvard D. The junction-associated protein, zonula occludens-1, localizes to the nucleus before the maturation and during the remodeling of cell-cell contacts. Proc Natl Acad Sci U S A 1996;93:10779-84.
11. Gonzalez-Mariscal L, Islas S, Contreras RG, et al. Molecular characterization of the tight junction protein ZO-1 in MDCK cells. Exp Cell Res 1999;248:97-109.
12. Polette M, Nawrocki-Raby B, Gilles C, Clavel C, Birembaut P. Tumour invasion and matrix metalloproteinases. Crit Rev Oncol Hematol 2004;49:179-86.
13. Seiki M, Yana I. Roles of pericellular proteolysis by membrane type-1 matrix metalloproteinase in cancer invasion and angiogenesis. Cancer Sci 2003;94:569-74.
14. Seiki M. Membrane-type 1 matrix metalloproteinase: a key enzyme for tumor invasion. Cancer Lett 2003;194:1-11.
15. Gilles C, Newgreen D, Sato H, Thompson EW. Matrix metalloproteinases and epithelia-to-mesenchymal transition: implications for carcinoma metastasis. In: Savagner P, editor. Rise and fall of epithelial phenotype. Eurekah.com and New York: Kluwer Academic/Plenum Publishers.; 2004. Chap. 22.
16. Hlubek F, Spaderna S, Jung A, Kirchner T, Brabletz T. β-Catenin activates a coordinated expression of the proinvasive factors laminin-5 γ2 chain and MT1-MMP in colorectal carcinomas. Int J Cancer 2004;108:321-6.
17. Takahashi M, Tsunoda T, Seiki M, Nakamura Y, Furukawa Y. Identification of membrane-type matrix metalloproteinase-1 as a target of the β-catenin/Tcf4 complex in human colorectal cancers. Oncogene 2002;21:5861-7.
18. Lohi J, Lehti K, Valtanen H, Parks WC, Keski-Oja J. Structural analysis and promoter characterization of the human membrane-type matrix metalloproteinase-1 (MT1-MMP) gene. Gene 2000;242:75-86.
19. Korinek V, Barker N, Morin PJ, et al. Constitutive transcriptional activation by a β-catenin-Tcf complex in APC-/- colon carcinoma. Science 1997;275:1784-7.
20. Sommers CL, Byers SW, Thompson EW, Torri JA, Gelmann EP. Differentiation state and invasiveness of human breast cancer cell lines. Breast Cancer Res Treat 1994;31:325-35.
21. Thompson EW, Paik S, Brunner N, et al. Association of increased basement membrane invasiveness with absence of estrogen receptor and expression of vimentin in human breast cancer cell lines. J Cell Physiol 1992;150:534-44.
22. Nawrocki RB, Polette M, Gilles C, et al. Quantitative cell dispersion analysis: new test to measure tumor cell aggressiveness. Int J Cancer 2001;93:644-52.
23. Staal FJ, Noort MM, Strous GJ, Clevers HC. Wnt signals are transmitted through N-terminally dephosphorylated β-catenin. EMBO Rep 2002;3:63-8.
24. Busch C, Hanssen TA, Wagener C, OBrink B. Downregulation of CEACAM1 in human prostate cancer: correlation with loss of cell polarity, increased proliferation rate, and Gleason grade 3 to 4 transition. Hum Pathol 2002;33:290-8.
25. Tobioka H, Isomura H, Kokai Y, Tokunaga Y, Yamaguchi J, Sawada N. Occludin expression decreases with the progression of human endometrial carcinoma. Hum Pathol 2004;35:159-64.
26. Hoevel T, Macek R, Mundigl O, Swisshelm K, Kubbies M. Expression and targeting of the tight junction protein CLDN1 in CLDN1-negative human breast tumor cells. J Cell Physiol 2002;191:60-8.
27. Wan H, Winton HL, Soeller C, et al. Tight junction properties of the immortalized human bronchial epithelial cell lines Calu-3 and 16HBE14o-. Eur Respir J 2000;15:1058-68.
28. Gilles C, Polette M, Coraux C, et al. Contribution of MT1-MMP and of human laminin-5 γ2 chain degradation to mammary epithelial cell migration. J Cell Sci 2001;114:2967-76.
29. Ueda J, Kajita M, Suenaga N, Fujii K, Seiki M. Sequence-specific silencing of MT1-MMP expression suppresses tumor cell migration and invasion: importance of MT1-MMP as a therapeutic target for invasive tumors. Oncogene 2003;22:8716-22.
30. Sounni NE, Devy L, Hajitou A, et al. MT1-MMP expression promotes tumor growth and angiogenesis through an up-regulation of vascular endothelial growth factor expression. FASEB J 2002;16:555-64.
31. Sato H, Takino T, Okada Y, et al. A matrix metalloproteinase expressed on the surface of invasive tumour cells [see comments]. Nature 1994;370:61-5.
32. Takahisa M, Togashi S, Suzuki T, et al. The Drosophila tamou gene, a component of the activating pathway of extramacrochaetae expression, encodes a protein homologous to mammalian cell-cell junction-associated protein ZO-1. Genes Dev 1996;10:1783-95.
33. Balda MS, Matter K. The tight junction protein ZO-1 and an interacting transcription factor regulate ErbB-2 expression. EMBO J 2000;19:2024-33.
34. Ryeom SW, Paul D, Goodenough DA. Truncation mutants of the tight junction protein ZO-1 disrupt corneal epithelial cell morphology. Mol Biol Cell 2000;11:1687-96.
35. Gottardi CJ, Gumbiner BM. Distinct molecular forms of β-catenin are targeted to adhesive or transcriptional complexes. J Cell Biol 2004;167:339-49.
36. Imamura Y, Itoh M, Maeno Y, Tsukita S, Nagafuchi A. Functional domains of α-catenin required for the strong state of cadherin-based cell adhesion. J Cell Biol 1999;144:1311-22.
37. Itoh M, Nagafuchi A, Moroi S, Tsukita S. Involvement of ZO-1 in cadherin-based cell adhesion through its direct binding to α catenin and actin filaments. J Cell Biol 1997;138:181-92.
38. Kausalya PJ, Phua DC, Hunziker W. Association of ARVCF with ZO-1 and ZO-2: binding to PDZ-domain proteins and cell-cell adhesion regulate plasma membrane and nuclear localization of ARVCF. Mol Biol Cell 2004;15:5503-15.