Overexpression of MMP-9 Contributes to Invasiveness of Prostate Cancer Cell Line LNCaP

REFERENCES

• Aalinkeel, R., Nair, M. P., Sufrin, G., Mahajan, S. D., Chadha, K. C., Chawda, R. P., and Schwartz S. A. (2004). Gene expression of angiogenic factors correlates with metastatic potential of prostate cancer cells. Cancer Res. 64:5311–5321.
   PubMed Web of Science ®Google Scholar
• Albini, A. (1998). Tumor and endothelial cell invasion of basement membranes. The matrigel chemoinvasion assay as a tool for dissecting molecular mechanisms. Pathol. Oncol. Res. 4: 230–241.
   PubMedGoogle Scholar
• Axelrod, J. H., Reich, R., and Miskin, R. (1989). Expression of human recombinant plasminogen activators enhances invasion and experimental metastasis of H-ras-transformed NIH 3T3 cells. Mol. Cell. Biol. 9:2133–2141.
   PubMedGoogle Scholar
• Bergers, G., Brekken, R., McMahon, G., Vu, T. H., Itoh, T., Tamaki, K., Tanzawa, K., Thorpe, P., Itohara, S., Werb, Z., and Hanahan, D. (2000). Matrix metalloproteinase-9 triggers the angiogenic switch during carcinogenesis. Nat. Cell. Biol. 2:737–744.
   PubMed Web of Science ®Google Scholar
• Bonfil, R. D., Reddel, R. R., Ura, H., Reich, R., Fridman, R., Harris, C. C., and Klein-Szanto, J. P. (1989). Invasive and metastatic potential of a v-Ha-ras-transformed human bronchial epithelial cell line. J. Natl. Cancer Inst. 81:587–594.
   Google Scholar
• Chiarugi, V., Ruggiero, M., and Magnelli, L. (2000). Molecular polarity in endothelial cells and tumor-induced angiogenesis. Oncol. Res. 12:1–4.
   PubMedGoogle Scholar
• Chomczynski, P., and Sacchi, N. (1987). Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:156–159.
   PubMed Web of Science ®Google Scholar
• Coussens, L. M., Fingleton B., and Matrisian L. M. (2002). Matrix metalloproteinase inhibitors and cancer: Trials and tribulations. Science 29:2387–2392.
   Google Scholar
• Coussens, L. M., Tinkle, C. L., Hanahan, D., and Werb, Z. (2000). MMP-9 supplied by bone marrow-derived cells contributes to skin carcinogenesis. Cell 103:481–490.
   PubMed Web of Science ®Google Scholar
• Coussens, L. M., and Werb, Z. (2002). Inflammation and cancer. Nature 420, 860–867.
   PubMed Web of Science ®Google Scholar
• Dahiya, R., Park, H. D., Cusick, J., Vessella, R. L., Fournier, G., and Narayan, P. (1994). Inhibition of tumorigenic potential and prostate-specific antigen expression in LNCaP human prostate cancer cell line by 13-cis-retinoic acid. Int. J. Cancer 59:126–132.
   Google Scholar
• Dano, K., Andreasen, P. A., Grondahl-Hansen, J., Kristensen, P., Nielsen, L. S., and Skriver, L. (1985). Plasminogen activators, tissue degradation, and cancer. Adv. Cancer Res. 44:139–266.
   PubMed Web of Science ®Google Scholar
• Dano, K., and Reich, E. (1978). Serine enzymes released by cultured neoplastic cells. J. Exp. Med. 147:745–757.
   PubMed Web of Science ®Google Scholar
• Dedhar, S., Saulnier, R., Nagle, R., and Overall, C. M. (1993). Specific alterations in the expression of alpha 3 beta 1 and alpha 6 beta 4 integrins in highly invasive and metastatic variants of human prostate carcinoma cells selected by in vitro invasion through reconstituted basement membrane. Clin. Exp. Metastasis 11:391–400.
   PubMed Web of Science ®Google Scholar
• Egeblad, M., and Werb, Z. (2002). New functions for the matrix metalloproteinases in cancer progression. Nat. Rev. Cancer 2:161–174.
   PubMed Web of Science ®Google Scholar
• Festuccia, C., Bologna, M., Vicentini, C., Tacconelli, A., Miano, R., Violini, S., and Mackay, A. R. (1996). Increased matrix metalloproteinase-9 secretion in short-term tissue cultures of prostatic tumor cells. Int. J. Cancer 69:386–393.
   Google Scholar
• Fingleton, B., and Matrisian, L. M. (2001). Matrix metalloproteinases as targets for therapy in Kaposi sarcoma. Curr. Opin. Oncol. 13:368–373.
   Google Scholar
• Fukumura, D., Yuan, F., Monsky, W. L., Chen, Y., and Jain, R. K. (1997). Effect of host microenvironment on the microcirculation of human colon adenocarcinoma. Am. J. Pathol. 151:679–688.
   PubMed Web of Science ®Google Scholar
• Ghosh, C., Stein, D., Weller, D., and Iversen, P. (2000). Evaluation of antisense mechanisms of action. Meth. Enzymol. 313:135–143.
   PubMed Web of Science ®Google Scholar
• Giles, R. V., Spiller, D. G., Clark, R. E., and Tidd, D. M. (1999). Antisense morpholino oligonucleotide analog induces missplicing of C-myc mRNA. Antisense Nucl. Acid Drug Dev. 9:213–220.
   PubMedGoogle Scholar
• Gleave, M., Hsieh, J. T., Gao, C. A., von Eschenbach, A. C., and Chung, L. W. (1991). Acceleration of human prostate cancer growth in vivo by factors produced by prostate and bone fibroblasts. Cancer Res. 51:3753–3761.
   PubMedGoogle Scholar
• Grondahl-Hansen, J., Lund, L. R., Ralfkiaer, E., Ottevanger, V., and Dano, K. (1988). Urokinase- and tissue-type plasminogen activators in keratinocytes during wound reepithelialization in vivo. J. Invest. Dermatol. 90:790–795.
   PubMed Web of Science ®Google Scholar
• Hoosein, N. M., Boyd, D. D., Hollas, W. J., Mazar, A., Henkin, J., and Chung, L. W. (1991). Involvement of urokinase and its receptor in the invasiveness of human prostatic carcinoma cell lines. Cancer Commun. 3:255–264.
   PubMedGoogle Scholar
• Huang, S., Van Arsdall, M., Tedjarati, S., McCarty, M., Wu, W., Langley, R., and Fidler, I. J. (2002). Contributions of stromal metalloproteinase-9 to angiogenesis and growth of human ovarian carcinoma in mice. J. Natl. Cancer Inst. 94:1134–1142.
   PubMed Web of Science ®Google Scholar
• Itoh, T., Tanioka, M., Matsuda, H., Nishimoto, H., Yoshioka, T., Suzuki, R., and Uehira, M. (1999). Experimental metastasis is suppressed in MMP-9-deficient mice. Clin. Exp. Metastasis 17:177–181.
   PubMed Web of Science ®Google Scholar
• Iversen P. L. (2001). Phosphorodiamidate morpholino oligomers: Favorable properties for sequence-specific gene inactivation. Curr. Opin. Mol. Ther. 3:235–238.
   PubMedGoogle Scholar
• Kim, J., Yu, W., Kovalski, K., and Ossowski, L. (1998). Requirement for specific proteases in cancer cell intravasation as revealed by a novel semiquantitative PCR-based assay. Cell 94:353–362.
   PubMed Web of Science ®Google Scholar
• Kondraganti, S., Mohanam, S., Chintala, S. K., Kin, Y., Jasti, S. L., Nirmala, C., Lakka, S. S., Adachi, Y., Kyritsis, A. P., Ali-Osman, F., Sawaya, R., Fuller, G. N., and Rao, J. S. (2000). Selective suppression of matrix metalloproteinase-9 in human glioblastoma cells by antisense gene transfer impairs glioblastoma cell invasion. Cancer Res. 60:6851–6855.
   PubMed Web of Science ®Google Scholar
• Lakka, S. S., Jasti, S. L., Gondi, C., Boyd, D., Chandrasekar, N., Dinh, D. H., Olivero, W. C., Gujrati, M., and Rao, J. S. (2002a). Downregulation of MMP-9 in ERK-mutated stable transfectants inhibits glioma invasion in vitro. Oncogene 21:5601–5608.
   PubMed Web of Science ®Google Scholar
• Lakka, S. S., Rajan, M., Gondi, C., Yanamandra, N., Chandrasekar, N., Jasti, S. L., Adachi, Y., Siddique, K., Gujrati, M., Olivero, W., Dinh, D. H., Kouraklis, G., Kyritsis, A. P., and Rao, J. S. (2002b). Adenovirus-mediated expression of antisense MMP-9 in glioma cells inhibits tumor growth and invasion. Oncogene 21:8011–8019.
   PubMed Web of Science ®Google Scholar
• Laniado, M. E., Lalani, E. N., Fraser, S. P., Grimes, J. A., Bhangal, G., Djamgoz, M. B., and Abel, P. D. (1997). Expression and functional analysis of voltage-activated Na+ channels in human prostate cancer cell lines and their contribution to invasion in vitro. Am. J. Pathol. 150:1213–1221.
   PubMed Web of Science ®Google Scholar
• Liotta, L. A., Steeg, P. S., and Stetler-Stevenson, W. G. (1991). Cancer metastasis and angiogenesis: an imbalance of positive and negative regulation. Cell 64:327–336.
   PubMed Web of Science ®Google Scholar
• Lokeshwar, B. L., Selzer, M. G., Block, N. L., and Gunja-Smith, Z. (1993). Secretion of matrix metalloproteinases and their inhibitors (tissue inhibitor of metalloproteinases) by human prostate in explant cultures: Reduced tissue inhibitor of metalloproteinase secretion by malignant tissues. Cancer Res. 53:4493–4498.
   PubMed Web of Science ®Google Scholar
• Nelson, A. R., Fingleton, B., Rothenberg, M. L., and Matrisian, L. M. (2000). Matrix metalloproteinases: biologic activity and clinical implications. J. Clin. Oncol. 18:1135–1149.
   PubMed Web of Science ®Google Scholar
• Ossowski, L., Biegel, D., and Reich, E. (1979). Mammary plasminogen activator: Correlation with involution, hormonal modulation and comparison between normal and neoplastic tissue. Cell 16:929–940.
   PubMedGoogle Scholar
• Ossowski, L., and Reich, E. (1983). Antibodies to plasminogen activator inhibit human tumor metastasis. Cell 35:611–619.
   PubMed Web of Science ®Google Scholar
• Paget, S. (1989). The distribution of secondary growths in cancer of the breast. Cancer Metastasis Rev. 8:98–101.
   PubMed Web of Science ®Google Scholar
• Pepper, M. S., Vassalli, J. D., Montesano, R., and Orci, L. (1987). Urokinase-type plasminogen activator is induced in migrating capillary endothelial cells. J. Cell. Biol. 105:2535–2541.
   PubMed Web of Science ®Google Scholar
• Rembrink, K., Romijn, J. C., van der Kwast, T. H., Rubben, H., and Schroder, F. H. (1997). Orthotopic implantation of human prostate cancer cell lines: A clinically relevant animal model for metastatic prostate cancer. Prostate 31:168–174.
   Google Scholar
• Rhee, J. S., and Coussens, L. M. (2002). RECKing MMP function: Implications for cancer development. Trends Cell. Biol. 12:209–211.
   PubMed Web of Science ®Google Scholar
• Sato, N., Gleave, M. E., Bruchovsky, N., Rennie, P. S., Beraldi, E., and Sullivan, L. D. (1997). A metastatic and androgen-sensitive human prostate cancer model using intraprostatic inoculation of LNCaP cells in SCID mice. Cancer Res. 57:1584–1589.
   PubMedGoogle Scholar
• Stephenson, R. A., Dinney, C. P., Gohji, K., Ordonez, N. G., Killion, J. J., and Fidler, I. J. (1992). Metastatic model for human prostate cancer using orthotopic implantation in nude mice. J. Natl. Cancer Inst. 84:951–957.
   PubMedGoogle Scholar
• Summerton J. (1999). Morpholino antisense oligomers: the case for an RNase H-independent structural type. Biochim. Biophys. Acta 1489:141–158.
   PubMed Web of Science ®Google Scholar
• Summerton J., and Weller D. (1997). Morpholino antisense oligomers: Design, preparation, and properties. Antisense Nucl. Acid Drug Dev. 7:187–195.
   PubMedGoogle Scholar
• Unkeless J., Dano K., Kellerman G. M., and Reich E. (1974). Fibrinolysis associated with oncogenic transformation. Partial purification and characterization of the cell factor, a plasminogen activator. J. Biol. Chem. 249:4295–4305.
   PubMed Web of Science ®Google Scholar
• van Kempen L. C., and Coussens L. M. (2002). MMP9 potentiates pulmonary metastasis formation. Cancer Cell 2:251–252.
   PubMed Web of Science ®Google Scholar
• van Kempen L. C., Rhee J. S., Dehne K., Lee J., Edwards D. R., and Coussens L. M. (2002). Epithelial carcinogenesis: Dynamic interplay between neoplastic cells and their microenvironment. Differentiation 70:610–623.
   Google Scholar
• Werb Z. (1997). ECM and cell surface proteolysis: Regulating cellular ecology. Cell 91:439–442.
   PubMed Web of Science ®Google Scholar
• Woessner J. F., Jr. (1991). Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB J. 5:2145–2154.
   PubMed Web of Science ®Google Scholar
• Wood M., Fudge K., Mohler J. L., Frost A. R., Garcia F., Wang M., and Stearns M. E. (1997). In situ hybridization studies of metalloproteinases 2 and 9 and TIMP-1 and TIMP-2 expression in human prostate cancer. Clin. Exp. Metastasis 15:246–258.
   PubMed Web of Science ®Google Scholar
• Xu D., McKee C. M., Cao Y., Ding Y., Kessler B. M., and Muschel R. J. (2010). Matrix metalloproteinase-9 regulates tumor cell invasion through cleavage of protease nexin-1. Cancer Res. 70:6988–6998.
   Google Scholar
• Xu D., Suenaga N., Edelmann M. J., Fridman R., Muschel R. J., and Kessler B. M. (2008). Novel MMP-9 substrates in cancer cells revealed by a label-free quantitative proteomics approach. Mol. Cell Proteomics 7:2215–2228.
   PubMed Web of Science ®Google Scholar