The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Selective Inhibition of Matrix Metalloproteinase-14 Blocks Tumor Growth, Invasion, and Angiogenesis
Open accessAbstract
Inhibition of specific matrix metalloproteinases (MMP) is an attractive noncytotoxic approach to cancer therapy. MMP-14, a membrane-bound zinc endopeptidase, has been proposed to play a central role in tumor growth, invasion, and neovascularization. Besides cleaving matrix proteins, MMP-14 activates proMMP-2 leading to an amplification of pericellular proteolytic activity. To examine the contribution of MMP-14 to tumor growth and angiogenesis, we used DX-2400, a highly selective fully human MMP-14 inhibitory antibody discovered using phage display technology. DX-2400 blocked proMMP-2 processing on tumor and endothelial cells, inhibited angiogenesis, and slowed tumor progression and formation of metastatic lesions. The combination of potency, selectivity, and robust in vivo activity shows the potential of a selective MMP-14 inhibitor for the treatment of solid tumors. [Cancer Res 2009;69(4):1517–26]
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Cites
New functions for the matrix metalloproteinases in cancer progression
Egeblad, M., & Werb, Z. (2002) · Nature Reviews Cancer · doi:10.1038/nrc745 · Cited by 6,108
Mace, K. A., Hansen, S. L., Myers, C., Young, D. M., & Boudreau, N. (2005) · Journal of Cell Science · doi:10.1242/jcs.02399 · Cited by 125
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Jain, R. K. (2014) · Cancer Cell · doi:10.1016/j.ccell.2014.10.006 · Cited by 1,589
The extracellular matrix in tumor progression and metastasis
Eble, J. A., & Niland, S. (2019) · Clinical & Experimental Metastasis · doi:10.1007/s10585-019-09966-1 · Cited by 613
Collagen as a double-edged sword in tumor progression
Fang, M., Yuan, J., Peng, C., & Li, Y. (2014) · Tumor Biology · doi:10.1007/s13277-013-1511-7 · Cited by 580
Membrane-type matrix metalloproteinases: Their functions and regulations
Itoh, Y. (2015) · Matrix Biology · doi:10.1016/j.matbio.2015.03.004 · Cited by 401
Ciliary Hedgehog Signaling Restricts Injury-Induced Adipogenesis
Kopinke, D., Roberson, E. C., & Reiter, J. F. (2017) · Cell · doi:10.1016/j.cell.2017.06.035 · Cited by 260
Inhibition of matrix metalloproteinase 14 (MMP-14)-mediated cancer cell migration.
Zarrabi, K., Dufour, A., Li, J., Kuscu, C., Pulkoski-Gross, A., Zhi, J., Hu, Y., Sampson, N. S., Zucker, S., & Cao, J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.256644 · Cited by 188
Zhu, L., Tang, Y., Li, X.-Y., Keller, E. T., Yang, J., Cho, J.-S., Feinberg, T. Y., & Weiss, S. J. (2020) · Science Translational Medicine · doi:10.1126/scitranslmed.aaw6143 · Cited by 178
“Recombinant humanized mAbs have been generated that effectively inhibit either human MMP9 or MMP14 (39, 40, 81).”
BackgroundNew strategies for targeting matrix metalloproteinases.
Fields, G. B. (2015) · Matrix Biology · doi:10.1016/j.matbio.2015.01.002 · Cited by 98
Matrix Metalloproteinases as New Targets in Alzheimer’s Disease: Opportunities and Challenges
Zipfel, P., Rochais, C., Baranger, K., Rivera, S., & Dallemagne, P. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00352 · Cited by 94
Ling, B., Watt, K., Banerjee, S., Newsted, D., Truesdell, P., Adams, J., Sidhu, S. S., & Craig, A. W. B. (2017) · Oncotarget · doi:10.18632/oncotarget.17702 · Cited by 92
Extracellular matrix determinants and the regulation of cancer cell invasion stratagems
WILLIS, A. L., SABEH, F., LI, X. ‐., & WEISS, S. J. (2013) · Journal of Microscopy · doi:10.1111/jmi.12064 · Cited by 85
Feinberg, T. Y., Zheng, H., Liu, R., Wicha, M. S., Yu, S. M., & Weiss, S. J. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.08.025 · Cited by 78
New approaches to selectively target cancer-associated matrix metalloproteinase activity
Tauro, M., McGuire, J., & Lynch, C. C. (2014) · Cancer and Metastasis Reviews · doi:10.1007/s10555-014-9530-4 · Cited by 70
Jung, J.-S., Jung, K., Kim, D.-H., & Kim, H.-S. (2012) · Pharmacological Research · doi:10.1016/j.phrs.2012.02.013 · Cited by 65
Shiryaev, S. A., Remacle, A. G., Golubkov, V. S., Ingvarsen, S., Porse, A., Behrendt, N., Cieplak, P., & Strongin, A. Y. (2013) · Oncogenesis · doi:10.1038/oncsis.2013.44 · Cited by 42
Srivastava, K., Pickard, A., McDade, S., & McCance, D. J. (2017) · Oncotarget · doi:10.18632/oncotarget.3892 · Cited by 28
Inhibition of MMP 14 potentiates the therapeutic effect of temozolomide and radiation in gliomas
Ulasov, I., Thaci, B., Sarvaiya, P., Yi, R., Guo, D., Auffinger, B., Pytel, P., Zhang, L., Kim, C. K., Borovjagin, A., et al. (2013) · Cancer Medicine · doi:10.1002/cam4.104 · Cited by 28
Matrix metalloproteinase-14 expression and its prognostic value in cervical carcinoma
Wang, H., Zhang, X., Huang, L., Li, J., Qu, S., & Pan, F. (2014) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-014-9974-8 · Cited by 16
Self-citationBasal localization of MT1-MMP is essential for epithelial cell morphogenesis in 3D collagen matrix.
Weaver, S. A., Wolters, B., Ito, N., Woskowicz, A. M., Kaneko, K., Shitomi, Y., Seiki, M., & Itoh, Y. (2014) · Journal of Cell Science · doi:10.1242/jcs.135236 · Cited by 15
Ulasov, I., Borovjagin, A. V., Kaverina, N., Schroeder, B., Shah, N., Lin, B., Baryshnikov, A., & Cobbs, C. (2015) · Cancer Letters · doi:10.1016/j.canlet.2015.06.002 · Cited by 14
Metadata
- Authors
- Devy, L., Huang, L., Naa, L., Yanamandra, N., Pieters, H., Frans, N., Chang, E., Tao, Q., Vanhove, M., Lejeune, A., van Gool, R., Sexton, D. J., Kuang, G., Rank, D., Hogan, S., Pazmany, C., Ma, Y. L., Schoonbroodt, S., Nixon, A. E., Ladner, R. C., Hoet, R., Henderikx, P., TenHoor, C., Rabbani, S. A., Valentino, M. L., Wood, C. R., & Dransfield, D. T.
- Venue
- Cancer Research
- Published
- 2009-02-12
- Volume
- 69
- Issue
- 4
- Pages
- 1517-1526
- ISSN
- 0008-5472 (ISSN-L)
- 1538-7445
- OpenAlex
- W2155879201
- Cited by
- 355
- References
- 2
- FWCI
- 8.06
- Type
- journal article
- Language
- en
- Open access
- bronze
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