Molecular mechanisms of glioma invasiveness: the role of proteases

New Perspectives in Cell Adhesion: RGD and Integrins

Ruoslahti, E. I., & Pierschbacher, M. D. (1987) · Science · doi:10.1126/science.2821619 · Cited by 4,893 · see citing works

How Matrix Metalloproteinases Regulate Cell Behavior

Sternlicht, M. D., & Werb, Z. (2001) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.17.1.463 · Cited by 3,959 · see citing works

Matrix metalloproteinase-9 triggers the angiogenic switch during carcinogenesis

Bergers, G., Brekken, R., McMahon, G., Vu, T. H., Itoh, T., Tamaki, K., Tanzawa, K., Thorpe, P., Itohara, S., Werb, Z., et al. (2000) · Nature Cell Biology · doi:10.1038/35036374 · Cited by 2,797 · see citing works

Matrix Metalloproteinase Inhibitors and Cancer—Trials and Tribulations

Coussens, L. M., Fingleton, B., & Matrisian, L. M. (2002) · Science · doi:10.1126/science.1067100 · Cited by 2,761 · see citing works

Plasminogen Activators, Tissue Degradation, and Cancer

Danø, K., Andreasen, P. A., Grøndahl-Hansen, J., Kristensen, P., Nielsen, L. S., & Skriver, L. (1985) · Advances in cancer research · doi:10.1016/s0065-230x(08)60028-7 · Cited by 2,535 · see citing works

Tissue inhibitors of metalloproteinases: structure, regulation and biological functions.

Gomez, D. E., Alonso, D. F., Yoshiji, H., & Thorgeirsson, U. P. (1997) · PubMed · Cited by 1,508 · see citing works

Regulation of matrix metalloproteinase expression in tumor invasion

Westermarck, J. K., & Kähäri, V. (1999) · The FASEB Journal · doi:10.1096/fasebj.13.8.781 · Cited by 1,494 · see citing works

MMP-9 Supplied by Bone Marrow–Derived Cells Contributes to Skin Carcinogenesis

Coussens, L. M., Tinkle, C. L., Hanahan, D., & Werb, Z. (2000) · Cell · doi:10.1016/s0092-8674(00)00139-2 · Cited by 1,306 · see citing works

Matrix metalloproteinases: they're not just for matrix anymore!

McCawley, L. J., & Matrisian, L. M. (2001) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00248-9 · Cited by 1,274 · see citing works

uPAR: a versatile signalling orchestrator

Blasi, F., & Carmeliet, P. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm977 · Cited by 1,224 · see citing works

Molecular architecture of basement membranes

Yurchenco, P. D., & Schittny, J. C. (1990) · The FASEB Journal · doi:10.1096/fasebj.4.6.2180767 · Cited by 949 · see citing works

Reduced angiogenesis and tumor progression in gelatinase A-deficient mice.

Itoh, T., Tanioka, M., Yoshida, H., Yoshioka, T., Nishimoto, H., & Itohara, S. (1998) · PubMed · Cited by 875 · see citing works

The Role of Extracellular Matrix in Development

Carbonetto, S. (1985) · Trends in Neurosciences · doi:10.1016/0166-2236(85)90201-2 · Cited by 864 · see citing works

A cellular binding site for the Mr 55,000 form of the human plasminogen activator, urokinase.

Vassalli, J. D., Baccino, D., & Belin, D. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.100.1.86 · Cited by 711 · see citing works

Intestinal tumorigenesis is suppressed in mice lacking the metalloproteinase matrilysin

Wilson, C. L., Heppner, K. J., Labosky, P. A., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.4.1402 · Cited by 612 · see citing works

Extracellular proteolytic cleavage by urokinase is required for activation of hepatocyte growth factor/scatter factor.

Naldini, L., Tamagnone, L., Vigna, E., Sachs, M., Hartmann, G. R., Birchmeier, W., Daikuhara, Y., Tsubouchi, H., Blasi, F., & Comoglio, P. M. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05588.x · Cited by 566 · see citing works

Molecular Determinants of Metalloproteinase Substrate Specificity: Matrix Metalloproteinase Substrate Binding Domains, Modules, and Exosites

Overall, C. M. (2002) · Molecular Biotechnology · doi:10.1385/mb:22:1:051 · Cited by 506 · see citing works

Topographic anatomy and CT correlations in the untreated glioblastoma multiforme

Burger, P. C., Heinz, E. R., SHIBATA, T., et al. (1988) · Journal of neurosurgery · doi:10.3171/jns.1988.68.5.0698 · Cited by 460 · see citing works

Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors.

Turk, B., Turk, V., & Türk, V. (1997) · PubMed · Cited by 440 · see citing works

Gelatinase-A (MMP-2), gelatinase-B (MMP-9) and membrane type matrix metalloproteinase-1 (MT1-MMP) are involved in different aspects of the pathophysiology of malignant gliomas

Forsyth, P. A., Wong, H., Laing, T. D., Rewcastle, N. B., Morris, D. G., Muzik, H., Leco, K. J., Johnston, R. N., Brasher, P. M. A., Sutherland, G. R., et al. (1999) · British Journal of Cancer · doi:10.1038/sj.bjc.6690291 · Cited by 436 · see citing works

Glioblastoma expression of vitronectin and the alpha v beta 3 integrin. Adhesion mechanism for transformed glial cells.

Gladson, C. L., & Cheresh, D. A. (1991) · Journal of Clinical Investigation · doi:10.1172/jci115516 · Cited by 420 · see citing works

Further studies on the activation of procollagenase, the latent precursor of bone collagenase. Effects of lysosomal cathepsin B, plasmin and kallikrein, and spontaneous activation

Eeckhout, Y., & Vaes, G. (1977) · Biochemical Journal · doi:10.1042/bj1660021 · Cited by 389 · see citing works

TIMP-2 Is Required for Efficient Activation of proMMP-2 in Vivo

Wang, Z., Jüttermann, R., & Soloway, P. D. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001270200 · Cited by 388 · see citing works

Urokinase receptor and integrin partnership: coordination of signaling for cell adhesion, migration and growth

Ossowski, L., & Aguirre‐Ghiso, J. A. (2000) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00140-x · Cited by 380 · see citing works

The fibrinolytic receptor for urokinase activates the G protein-coupled chemotactic receptor FPRL1/LXA4R

Resnati, M., Pallavicini, I., Wang, J. M., Oppenheim, J. J., Serhan, C. N., Romano, M., & Blasi, F. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.022652999 · Cited by 359 · see citing works

The Role of extracellular matrix in development

Trelstad, R. L. (1984) · Medical Entomology and Zoology · Cited by 350 · see citing works

Experimental metastasis is suppressed in MMP-9-deficient mice

Itoh, T., Tanioka, M., Matsuda, H., Nishimoto, H., Yoshioka, T., Suzuki, R., & Uehira, M. (1999) · Clinical & Experimental Metastasis · doi:10.1023/a:1006603723759 · Cited by 308 · see citing works

The extracellular matrix of the central and peripheral nervous systems: structure and function

Rutka, J. T., Apodaca, G., Stern, R., & Rosenblum, M. L. (1988) · Journal of neurosurgery · doi:10.3171/jns.1988.69.2.0155 · Cited by 307 · see citing works

In Vivo Evidence That the Stromelysin-3 Metalloproteinase Contributes in a Paracrine Manner to Epithelial Cell Malignancy

Masson, R., Lefèbvre, O., Noël, A., Fahime, E. E., Chenard, M., Wendling, C., Kebers, F., LeMeur, M., Dierich, A., Foidart, J., et al. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.140.6.1535 · Cited by 289 · see citing works

Functional overlap between two classes of matrix‐degrading proteases in wound healing

Lund, L. R., Rømer, J., Bugge, T. H., Nielsen, B. S., Frandsen, T. L., Degen, J. L., Stephens, R. W., & Danø, K. (1999) · The EMBO Journal · doi:10.1093/emboj/18.17.4645 · Cited by 270 · see citing works

Disruption of matrix metalloproteinase 2 binding to integrin alpha vbeta 3 by an organic molecule inhibits angiogenesis and tumor growth in vivo

Silletti, S. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.011343298 · Cited by 262 · see citing works

Elevated levels of M(r) 92,000 type IV collagenase in human brain tumors.

Rao, J. S., Steck, P. A., Mohanam, S., et al. (1993) · PubMed · Cited by 258 · see citing works

Multiple integrins mediate cell attachment to cytotactin/tenascin.

Prieto, A. L., Edelman, G. M., & Crossin, K. L. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.21.10154 · Cited by 245 · see citing works

Expression of collagenase-3 (MMP-13) and collagenase-1 (MMP-1) by transformed keratinocytes is dependent on the activity of p38 mitogen-activated protein kinase

Johansson, N., Ala‐aho, R., Uitto, V., Grenman, R. A., Fusenig, N. E., López-Otı́n, C., & Kähäri, V. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.2.227 · Cited by 243 · see citing works

Increased gelatinase A (MMP-2) and cathepsin B activity in invasive tumor regions of human colon cancer samples.

Emmert‐Buck, M. R., Roth, M. J., Zhuang, Z., Campo, E., Rozhin, J., Sloane, B. F., Liotta, L. A., & Stetler‐Stevenson, W. G. (1994) · PubMed Central · Cited by 238 · see citing works

Gelatinase-A (MMP-2), gelatinase-B (MMP-9) and membrane type matrix metalloproteinase-1 (MT1-MMP) are involved in different aspects of the pathophysiology of malignant gliomas

Forsyth, P. A., Wong, H., Laing, T. D., et al. (1999) · British Journal of Cancer · doi:10.1038/sj.bjc.6990291 · Cited by 225 · see citing works

Cathepsin B expression and localization in glioma progression and invasion.

Rempel, S. A., Rosenblum, M. L., Mikkelsen, T., Yan, P., Ellis, K. D., Golembieski, W., Sameni, M., Rozhin, J., Ziegler, G., & Sloane, B. F. (1994) · PubMed · Cited by 222 · see citing works

Lysosomal Cysteine Proteinases

Kirschke, H., Langner, J., Riemann, S., et al. (1980) · Novartis Foundation symposium · doi:10.1002/9780470720585.ch2 · Cited by 206 · see citing works

Expression and localization of 72 kDa type IV collagenase (MMP-2) in human malignant gliomas in vivo

Sawaya, R. A., Yamamoto, M., Gokaslan, Z. L., Wang, S. W., Mohanam, S., Fuller, G. N., McCutcheon, I. E., Stetler‐Stevenson, W. G., Nicolson, G. L., & Rao, J. S. (1996) · Clinical & Experimental Metastasis · doi:10.1007/bf00157684 · Cited by 195 · see citing works

Direct Binding of Occupied Urokinase Receptor (uPAR) to LDL Receptor-related Protein Is Required for Endocytosis of uPAR and Regulation of Cell Surface Urokinase Activity

Czekay, R., KUEMMEL, T. A., Orlando, R. A., & Farquhar, M. G. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.5.1467 · Cited by 194 · see citing works

Phosphatidylinositol 3-kinase activity in epidermal growth factor-stimulated matrix metalloproteinase-9 production and cell surface association.

Ellerbroek, S. M., Halbleib, J. M., Benavidez, M., Warmka, J. K., Wattenberg, E. V., Stack, M. S., & Hudson, L. G. (2001) · PubMed · Cited by 193 · see citing works

New Treatment Strategies for Malignant Gliomas

Avgeropoulos, N. G., & Batchelor, T. T. (1999) · The Oncologist · doi:10.1634/theoncologist.4-3-209 · Cited by 182 · see citing works

Active matrix metalloproteinase 9 expression is associated with primary glioblastoma subtype.

Choe, G., Park, J. K., Jouben-Steele, L., Kremen, T. J., Liau, L. M., Vinters, H. V., Cloughesy, T. F., & Mischel, P. S. (2002) · PubMed · Cited by 174 · see citing works

Stimulation of angiogenesis through cathepsin B inactivation of the tissue inhibitors of matrix metalloproteinases

Kostoulas, G., Lang, A., Nagase, H., & Baici, A. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00897-2 · Cited by 170 · see citing works

Inhibition of in vitro ovarian cancer cell invasion by modulation of urokinase-type plasminogen activator and cathepsin B.

Kobayashi, H., Ohi, H., Sugimura, M., et al. (1992) · PubMed · Cited by 167 · see citing works

Collagenase: a key enzyme in collagen turnover

Shingleton, W. D., Cawston, T. E., Hodges, D. J., & Brick, P. (1996) · Biochemistry and Cell Biology · doi:10.1139/o96-083 · Cited by 166 · see citing works

Selective suppression of matrix metalloproteinase-9 in human glioblastoma cells by antisense gene transfer impairs glioblastoma cell invasion.

Kondraganti, S. R., Mohanam, S., Chintala, S. K., et al. (2000) · PubMed · Cited by 163 · see citing works

Modulation of in vitro invasion of human glioblastoma cells by urokinase-type plasminogen activator receptor antibody.

Mohanam, S., Sawaya, R. A., McCutcheon, I. E., Ali‐Osman, F., Boyd, D. D., & Rao, J. (1993) · PubMed · Cited by 156 · see citing works

PTEN suppresses hyaluronic acid induced matrix metalloproteinase-9 expression in U87MG glioblastoma cells through focal adhesion kinase dephosphorylation

Park, M., Kim, M., Park, I., Kang, H., Yoo, H., Park, S. H., Rhee, C. H., Hong, S., & Lee, S. (2002) · European Journal of Cancer · doi:10.1016/s0959-8049(02)80906-6 · Cited by 155 · see citing works

Expression and localization of urokinase-type plasminogen activator in human astrocytomas in vivo.

Yamamoto, M., Sawaya, R. A., Mohanam, S., Bindal, A. K., Bruner, J. M., Oka, K., Rao, V. H., Tomonaga, M., Nicolson, G. L., & Rao, J. S. (1994) · PubMed · Cited by 154 · see citing works

Expression and localization of urokinase-type plasminogen activator receptor in human gliomas.

Yamamoto, M., Sawaya, R. A., Mohanam, S., Rao, V. H., Bruner, J. M., Nicolson, G. L., & Rao, J. S. (1994) · PubMed · Cited by 149 · see citing works

Complex Carbohydrates of Nervous Tissue

Margolis, R. U., & Margolis, R. K. (1979) · Springer eBooks · doi:10.1007/978-1-4613-2925-1 · Cited by 145 · see citing works

Differential regulation of interstitial collagenase (MMP-1) gene expression by ETS transcription factors

Westermarck, J. K., Seth, A. K., & Kähäri, V. (1997) · Oncogene · doi:10.1038/sj.onc.1201111 · Cited by 145 · see citing works

Proteinases 1: lysosomal cysteine proteinases.

Kirschke, H., Barrett, A. J., & Rawlings, N. D. (1995) · PubMed · Cited by 145 · see citing works

Marked inhibition of tumor growth in a malignant glioma tumor model by a novel synthetic matrix metalloproteinase inhibitor AG3340.

Price, A., Shi, Q., Morris, D., et al. (1999) · PubMed · Cited by 137 · see citing works

An inhibitor of c-jun aminoterminal kinase (SP600125) represses c-Jun activation, DNA-binding and PMA-inducible 92-kDa type IV collagenase expression

Shin, M., Yan, C., & Boyd, D. D. (2002) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(02)00195-7 · Cited by 137 · see citing works

Interrelationship between Schwann cell function and extracellular matrix production

Bunge, R. P., & Bunge, M. B. (1983) · Trends in Neurosciences · doi:10.1016/0166-2236(83)90235-7 · Cited by 127 · see citing works

Immunocytochemical localization of a chondroitin sulfate proteoglycan in nervous tissue. II. Studies in developing brain.

Aquino, D. A., Margolis, R. U., & Margolis, R. K. (1984) · The Journal of Cell Biology · doi:10.1083/jcb.99.3.1130 · Cited by 126 · see citing works

Roles of Extracellular Signal‐regulated Kinase 1/2 and p38 Mitogen‐activated Protein Kinase in the Signal Transduction of Basic Fibroblast Growth Factor in Endothelial Cells during Angiogenesis

Tanaka, K., Abé, M., & Sato, Y. (1999) · Japanese Journal of Cancer Research · doi:10.1111/j.1349-7006.1999.tb00796.x · Cited by 125 · see citing works

Immunolocalization of cathepsin B in human glioma: implications for tumor invasion and angiogenesis

Mikkelsen, T., Yan, P., Ho, K., et al. (1995) · Journal of neurosurgery · doi:10.3171/jns.1995.83.2.0285 · Cited by 125 · see citing works

Cathepsin B immunohistochemical staining in tumor and endothelial cells is a new prognostic factor for survival in patients with brain tumors.

Strojnik, T., Kos, J., Židanik, B., et al. (1999) · PubMed · Cited by 122 · see citing works

The role of extracellular matrix in human astrocytoma migration and proliferation studied in a microliter scale assay

Berens, M. E., Rief, M. D., Loo, M. A., & Giese, A. (1994) · Clinical & Experimental Metastasis · doi:10.1007/bf01755884 · Cited by 118 · see citing works

Overexpression and localization of cathepsin B during the progression of human gliomas

Sivaparvathi, M., Sawaya, R. A., Wang, S. W., et al. (1995) · Clinical & Experimental Metastasis · doi:10.1007/bf00144018 · Cited by 115 · see citing works

The p16INK4a tumour suppressor protein inhibits αvβ3 integrin‐mediated cell spreading on vitronectin by blocking PKC‐dependent localization of αvβ3 to focal contacts

Fåhræus, R., & Lane, D. P. (1999) · The EMBO Journal · doi:10.1093/emboj/18.8.2106 · Cited by 112 · see citing works

Inflammatory Cytokines and Vascular Endothelial Growth Factor Stimulate the Release of Soluble Tie Receptor From Human Endothelial Cells Via Metalloprotease Activation

Yabkowitz, R., MEYER, S. R., Black, T., Elliott, G., Merewether, L. A., & Yamane, H. K. (1999) · Blood · doi:10.1182/blood.v93.6.1969.406k14_1969_1979 · Cited by 112 · see citing works

Treatment of colorectal liver metastases by adenoviral transfer of tissue inhibitor of metalloproteinases-2 into the liver tissue.

Brand, K., Baker, A. H., Pérez‐Canto, A., et al. (2000) · PubMed · Cited by 105 · see citing works

Functional Analysis of Cathepsin B-like Cysteine Proteases fromLeishmania donovani Complex

Somanna, A., Mundodi, V., & Gedamu, L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203034200 · Cited by 104 · see citing works

Proteases and their inhibitors in human brain tumours: a review.

ROOPRAI, H. K., & McCormick, D. (1998) · PubMed · Cited by 104 · see citing works

Biological Mechanisms of Glioma Invasion and Potential Therapeutic Targets

Tysnes, B. B., & Mahesparan, R. (2001) · Journal of Neuro-Oncology · doi:10.1023/a:1012249216117 · Cited by 103 · see citing works

Role of TGF-? in immune-evasion of cancer

Beck, C., Schreiber, H. W., & Rowley, D. A. (2001) · Microscopy Research and Technique · doi:10.1002/1097-0029(20010215)52:4 · Cited by 103 · see citing works

Cathepsin B and glioma invasion

Demchik, L. L., Sameni, M., Nelson, K. K., et al. (1999) · International Journal of Developmental Neuroscience · doi:10.1016/s0736-5748(99)00011-8 · Cited by 103 · see citing works

Vascular Endothelial Growth Factor Tightly Regulates In Vivo Development of Murine Hepatocellular Carcinoma Cells

Yoshiji, H., Kuriyama, S., Yoshii, J., Yamazaki, M., Kikukawa, M., Tsujinoue, H., Nakatani, T., & Fukui, H. (1998) · Hepatology · doi:10.1002/hep.510280607 · Cited by 101 · see citing works

Adenovirus-mediated delivery of antisense gene to urokinase-type plasminogen activator receptor suppresses glioma invasion and tumor growth.

Mohan, P., Chintala, S. K., Mohanam, S., Gladson, C. L., Kim, E. S., Gokaslan, Z. L., Lakka, S. S., Roth, J. A., Fang, B., Sawaya, R. A., et al. (1999) · PubMed · Cited by 97 · see citing works

Evaluation of the effects of swainsonine, captopril, tangeretin and nobiletin on the biological behaviour of brain tumour cells in vitro

ROOPRAI, H. K., Kandanearatchi, A., Maidment, S. L., Christidou, M., Trillo‐Pazos, G., Dexter, D. T., Rucklidge, G. J., Widmer, W. W., & Pilkington, G. J. (2001) · Neuropathology and Applied Neurobiology · doi:10.1046/j.0305-1846.2000.00298.x · Cited by 96 · see citing works

Up-regulation of urokinase and urokinase receptor genes in malignant astrocytoma.

Gladson, C. L., Pijuan-Thompson, V., Olman, M. A., et al. (1995) · PubMed · Cited by 95 · see citing works

Urokinase Regulates Vitronectin Binding by Controlling Urokinase Receptor Oligomerization

Sidénius, N., Andolfo, A., Fesce, R., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111736200 · Cited by 95 · see citing works

Wild Type and Mutant p53 Differentially Regulate the Gene Expression of Human Collagenase-3 (hMMP-13)

Sun, Y., Cheung, J. M., Martel‐Pelletier, J., Pelletier, J. P., Wenger, L., Altman, R. D., Howell, D. S., & Cheung, H. S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.15.11327 · Cited by 95 · see citing works

Transcription of Human Cathepsin B Is Mediated by Sp1 and Ets Family Factors in Glioma

Yan, S., Berquin, I. M., Troen, B. R., & Sloane, B. F. (2000) · DNA and Cell Biology · doi:10.1089/104454900314591 · Cited by 95 · see citing works

Urokinase‐type plasminogen activator and its receptor synergize to promote pathogenic proteolysis

Zhou, H., Nichols, A., Meda, P., & Vassalli, J. (2000) · The EMBO Journal · doi:10.1093/emboj/19.17.4817 · Cited by 94 · see citing works

Targeting Urokinase-Type Plasminogen Activator Receptor on Human Glioblastoma Tumors With Diphtheria Toxin Fusion Protein DTAT

Vallera, D. A. (2002) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/94.8.597 · Cited by 94 · see citing works

The high molecular weight Cat-301 chondroitin sulfate proteoglycan from brain is related to the large aggregating proteoglycan from cartilage, aggrecan.

Fryer, H. J., Kelly, G. M., Molinaro, L., & Hockfield, S. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50175-2 · Cited by 92 · see citing works

A peptide derived from the non-receptor-binding region of urokinase plasminogen activator inhibits glioblastoma growth and angiogenesis in vivo in combination with cisplatin

Mishima, K., Mazar, A. P., Gown, A. M., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.150239497 · Cited by 90 · see citing works

Age and Radiation Response in Glioblastoma Multiforme

Barker, F. G., Chang, S. M., Larson, D. A., Sneed, P. K., Wara, W. M., Wilson, C. B., & Prados, M. D. (2001) · Neurosurgery · doi:10.1097/00006123-200112000-00002 · Cited by 87 · see citing works

Some observations on the localization of hyaluronic acid in adult, newborn and embryonal rat brain

Bignami, A., & Asher, R. (1992) · International Journal of Developmental Neuroscience · doi:10.1016/0736-5748(92)90006-l · Cited by 87 · see citing works

The in situ localization of tenascin splice variants and thrombospondin 2 mRNA in the avian embryo

Tucker, R. P. (1993) · Development · doi:10.1242/dev.117.1.347 · Cited by 86 · see citing works

Induction of Matrix Metalloproteinase-9 Requires a Polymerized Actin Cytoskeleton in Human Malignant Glioma Cells

Chintala, S. K., Sawaya, R. A., Aggarwal, B. B., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.22.13545 · Cited by 78 · see citing works

Inhibition of in vivo tumorigenicity and invasiveness of a human glioblastoma cell line transfected with antisense uPAR vectors

Go, Y., Chintala, S. K., Mohanam, S., et al. (1997) · Clinical & Experimental Metastasis · doi:10.1023/a:1018410523635 · Cited by 77 · see citing works

Modulation of matrix metalloprotease-2 and invasion in human glioma cells by α3β1 integrin

Chintala, S. K., Sawaya, R. A., Gokaslan, Z. L., et al. (1996) · Cancer Letters · doi:10.1016/0304-3835(96)04215-2 · Cited by 74 · see citing works

Modulation of cystatin C expression impairs the invasive and tumorigenic potential of human glioblastoma cells

Konduri, S. D., Yanamandra, N., Siddique, K., Joseph, A., Dinh, D. H., Olivero, W. C., Gujrati, M., Kouraklis, G. P., Swaroop, A., Kyritsis, A. P., et al. (2002) · Oncogene · doi:10.1038/sj.onc.1205949 · Cited by 74 · see citing works

Role of plasminogen activator and of 92-KDa type IV collagenase in glioblastoma invasion using anin vitro Matrigel model

Rao, J. S., Steck, P. A., Tofilon, P. J., et al. (1994) · Journal of Neuro-Oncology · doi:10.1007/bf01050419 · Cited by 73 · see citing works

Immunohistochemical localization of extracellular matrix proteins in human glioma, both in vivo and in vitro

Chintala, S. K., Sawaya, R. A., Gokaslan, Z. L., et al. (1996) · Cancer Letters · doi:10.1016/0304-3835(96)04124-9 · Cited by 72 · see citing works

Interaction of Human Breast Fibroblasts with Collagen I Increases Secretion of Procathepsin B

Koblinski, J. E., Dosescu, J., Sameni, M., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204708200 · Cited by 71 · see citing works

Inhibition of Wilms' tumor growth by intramuscular administration of tissue inhibitor of metalloproteinases-4 plasmid DNA

Celiker, M., Wang, M., Atsidaftos, E., Liu, X., Liu, Y., Jiang, Y., Valderrama, E., Goldberg, I. D., & Shi, Y. E. (2001) · Oncogene · doi:10.1038/sj.onc.1204508 · Cited by 67 · see citing works

Prolonged p53 protein accumulation in trichothiodystrophy fibroblasts dependent on unrepaired pyrimidine dimers on the transcribed strands of cellular genes

Dumaz, N., Duthu, A., Ehrhart, J., Drougard, C., Appella, E., Anderson, C. W., May, P., Sarasin, A. R., & Daya–Grosjean, L. (1997) · Molecular Carcinogenesis · doi:10.1002/(sici)1098-2744(199712)20:4 · Cited by 66 · see citing works

ECM-mediated glioma cell invasion

Goldbrunner, R., Bernstein, J. J., & Tonn, J. (1998) · Microscopy Research and Technique · doi:10.1002/(sici)1097-0029(19981101)43:3 · Cited by 65 · see citing works

A synaptic vesicle antigen is restricted to the junctional region of the presynaptic plasma membrane.

Buckley, K. M., Schweitzer, E. S., Miljanich, G. P., et al. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.23.7342 · Cited by 63 · see citing works

Proteoglycans and neoplastic—mesenchymal cell interactions

Iozzo, R. V. (1984) · Human Pathology · doi:10.1016/s0046-8177(84)80326-3 · Cited by 63 · see citing works

Structure and Distribution of Glycoproteins and Glycosaminoglycans

Margolis, R. K., & Margolis, R. U. (1979) · Springer eBooks · doi:10.1007/978-1-4613-2925-1_3 · Cited by 61 · see citing works

Cathepsin B activity in human lung tumor cell lines: ultrastructural localization, pH sensitivity, and inhibitor status at the cellular level.

Spieß, E., Brüning, A. R. N. E., Gack, S., et al. (1994) · Journal of Histochemistry & Cytochemistry · doi:10.1177/42.7.8014475 · Cited by 61 · see citing works

Plasminogen activators catalyse conversion of inhibitor from fibrosarcoma cells to an inactive form with a lower apparent molecular mass

Nielsen, L. S., Andreasen, P. A., Grøndahl-Hansen, J., et al. (1986) · FEBS Letters · doi:10.1016/0014-5793(86)80261-7 · Cited by 61 · see citing works

High‐affinity urokinase‐derived cyclic peptides inhibiting urokinase/urokinase receptor‐interaction: effects on tumor growth and spread

Sato, S., Kopitz, C., Schmalix, W. A., Muehlenweg, B., Kessler, H., Schmitt, M., Krüger, A., & Magdolen, V. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03311-2 · Cited by 60 · see citing works

v-src induces cisplatin resistance by increasing the repair of cisplatin-DNA interstrand cross-links in human gallbladder adenocarcinoma cells

Masumoto, N., Nakano, S., Fujishima, H., Kohno, K., & Niho, Y. (1999) · International Journal of Cancer · doi:10.1002/(sici)1097-0215(19990301)80:5 · Cited by 57 · see citing works

The role of integrin receptors in aspects of glioma invasion in vitro

ROOPRAI, H. K., Meter, T. E. V., Panou, C., et al. (1999) · International Journal of Developmental Neuroscience · doi:10.1016/s0736-5748(99)00051-9 · Cited by 57 · see citing works

3-Amidinophenylalanine-based inhibitors of urokinase

Stürzebecher, J., Vieweg, H., Steinmetzer, T., et al. (1999) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(99)00541-7 · Cited by 56 · see citing works

Secretion of cathepsin B by human gliomas in vitro

McCormick, D. (1993) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.1993.tb00420.x · Cited by 56 · see citing works

The Structure of the Mouse Cathepsin B Gene and Its Putative Promoter

QIAN, F., Frankfater, A., Chan, S. J., & Steiner, D. F. (1991) · DNA and Cell Biology · doi:10.1089/dna.1991.10.159 · Cited by 55 · see citing works

Expression of the c-Kit receptor and its ligand SCF in non-small-cell lung carcinomas

Pietsch, T., Nicotra, M. R., Fraioli, R., Wolf, H. K., Mottolese, M., & Natali, P. G. (1998) · International Journal of Cancer · doi:10.1002/(sici)1097-0215(19980119)75:2 · Cited by 52 · see citing works

Nerve-dependent and -independent tenascin expression in the developing chick limb bud

Wehrle‐Haller, B., Koch, M., Baumgartner, S., Spring, J., & Chiquet, M. (1991) · Development · doi:10.1242/dev.112.2.627 · Cited by 51 · see citing works

Regulation of MMP-9 (type IV collagenase) production and invasiveness in gliomas by the extracellular signal-regulated kinase and jun amino-terminal kinase signaling cascades

Lakka, S. S., Jasti, S. L., Kyritsis, A. P., et al. (2000) · Clinical & Experimental Metastasis · doi:10.1023/a:1006724826083 · Cited by 50 · see citing works

Transfection of an Invasive Human Astrocytoma Cell Line with a TIMP-1 cDNA

Matsuzawa, K., Fukuyama, K., Hubbard, S. L., Dirks, P. B., & Rutka, J. T. (1996) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199601000-00009 · Cited by 50 · see citing works

Up-regulation of Urokinase-type Plasminogen Activator and its Receptor Correlates with Enhanced Invasion Activity of Human Glioma Cells Mediated by Transforming Growth Factor-α or Basic Fibroblast Growth Factor

Mori, T., Abé, T., Wakabayashi, Y., Hikawa, T., Matsuo, K., Yamada, Y., Kuwano, M., & Hori, S. (2000) · Journal of Neuro-Oncology · doi:10.1023/a:1006339717748 · Cited by 49 · see citing works

Elevated Levels of Mr92,000 Type IV Collagenase during Tumor Growthin Vivo

Sawaya, R. A., Go, Y., Kyritisis, A. P., et al. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9466 · Cited by 49 · see citing works

Inhibition of mammary tumor cell adhesion, migration, and invasion by the selective synthetic urokinase inhibitor B428.

Alonso, D. F., Tejera, Á. M., Ef, F., Joffé, E. B. D. K., & Gomez, D. E. (1998) · PubMed · Cited by 49 · see citing works

Production of Urokinase-Type Plasminogen Activator (u-PA) and Plasminogen Activator Inhibitor-1 (PAI-1) in Human Brain Tumours

Arai, Y., Kubota, T., Nakagawa, T., et al. (1998) · Acta Neurochirurgica · doi:10.1007/s007010050112 · Cited by 44 · see citing works

Binding of the urokinase-type plasminogen activator to its cell surface receptor is inhibited by low doses of suramin.

Behrendt, N., Rønne, E., & Danø, K. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53416-5 · Cited by 42 · see citing works

Matrix metalloprotease-9 release from monocytes increases as a function of differentiation: implications for neuroinflammation and neurodegeneration

Vos, C. M. P., Gartner, S., Ransohoff, R. M., et al. (2000) · Journal of Neuroimmunology · doi:10.1016/s0165-5728(00)00308-8 · Cited by 41 · see citing works

Time and dose dependency of the suppression of pulmonary metastases of rat mammary cancer by amiloride

Evans, D. M., Sloan-Stakleff, K. D., Arvan, M. E., et al. (1998) · Clinical & Experimental Metastasis · doi:10.1023/a:1006517614491 · Cited by 40 · see citing works

Elevated levels of cathepsin B in human glioblastoma cell lines

Konduri, S. D., Lakka, S. S., Τάσιου, Α., Yanamandra, N., Gondi, C. S., Dinh, D. T., Olivero, W. C., Gujrati, M. D., & Rao, J. S. (2001) · International Journal of Oncology · doi:10.3892/ijo.19.3.519 · Cited by 40 · see citing works

Stable transfection of urokinase-type plasminogen activator antisense construct modulates invasion of human glioblastoma cells.

Mohanam, S., Jasti, S. L., Kondraganti, S., et al. (2001) · PubMed · Cited by 40 · see citing works

Urokinase induces receptor mediated brain tumor cell migration and invasion

MacDonald, T. J., DeClerck, Y. A., & Laug, W. E. (1998) · Journal of Neuro-Oncology · doi:10.1023/a:1006150506789 · Cited by 39 · see citing works

Hepatic expression of acute-phase protein genes during carcinogenesis induced by peroxisome proliferators

Anderson, S. P., Cattley, R. C., & Corton, J. C. (1999) · Molecular Carcinogenesis · doi:10.1002/(sici)1098-2744(199912)26:4 · Cited by 39 · see citing works

Cathepsin B and its inhibitor stefin A in brain tumors

Strojnik, T., Zajc, I., Bervar, A., et al. (2000) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s004240000114 · Cited by 39 · see citing works

Inhibitory effects of phenylbutyrate on the proliferation, morphology, migration and invasiveness of malignant glioma cells

Engelhard, H. H., Homer, R. J., Duncan, H. A., et al. (1998) · Journal of Neuro-Oncology · doi:10.1023/a:1005865125588 · Cited by 38 · see citing works

Modulation of invasive properties of human glioblastoma cells stably expressing amino-terminal fragment of urokinase-type plasminogen activator

Mohanam, S., Chandrasekar, N., Yanamandra, N., Siddique, K., Mirza, F., Dinh, D. H., Olivero, W. C., & Rao, J. S. (2002) · Oncogene · doi:10.1038/sj.onc.1205893 · Cited by 38 · see citing works

Expression of cysteine protease inhibitors in human gliomas and meningiomas

Sivaparvathi, M., McCutcheon, I. E., Sawaya, R. A., Nicolson, G. L., & Rao, J. S. (1996) · Clinical & Experimental Metastasis · doi:10.1007/bf00123393 · Cited by 34 · see citing works

Biological Functions of Proteases and Inhibitors

Katunuma, N. (1994) · Cited by 33 · see citing works

Fibronectin-Proteoglycan Binding as the Molecular Basis for Fibroblast Adhesion to Extracellular Matrices

Rollins, B. J., Cathcart, M. K., & Culp, L. A. (1982) · Elsevier eBooks · doi:10.1016/b978-0-12-356103-9.50019-1 · Cited by 28 · see citing works

A novel role for the urokinase-type plasminogen activator receptor in apoptosis of malignant gliomas.

Kin, Y., Chintala, S. K., Go, Y., et al. (2000) · International Journal of Oncology · doi:10.3892/ijo.17.1.61 · Cited by 27 · see citing works

Expression and cellular localization of low-density lipoprotein receptor-related protein/α2-macroglobulin receptor in human glioblastoma in vivoreceptor in human glioblastoma in vivo

Yamamoto, M., Ikeda, K., Ohshima, K., Tsugu, H., Kimura, H., & Tomonaga, M. (1998) · Brain Tumor Pathology · doi:10.1007/bf02482097 · Cited by 25 · see citing works

Downregulation of urokinase-type plasminogen activator receptor (uPAR) induces caspase-mediated cell death in human glioblastoma cells

Yanamandra, N., Konduri, S. D., Mohanam, S., et al. (2000) · Clinical & Experimental Metastasis · doi:10.1023/a:1011941114862 · Cited by 25 · see citing works

Modulation of endothelial cell morphogenesis in vitro by MMP-9 during glial-endothelial cell interactions*

Chandrasekar, N., Jasti, S. L., Alfred-Yung, W. K., Ali‐Osman, F., Dinh, D. H., Olivero, W. C., Gujrati, M., Kyritsis, A. P., Nicolson, G. L., Rao, J. S., et al. (2000) · Clinical & Experimental Metastasis · doi:10.1023/a:1010833730407 · Cited by 24 · see citing works

Urokinase Antisense Oligodeoxynucleotides as a Novel Therapeutic Agent for Malignant Glioma:In Vitroandin VivoStudies of Uptake, Effects and Toxicity

Engelhard, H. H., Narang, C., Homer, R. J., et al. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.1519 · Cited by 24 · see citing works

Regulation of the urokinase-type plasminogen activator receptor gene in different grades of human glioma cell lines.

Bhattacharya, A., Lakka, S. S., Mohanam, S., Boyd, D. D., & Rao, J. S. (2001) · PubMed · Cited by 23 · see citing works

Regulation of the uPA gene in various grades of human glioma cells.

Lakka, S. S., Bhattacharya, A., Mohanam, S., et al. (2001) · International Journal of Oncology · doi:10.3892/ijo.18.1.71 · Cited by 22 · see citing works

Elevated levels of urokinase-type plasminogen activator and its receptor during tumor growth in vivo.

Mohanam, S., Go, Y., Sawaya, R. A., Venkaiah, B., Mohan, P. M., Kouraklis, G. P., Gokaslan, Z. L., Lagos, G., & Rao, J. (1999) · International Journal of Oncology · doi:10.3892/ijo.14.1.169 · Cited by 21 · see citing works

Expression and localisation of urokinase-type plasminogen activator gene in gliomas

Zhang, X., Bu, X., Zhen, H., Fei, Z., Zhang, J.-N., & Fu, L. (2000) · Journal of Clinical Neuroscience · doi:10.1054/jocn.1999.0161 · Cited by 19 · see citing works

Glioma cells deficient in urokinase plaminogen activator receptor expression are susceptible to tumor necrosis factor-alpha-related apoptosis-inducing ligand-induced apoptosis.

Krishnamoorthy, B., Darnay, B. G., Aggarwal, B. B., et al. (2001) · PubMed · Cited by 18 · see citing works

Increased invasion of neuroglioma cells transfected with urokinase plasminogen activator receptor cDNA.

Mohanam, S., Chintala, S. K., Mohan, P., et al. (1998) · International Journal of Oncology · doi:10.3892/ijo.13.6.1285 · Cited by 11 · see citing works

High-Molecular-Weight Serum Protein Complexes Differentially Promote Cell Migration and the Focal Adhesion Localization of the Urokinase Receptor in Human Glioma Cells

Hedberg, K. K., Stauff, C., Høyer‐Hansen, G., et al. (2000) · Experimental Cell Research · doi:10.1006/excr.2000.4873 · Cited by 10 · see citing works

The role of microglia in central nervous system immunity and glioma immunology

Yang, I., Han, S. J., Kaur, G., Crane, C., & Parsa, A. T. (2010) · Journal of Clinical Neuroscience · doi:10.1016/j.jocn.2009.05.006 · Cited by 410 · see citing works

The urokinase plasminogen activator system: a target for anti-cancer therapy

Ulisse, S., Baldini, E., Sorrenti, S., & D'Armiento, M. (2009) · Current Cancer Drug Targets · doi:10.2174/156800909787314002 · Cited by 312 · see citing works

A Role for Fibrillar Collagen Deposition and the Collagen Internalization Receptor Endo180 in Glioma Invasion

Huijbers, I. J., Iravani, M., Popov, S., Robertson, D., Al-Sarraj, S., Jones, C., & Isacke, C. M. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009808 · Cited by 223 · see citing works

Perineuronal nets decrease membrane capacitance of peritumoral fast spiking interneurons in a model of epilepsy

Tewari, B. P., Chaunsali, L., Campbell, S. L., Patel, D. C., Goode, A. E., & Sontheimer, H. (2018) · Nature Communications · doi:10.1038/s41467-018-07113-0 · Cited by 208 · see citing works

Cannabidiol, a non-psychoactive cannabinoid compound, inhibits proliferation and invasion in U87-MG and T98G glioma cells through a multitarget effect

Solinas, M., Massi, P., Cinquina, V., Valenti, M., Bolognini, D., Gariboldi, M., Monti, E., Rubino, T., & Parolaro, D. (2013) · PLoS ONE · doi:10.1371/journal.pone.0076918 · Cited by 159 · see citing works

Lost in disruption: Role of proteases in glioma invasion and progression

Mentlein, R., Hattermann, K., & Held-Feindt, J. (2012) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2011.12.001 · Cited by 85 · see citing works

Contamination of Tissue Cultures by Mycoplasmas

Rottem, S., S., N., & D., J. (2012) · Biomedical Tissue Culture · doi:10.5772/51518 · Cited by 28 · see citing works

[Partial purification and properties of proteases of bitoxibacillin].

Kuchera, M., & Nm, B. (1980) · PubMed

ANALYSIS OF PROTEASE KINDS AND ACTIVITIES IN SEVEN KINDS OF TISSUES AND ORGANS OF ANDRIAS DAVIDIANUS

Ze-hua, X. (2004) · Chieh P'ou Hsueh Pao

In search of partners: linking extracellular proteases to substrates

Overall, C. M., & Blobel, C. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2120 · Cited by 350 · see citing works

Proteases in the diet of monogastric animals

Kryukov, V., Zinoviev, S. V., & Nekrasov, R. V. (2021) · Agrarian science · doi:10.32634/0869-8155-2021-344-1-30-38 · Cited by 3 · see citing works

Are bacterial proteases important virulence factors?

Lantz, M. S. (1997) · Journal of Periodontal Research · doi:10.1111/j.1600-0765.1997.tb01393.x · Cited by 91 · see citing works