Cancer Metastasis: The Role of the Extracellular Matrix and the Heparan Sulfate Proteoglycan Perlecan

Global cancer statistics 2018: GLOBOCAN estimates of incidence and mortality worldwide for 36 cancers in 185 countries

Bray, F., Ferlay, J., Soerjomataram, I., Siegel, R. L., Torre, L. A., & Jemal, A. (2018) · CA: A Cancer Journal for Clinicians · doi:10.3322/caac.21492 · Cited by 84,109 · see citing works

Hallmarks of Cancer: The Next Generation

Hanahan, D., & Weinberg, R. A. (2011) · Cell · doi:10.1016/j.cell.2011.02.013 · Cited by 66,590 · see citing works

Epithelial-Mesenchymal Transitions in Development and Disease

Thiery, J. P., Acloque, H., Huang, R. Y. J., & Nieto, M. A. (2009) · Cell · doi:10.1016/j.cell.2009.11.007 · Cited by 9,931 · see citing works

Microenvironmental regulation of tumor progression and metastasis

Quail, D. F., & Joyce, J. A. (2013) · Nature Medicine · doi:10.1038/nm.3394 · Cited by 7,994 · see citing works

Molecular Mechanisms of Stress-Responsive Changes in Collagen and Elastin Networks in Skin

Aziz, J., Shezali, H., Radzi, Z., Yahya, N. A., Abu Kassim, N. H., Czernuszka, J., & Rahman, M. T. (2016) · Skin Pharmacology and Physiology · doi:10.1159/000447017 · Cited by 7,323 · see citing works

Remodelling the extracellular matrix in development and disease

Bonnans, C., Chou, J., & Werb, Z. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3904 · Cited by 4,367 · see citing works

Cancer genes and the pathways they control

Vogelstein, B., & Kinzler, K. W. (2004) · Nature Medicine · doi:10.1038/nm1087 · Cited by 4,245 · see citing works

The Extracellular Matrix: Not Just Pretty Fibrils

Hynes, R. O. (2009) · Science · doi:10.1126/science.1176009 · Cited by 3,527 · see citing works

Transitions between epithelial and mesenchymal states: acquisition of malignant and stem cell traits

Polyak, K., & Weinberg, R. A. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2620 · Cited by 3,302 · see citing works

VEGFR1-positive haematopoietic bone marrow progenitors initiate the pre-metastatic niche

Kaplan, R. N., Riba, R. D., Zacharoulis, S., Bramley, A. H., Vincent, L., Costa, C., MacDonald, D. D., Jin, D. K., Shido, K., Kerns, S. A., et al. (2005) · Nature · doi:10.1038/nature04186 · Cited by 3,288 · see citing works

The extracellular matrix: A dynamic niche in cancer progression

Lu, P., Weaver, V. M., & Werb, Z. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201102147 · Cited by 3,024 · see citing works

Extracellular matrix structure

Theocharis, A. D., Skandalis, S. S., Gialeli, C., & Karamanos, N. K. (2016) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2015.11.001 · Cited by 2,598 · see citing works

Extracellular Matrix Degradation and Remodeling in Development and Disease

Lu, P., Takai, K., Weaver, V. M., & Werb, Z. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005058 · Cited by 2,265 · see citing works

Mechanotransduction and extracellular matrix homeostasis

Humphrey, J. D., Dufresne, E. R., & Schwartz, M. A. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3896 · Cited by 2,187 · see citing works

Tumor metastasis: mechanistic insights and clinical challenges

Steeg, P. S. (2006) · Nature Medicine · doi:10.1038/nm1469 · Cited by 2,125 · see citing works

The extracellular matrix modulates the hallmarks of cancer

Pickup, M. W., Mouw, J. K., & Weaver, V. M. (2014) · EMBO Reports · doi:10.15252/embr.201439246 · Cited by 2,014 · see citing works

Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis.

Yu, Q., & Stamenkovic, I. (2000) · PubMed · Cited by 1,952 · see citing works

Pre-metastatic niches: organ-specific homes for metastases

Peinado, H., Zhang, H., Matei, I. R., Costa-Silva, B., Hoshino, A., Rodrigues, G., Psaila, B., Kaplan, R. N., Bromberg, J. F., Kang, Y., et al. (2017) · Nature Reviews Cancer · doi:10.1038/nrc.2017.6 · Cited by 1,889 · see citing works

The multistep nature of cancer

Vogelstein, B., & Kinzler, K. W. (1993) · Trends in Genetics · doi:10.1016/0168-9525(93)90209-z · Cited by 1,858 · see citing works

Microenvironmental regulation of tumour angiogenesis

De Palma, M., Biziato, D., & Petrova, T. V. (2017) · Nature Reviews Cancer · doi:10.1038/nrc.2017.51 · Cited by 1,847 · cited 1× · see citing works

Direct signaling between platelets and cancer cells induces an epithelial–mesenchymal-like transition and promotes metastasis

Labelle, M., Begum, S., & Hynes, R. O. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.09.009 · Cited by 1,833 · see citing works

Collagen reorganization at the tumor-stromal interface facilitates local invasion

Provenzano, P. P., Eliceiri, K. W., Campbell, J. M., Inman, D. R., White, J. G., & Keely, P. J. (2006) · BMC Medicine · doi:10.1186/1741-7015-4-38 · Cited by 1,804 · see citing works

VEGF as a Key Mediator of Angiogenesis in Cancer

Carmeliet, P. (2005) · Oncology · doi:10.1159/000088478 · Cited by 1,776 · see citing works

Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-β and promotes tumor invasion and angiogenesis

Yu, Q., & Stamenkovic, I. (2000) · Genes & Development · doi:10.1101/gad.14.2.163 · Cited by 1,754 · see citing works

Basement membranes: structure, assembly and role in tumour angiogenesis

Kalluri, R. (2003) · Nature reviews. Cancer · doi:10.1038/nrc1094 · Cited by 1,748 · see citing works

Heparan sulphate proteoglycans fine-tune mammalian physiology

Bishop, J. R., Schuksz, M., & Esko, J. D. (2007) · Nature · doi:10.1038/nature05817 · Cited by 1,631 · see citing works

Remodeling and homeostasis of the extracellular matrix: implications for fibrotic diseases and cancer

Cox, T. R., & Erler, J. T. (2011) · Disease Models & Mechanisms · doi:10.1242/dmm.004077 · Cited by 1,569 · see citing works

Extracellular Matrix Assembly: A Multiscale Deconstruction

Mouw, J. K., Ou, G., & Weaver, V. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3902 · Cited by 1,534 · see citing works

Heparan Sulfate ProteoglycansPreprint

Sarrazin, S., Lamanna, W. C., & Esko, J. D. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004952 · Cited by 1,524 · see citing works

Reversion of the Malignant Phenotype of Human Breast Cells in Three-Dimensional Culture and In Vivo by Integrin Blocking Antibodies

Weaver, V. M., Petersen, O. W., Wang, F., Larabell, C. A., Briand, P., Damsky, C., & Bissell, M. J. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.137.1.231 · Cited by 1,483 · see citing works

The biology and role of CD44 in cancer progression: therapeutic implications

Chen, C., Zhao, S., Karnad, A. B., & Freeman, J. W. (2018) · Journal of Hematology & Oncology · doi:10.1186/s13045-018-0605-5 · Cited by 1,404 · see citing works

Interactions between cancer stem cells and their niche govern metastatic colonization

Malanchi, I., Santamaria-Martínez, A., Susanto, E., Peng, H., Lehr, H.-A., Delaloye, J.-F., & Huelsken, J. (2012) · Nature · doi:10.1038/nature10694 · Cited by 1,339 · see citing works

Aligned Collagen Is a Prognostic Signature for Survival in Human Breast Carcinoma

Conklin, M. W., Eickhoff, J. C., Riching, K. M., Pehlke, C. A., Eliceiri, K. W., Provenzano, P. P., Friedl, A., & Keely, P. J. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2010.11.076 · Cited by 1,273 · see citing works

The perivascular niche regulates breast tumour dormancy

Ghajar, C. M., Peinado, H., Mori, H., Matei, I. R., Evason, K. J., Brazier, H., Almeida, D., Koller, A., Hajjar, K. A., Stainier, D. Y. R., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2767 · Cited by 1,148 · cited 2× · see citing works

Pan-cancer whole-genome analyses of metastatic solid tumours

Priestley, P., Baber, J., Lolkema, M. P., Steeghs, N., de Bruijn, E., Shale, C., Duyvesteyn, K., Haidari, S., van Hoeck, A., Onstenk, W., et al. (2019) · Nature · doi:10.1038/s41586-019-1689-y · Cited by 1,106 · see citing works

Role of Extracellular Matrix in Development and Cancer Progression

Walker, C., Mojares, E., & Hernández, A. E. D. R. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19103028 · Cited by 1,103 · see citing works

Platelets and fibrin(ogen) increase metastatic potential by impeding natural killer cell–mediated elimination of tumor cells

Palumbo, J. S., Talmage, K. E., Massari, J. V., Jeunesse, C. M. L., Flick, M. J., Kombrinck, K. W., Jiroušková, M., & Degen, J. L. (2004) · Blood · doi:10.1182/blood-2004-06-2272 · Cited by 1,000 · see citing works

Molecular diversity of heparan sulfate

Esko, J. D., & Lindahl, U. (2001) · Journal of Clinical Investigation · doi:10.1172/jci200113530 · Cited by 945 · see citing works

Breast cancer cells produce tenascin C as a metastatic niche component to colonize the lungs

Oskarsson, T., Acharyya, S., Zhang, X. H.-F., Vanharanta, S., Tavazoie, S. F., Morris, P. G., Downey, R. J., Manova-Todorova, K., Brogi, E., & Massagué, J. (2011) · Nature Medicine · doi:10.1038/nm.2379 · Cited by 869 · see citing works

Mammalian heparanase: Gene cloning, expression and function in tumor progression and metastasis

Vlodavsky, I., Friedmann, Y., Elkin, M., Aingorn, H., Atzmon, R., Ishai-Michaeli, R., Bitan, M., Pappo, O., Peretz, T., Michal, I., et al. (1999) · Nature Medicine · doi:10.1038/10518 · Cited by 803 · see citing works

Metastasis genes: A progression puzzle

Bernards, R., & Weinberg, R. A. (2002) · Nature · doi:10.1038/418823a · Cited by 801 · see citing works

Early dissemination seeds metastasis in breast cancer

Hosseini, H., Obradović, M. M. S., Hoffmann, M., Harper, K. L., Sosa, M. S., Werner‐Klein, M., Nanduri, L. K., Werno, C., Ehrl, C., Maneck, M., et al. (2016) · Nature · doi:10.1038/nature20785 · Cited by 740 · see citing works

Preparing the “Soil”: The Premetastatic Niche

Kaplan, R. N., Rafii, S., & Lyden, D. C. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-2407 · Cited by 665 · see citing works

Protease-dependent versus -independent cancer cell invasion programs: three-dimensional amoeboid movement revisited

Sabeh, F., Shimizu‐Hirota, R., & Weiss, S. J. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200807195 · Cited by 658 · see citing works

Tumor microenvironment: The role of the tumor stroma in cancer

Li, H., Fan, X., & Houghton, J. (2007) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21159 · Cited by 646 · see citing works

Roles of heparan-sulphate glycosaminoglycans in cancer

Sasisekharan, R., Shriver, Z. H., Venkataraman, G., & Narayanasami, U. (2002) · Nature reviews. Cancer · doi:10.1038/nrc842 · Cited by 621 · see citing works

Suppression of anoikis and induction of metastasis by the neurotrophic receptor TrkB

Douma, S., van Laar, T., Zevenhoven, J., Meuwissen, R. L. J., van Garderen, E., & Peeper, D. S. (2004) · Nature · doi:10.1038/nature02765 · Cited by 608 · see citing works

The Degradation of Human Endothelial Cell-derived Perlecan and Release of Bound Basic Fibroblast Growth Factor by Stromelysin, Collagenase, Plasmin, and Heparanases

Whitelock, J. M., Murdoch, A. D., Iozzo, R. V., & Underwood, P. A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.17.10079 · Cited by 597 · see citing works

The rationale for targeting the LOX family in cancer

Barker, H. E., Cox, T. R., & Erler, J. T. (2012) · Nature reviews. Cancer · doi:10.1038/nrc3319 · Cited by 595 · see citing works

Malignant cells facilitate lung metastasis by bringing their own soil

Duda, D. G., Duyverman, A. M. M. J., Kohno, M., Snuderl, M., Steller, E. J. A., Fukumura, D., & Jain, R. K. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016234107 · Cited by 594 · see citing works

Mechanoreciprocity in cell migration

van Helvert, S., Storm, C., & Friedl, P. (2018) · Nature Cell Biology · doi:10.1038/s41556-017-0012-0 · Cited by 587 · see citing works

LOX-Mediated Collagen Crosslinking Is Responsible for Fibrosis-Enhanced Metastasis

Cox, T. R., Bird, D., Baker, A.-M., Barker, H. E., Ho, M. W.-Y., Lang, G., & Erler, J. T. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-2233 · Cited by 571 · see citing works

Proteoglycans in cancer biology, tumour microenvironment and angiogenesis

Iozzo, R. V., & Sanderson, R. D. (2010) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2010.01236.x · Cited by 569 · see citing works

Mechanism of early dissemination and metastasis in Her2+ mammary cancer

Harper, K. L., Sosa, M. S., Entenberg, D. R., Hosseini, H., Cheung, J. F., Nobre, A. R., Avivar‐Valderas, A., Nagi, C., Girnius, N., Davis, R. J., et al. (2016) · Nature · doi:10.1038/nature20609 · Cited by 569 · see citing works

Sulfation patterns of glycosaminoglycans encode molecular recognition and activity

Gama, C. I., Tully, S. E., Sotogaku, N., Clark, P. M., Rawat, M., Vaidehi, N., Goddard, W. A., Nishi, A., & Hsieh‐Wilson, L. C. (2006) · Nature Chemical Biology · doi:10.1038/nchembio810 · Cited by 561 · see citing works

Glycosaminoglycans: key players in cancer cell biology and treatment

Afratis, N. A., Gialeli, C., Nikitovic, D., Tsegenidis, T., Karousou, E. G., Theocharis, A. D., Pavão, M. S. G., Tzanakakis, G. N., & Karamanos, N. K. (2012) · FEBS Journal · doi:10.1111/j.1742-4658.2012.08529.x · Cited by 557 · see citing works

Autologous Chemotaxis as a Mechanism of Tumor Cell Homing to Lymphatics via Interstitial Flow and Autocrine CCR7 Signaling

Shields, J. D., Fleury, M. E., Yong, C., Tomei, A. A., Randolph, G. J., & Swartz, M. A. (2007) · Cancer Cell · doi:10.1016/j.ccr.2007.04.020 · Cited by 555 · see citing works

Perlecan, basal lamina proteoglycan, promotes basic fibroblast growth factor-receptor binding, mitogenesis, and angiogenesis.

Aviezer, D., Hecht, D., Safran, M., Eisinger, M., David, G., & Yayon, A. (1994) · Cell · doi:10.1016/0092-8674(94)90031-0 · Cited by 546 · see citing works

Activating and inhibitory heparin sequences for FGF-2 (basic FGF). Distinct requirements for FGF-1, FGF-2, and FGF-4.

Guimond, S. E., Maccarana, M., Olwin, B. B., Lindahl, U., & Rapraeger, A. C. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80471-2 · Cited by 545 · see citing works

Basement membrane proteoglycans: from cellar to ceiling

Iozzo, R. V. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1702 · Cited by 521 · see citing works

Anoikis: A necessary death program for anchorage-dependent cells

Chiarugi, P., & Giannoni, E. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2008.07.023 · Cited by 495 · see citing works

RNA sequencing of pancreatic circulating tumour cells implicates WNT signalling in metastasis

Yu, M., Ting, D. T., Stott, S. L., Wittner, B. S., Ozsolak, F., Paul, S., Ciciliano, J. C., Smas, M. E., Winokur, D., Gilman, A. J., et al. (2012) · Nature · doi:10.1038/nature11217 · Cited by 484 · see citing works

Biomarker Discovery from Pancreatic Cancer Secretome Using a Differential Proteomic Approach

Grønborg, M., Kristiansen, T. Z., Iwahori, A., Chang, R., Reddy, R., Sato, N., Molina, H., Jensen, O. N., Hruban, R. H., Goggins, M., et al. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m500178-mcp200 · Cited by 482 · see citing works

Glypican-3 Promotes the Growth of Hepatocellular Carcinoma by Stimulating Canonical Wnt Signaling

Capurro, M., Xiang, Y., Lobe, C. G., & Filmus, J. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-4244 · Cited by 470 · see citing works

Heparan sulfate proteoglycans: heavy hitters in the angiogenesis arena

Iozzo, R. V., & Antonio, J. D. S. (2001) · Journal of Clinical Investigation · doi:10.1172/jci13738 · Cited by 455 · see citing works

Breaching the basement membrane: who, when and how?

Rowe, R. G., & Weiss, S. J. (2008) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.08.007 · Cited by 443 · see citing works

Glypican-3 as a Serum Marker for Hepatocellular Carcinoma

Capurro, M., & Filmus, J. (2005) · Cancer Research · doi:10.1158/0008-5472.372.65.1 · Cited by 432 · see citing works

Cloning and Characterization of Two Extracellular Heparin-degrading Endosulfatases in Mice and Humans

Morimoto‐Tomita, M., Uchimura, K., Werb, Z., Hemmerich, S., & Rosen, S. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205131200 · Cited by 430 · see citing works

The BMP Inhibitor Coco Reactivates Breast Cancer Cells at Lung Metastatic Sites

Gao, H., Chakraborty, G., Lee-Lim, A. P., Mo, Q., Decker, M., Vonica, A., Shen, R., Brogi, E., Brivanlou, A. H., & Giancotti, F. G. (2012) · Cell · doi:10.1016/j.cell.2012.06.035 · Cited by 430 · see citing works

Hypoxic stimulation of vascular endothelial growth factor expression in vitro and in vivo.

Minchenko, О. H., Bauer, T., Salceda, S., & Caro, J. (1994) · PubMed · Cited by 429 · see citing works

Bone morphogenetic protein 7 in dormancy and metastasis of prostate cancer stem-like cells in bone

Kobayashi, A., Okuda, H., Xing, F., Pandey, P. R., Watabe, M., Hirota, S., Pai, S. K., Liu, W., Fukuda, K., Chambers, C., et al. (2011) · The Journal of Experimental Medicine · doi:10.1084/jem.20110840 · Cited by 428 · see citing works

Members of the syndecan family of heparan sulfate proteoglycans are expressed in distinct cell-, tissue-, and development-specific patterns.

Kim, C. W., Goldberger, O., Gallo, R. L., & Bernfield, M. R. (1994) · Molecular Biology of the Cell · doi:10.1091/mbc.5.7.797 · Cited by 426 · see citing works

Remodeling of the Collagen Matrix in Aging Skin Promotes Melanoma Metastasis and Affects Immune Cell Motility

Kaur, A., Ecker, B. L., Douglass, S. M., Kugel, C. H., Webster, M. R., Almeida, F. V., Somasundaram, R., Hayden, J. E., Ban, E., Ahmadzadeh, H., et al. (2018) · Cancer Discovery · doi:10.1158/2159-8290.cd-18-0193 · Cited by 421 · see citing works

Heparan Sulfate: A Complex Polymer Charged with Biological Activity

Whitelock, J. M., & Iozzo, R. V. (2005) · Chemical Reviews · doi:10.1021/cr010213m · Cited by 410 · see citing works

Feeling Stress: The Mechanics of Cancer Progression and Aggression

Northcott, J. M., Dean, I. S., Mouw, J. K., & Weaver, V. M. (2018) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2018.00017 · Cited by 407 · see citing works

Proteoglycans in health and disease: novel roles for proteoglycans in malignancy and their pharmacological targeting

Theocharis, A. D., Skandalis, S. S., Tzanakakis, G. N., & Karamanos, N. K. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07800.x · Cited by 403 · see citing works

Angiocrine factors from Akt-activated endothelial cells balance self-renewal and differentiation of haematopoietic stem cells

Kobayashi, H., Butler, J. M., O’Donnell, R. K., Kobayashi, M., Ding, B., Bonner, B., Chiu, V. K., Nolan, D. J., Shido, K., Benjamin, L. E., et al. (2010) · Nature Cell Biology · doi:10.1038/ncb2108 · Cited by 402 · see citing works

Organotropism: new insights into molecular mechanisms of breast cancer metastasis

Chen, W., Hoffmann, A. D., Liu, H., & Liu, X. (2018) · npj Precision Oncology · doi:10.1038/s41698-018-0047-0 · Cited by 393 · see citing works

Heparan sulfate proteoglycans: heavy hitters in the angiogenesis arena

Iozzo, R. V., & Antonio, J. D. S. (2001) · Journal of Clinical Investigation · doi:10.1172/jci200113738 · Cited by 390 · see citing works

Gr-1+CD11b+ Myeloid Cells Tip the Balance of Immune Protection to Tumor Promotion in the Premetastatic Lung

Yan, H. H., Pickup, M. W., Pang, Y., Gorska, A. E., Li, Z., Chytil, A. M., Geng, Y., Gray, J. W., Moses, H. L., & Yang, L. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-0706 · Cited by 372 · see citing works

The cell-surface heparan sulfate proteoglycan glypican-1 regulates growth factor action in pancreatic carcinoma cells and is overexpressed in human pancreatic cancer.

Kleeff, J. H., Ishiwata, T., Kumbasar, A., Friess, H., Büchler, M. W., Lander, A. D., & Korc, M. (1998) · Journal of Clinical Investigation · doi:10.1172/jci4105 · Cited by 369 · see citing works

Integrin β 1 -focal adhesion kinase signaling directs the proliferation of metastatic cancer cells disseminated in the lungs

Shibue, T., & Weinberg, R. A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904227106 · Cited by 365 · see citing works

Biomechanical and biochemical remodeling of stromal extracellular matrix in cancer

Malik, R., Lelkes, P. I., & Cukierman, E. (2015) · Trends in biotechnology · doi:10.1016/j.tibtech.2015.01.004 · Cited by 346 · see citing works

Proteoglycans in health and disease: the multiple roles of syndecan shedding

Manon‐Jensen, T., Itoh, Y., & Couchman, J. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07798.x · Cited by 337 · see citing works

Physiological degradation converts the soluble syndecan-1 ectodomain from an inhibitor to a potent activator of FGF-2

Kato, M., Wang, H., Kainulainen, V., Fitzgerald, M. L., Ledbetter, S. R., Ornitz, D. M., & Bernfield, M. R. (1998) · Nature Medicine · doi:10.1038/nm0698-691 · Cited by 337 · see citing works

Primary structure of the human heparan sulfate proteoglycan from basement membrane (HSPG2/perlecan). A chimeric molecule with multiple domains homologous to the low density lipoprotein receptor, laminin, neural cell adhesion molecules, and epidermal growth factor.

Murdoch, A. D., Dodge, G. R., COHEN, I. R., Tuan, R. S., & Iozzo, R. V. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42478-7 · Cited by 315 · see citing works

Tumor cell–associated tissue factor and circulating hemostatic factors cooperate to increase metastatic potential through natural killer cell–dependent and–independent mechanisms

Palumbo, J. S., Talmage, K. E., Massari, J. V., Jeunesse, C. M. L., Flick, M. J., Kombrinck, K. W., Hu, Z., Barney, K. A., & Degen, J. L. (2007) · Blood · doi:10.1182/blood-2007-01-065995 · Cited by 313 · see citing works

Development of T Cells Redirected to Glypican-3 for the Treatment of Hepatocellular Carcinoma

Gao, H., Li, K., Tu, H., Pan, X., Jiang, H., Shi, B., Kong, J., Wang, H., Yang, S., Gu, J., et al. (2014) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-1170 · Cited by 313 · see citing works

CAF Subpopulations: A New Reservoir of Stromal Targets in Pancreatic Cancer

Pereira, B., Vennin, C., Papanicolaou, M., Chambers, C. R., Herrmann, D., Morton, J. P., Cox, T. R., & Timpson, P. (2019) · Trends in cancer · doi:10.1016/j.trecan.2019.09.010 · Cited by 309 · see citing works

Heparan Sulfate Biosynthesis

Kreuger, J., & Kjellén, L. (2012) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155412464972 · Cited by 302 · see citing works

Proteolytic interstitial cell migration: a five-step process

Friedl, P., & Wolf, K. (2009) · Cancer and Metastasis Reviews · doi:10.1007/s10555-008-9174-3 · Cited by 288 · see citing works

Chapter 3 Interactions Between Heparan Sulfate and Proteins—Design and Functional Implications

Lindahl, U., & Li, J. (2009) · International review of cytology · doi:10.1016/s1937-6448(09)76003-4 · Cited by 274 · see citing works

Diverse Cell Signaling Events Modulated by Perlecan

Whitelock, J. M., Melrose, J., & Iozzo, R. V. (2008) · Biochemistry · doi:10.1021/bi8013938 · Cited by 270 · see citing works

CAF hierarchy driven by pancreatic cancer cell p53-status creates a pro-metastatic and chemoresistant environment via perlecan

Vennin, C., Mélénec, P., Rouet, R., Nobis, M., Cazet, A. S., Murphy, K. J., Herrmann, D., Reed, D. A., Lucas, M. C., Warren, S. C., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10968-6 · Cited by 268 · see citing works

Substrate Specificity of Heparanases from Human Hepatoma and Platelets

Pikas, D. S., Li, J., Vlodavsky, I., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.30.18770 · Cited by 264 · see citing works

Transient tissue priming via ROCK inhibition uncouples pancreatic cancer progression, sensitivity to chemotherapy, and metastasis

Vennin, C., Chin, V. T., Warren, S. C., Lucas, M. C., Herrmann, D., Magenau, A., Mélénec, P., Walters, S. N., del Monte‐Nieto, G., Conway, J. R. W., et al. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aai8504 · Cited by 264 · see citing works

Heparan sulfate proteoglycans in invasion and metastasis

Sanderson, R. D. (2001) · Seminars in Cell and Developmental Biology · doi:10.1006/scdb.2000.0241 · Cited by 263 · see citing works

KLF4-dependent perivascular cell plasticity mediates pre-metastatic niche formation and metastasis

Murgai, M., Ju, W., Eason, M., Kline, J., Beury, D. W., Kaczanowska, S., Miettinen, M. M., Kruhlak, M., Lei, H., Shern, J. F., et al. (2017) · Nature Medicine · doi:10.1038/nm.4400 · Cited by 263 · see citing works

The emerging role of TGF-β superfamily coreceptors in cancer

Bernabéu, C., López-Novoa, J. M., & Quintanilla, M. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.07.003 · Cited by 254 · see citing works

Endorepellin causes endothelial cell disassembly of actin cytoskeleton and focal adhesions through α2β1 integrin

Bix, G. J., Fu, J., González, E. M. G., Macro, L., Barker, A., Campbell, S., Zutter, M. M., Santoro, S. A., Kim, J. K., Höök, M., et al. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200401150 · Cited by 252 · see citing works

Targeting ECM Disrupts Cancer Progression

Venning, F. A., Wullkopf, L., & Erler, J. T. (2015) · Frontiers in Oncology · doi:10.3389/fonc.2015.00224 · Cited by 252 · see citing works

Pulmonary Vascular Destabilization in the Premetastatic Phase Facilitates Lung Metastasis

Huang, Y., Song, N., Ding, Y., Yuan, S., Li, X., Cai, H., Shi, H., & Luo, Y. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-4382 · Cited by 247 · see citing works

Significance of Heparanase in Cancer and Inflammation

Vlodavsky, I., Beckhove, P., Lerner, I., Pisano, C., Meirovitz, A., Ilan, N., & Elkin, M. (2011) · Cancer Microenvironment · doi:10.1007/s12307-011-0082-7 · Cited by 240 · see citing works

Force Matters: Biomechanical Regulation of Cell Invasion and Migration in Disease

Kai, F., Laklai, H., & Weaver, V. M. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.03.007 · Cited by 240 · see citing works

Heparanase expression in primary and metastatic pancreatic cancer.

Koliopanos, A., Friess, H., Kleeff, J. H., et al. (2001) · PubMed · Cited by 237 · see citing works

Structural interactions of fibroblast growth factor receptor with its ligands

Stauber, D. J., DiGabriele, A. D., & Hendrickson, W. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.1.49 · Cited by 233 · see citing works

An Introduction to Proteoglycans and Their Localization

Couchman, J., & Pataki, C. A. (2012) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155412464638 · Cited by 233 · see citing works

Heparan Sulfate Proteoglycans as Extracellular Docking Molecules for Matrilysin (Matrix Metalloproteinase 7)

Yu, W., & Woessner, J. F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.6.4183 · Cited by 232 · see citing works

Modulation of the Heparanase-inhibiting Activity of Heparin through Selective Desulfation, Graded N-Acetylation, and Glycol Splitting

Naggi, A., Casu, B., Pérez, M., Torri, G., Cassinelli, G., Penco, S., Pisano, C., Giannini, G., Ishai-Michaeli, R., & Vlodavsky, I. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414217200 · Cited by 228 · see citing works

Tumor cell surface heparan sulfate as cryptic promoters or inhibitors of tumor growth and metastasis

Liu, D., Shriver, Z. H., Venkataraman, G., Shabrawi, Y. E., & Sasisekharan, R. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.012578299 · Cited by 227 · see citing works

Basement Membrane Proteoglycans: Modulators Par Excellence of Cancer Growth and Angiogenesis

Iozzo, R. V., Zoeller, J. J., & Nyström, A. (2009) · Molecules and Cells · doi:10.1007/s10059-009-0069-0 · Cited by 221 · see citing works

Critical role for lysyl oxidase in mesenchymal stem cell-driven breast cancer malignancy

El-Haibi, C. P., Bell, G. W., Zhang, J., Collmann, A. Y., Wood, D. K., Scherber, C. M., Csizmadia, E., Mariani, O., Zhu, C., Campagne, A., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1206653109 · Cited by 218 · see citing works

A current view of perlecan in physiology and pathology: A mosaic of functions

Gubbiotti, M. A., Neill, T., & Iozzo, R. V. (2016) · Matrix Biology · doi:10.1016/j.matbio.2016.09.003 · Cited by 216 · see citing works

Heparanase: busy at the cell surface

Fux, L., Ilan, N., Sanderson, R. D., & Vlodavsky, I. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.06.005 · Cited by 215 · see citing works

Heparanase regulation of cancer, autophagy and inflammation: new mechanisms and targets for therapy

Sanderson, R. D., Elkin, M., Rapraeger, A. C., Ilan, N., & Vlodavsky, I. (2016) · FEBS Journal · doi:10.1111/febs.13932 · Cited by 212 · see citing works

Sulf-2: an extracellular modulator of cell signaling and a cancer target candidate

Rosen, S. D., & Lemjabbar‐Alaoui, H. (2010) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2010.504718 · Cited by 210 · see citing works

Sulfatase 2 up‐regulates glypican 3, promotes fibroblast growth factor signaling, and decreases survival in hepatocellular carcinoma†

Lai, J., Sandhu, D. S., Yu, C., et al. (2008) · Hepatology · doi:10.1002/hep.22202 · Cited by 209 · see citing works

Impaired Angiogenesis, Delayed Wound Healing and Retarded Tumor Growth in Perlecan Heparan Sulfate-Deficient Mice

Zhou, Z., Wang, J. M., Cao, R., Morita, H., Soininen, R., Chan, K. M., Liu, B., Cao, Y., & Tryggvason, K. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-0810 · Cited by 208 · see citing works

Expression of Heparanase in Normal, Dysplastic, and Neoplastic Human Colonic Mucosa and Stroma

Friedmann, Y., Vlodavsky, I., Aingorn, H., et al. (2000) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64632-9 · Cited by 203 · see citing works

Identification of GPC2 as an oncoprotein and candidate immunotherapeutic target in high-risk neuroblastoma

Bosse, K., Raman, P., Zhu, Z.-Y., Lane, M., Martinez, D., Heitzeneder, S., Rathi, K., Kendsersky, N. M., Randall, M. P., Donovan, L., et al. (2017) · Cancer Cell · doi:10.1016/j.ccell.2017.08.003 · Cited by 203 · see citing works

Heparan sulfate signaling in cancer

Knelson, E. H., Nee, J. C., & Blobe, G. C. (2014) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2014.03.001 · Cited by 198 · see citing works

Antisense targeting of perlecan blocks tumor growth and angiogenesis in vivo.

Sharma, B., Handler, M., Eichstetter, I., Whitelock, J. M., Nugent, M. A., & Iozzo, R. V. (1998) · Journal of Clinical Investigation · doi:10.1172/jci3793 · Cited by 194 · see citing works

First-in-Man Phase I Study of GC33, a Novel Recombinant Humanized Antibody Against Glypican-3, in Patients with Advanced Hepatocellular Carcinoma

Zhu, A. X., Gold, P. J., El-Khoueiry, A. B., Abrams, T. A., Morikawa, H., Ohishi, N., Ohtomo, T., & Philip, P. A. (2013) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-12-2616 · Cited by 193 · see citing works

Tinagl1 Suppresses Triple-Negative Breast Cancer Progression and Metastasis by Simultaneously Inhibiting Integrin/FAK and EGFR Signaling

Shen, M., Jiang, Y., Wei, Y., Ell, B. J., Sheng, X., Esposito, M., Kang, J., Hang, X., Zheng, H., Rowicki, M., et al. (2019) · Cancer Cell · doi:10.1016/j.ccell.2018.11.016 · Cited by 193 · see citing works

BMP-1/Tolloid-like Metalloproteases Process Endorepellin, the Angiostatic C-terminal Fragment of Perlecan

González, E. M., Reed, C. C., Bix, G. J., Fu, J., Zhang, Y., Gopalakrishnan, B., Greenspan, D. S., & Iozzo, R. V. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m409841200 · Cited by 191 · see citing works

Transactivation of Sphingosine 1-Phosphate Receptors Is Essential for Vascular Barrier Regulation

Singleton, P. A., Dudek, S. M., Ma, S.-F., & Garcia, J. G. N. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603680200 · Cited by 189 · see citing works

Glypican-1 modulates the angiogenic and metastatic potential of human and mouse cancer cells

Aikawa, T., Whipple, C. A., Lopez, M. E., Gunn, J. R., Young, A., Lander, A. D., & Korc, M. (2008) · Journal of Clinical Investigation · doi:10.1172/jci32412 · Cited by 188 · see citing works

Traversing the basement membrane in vivo: A diversity of strategies

Kelley, L. C., Lohmer, L. L., Hagedorn, E. J., & Sherwood, D. R. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201311112 · Cited by 183 · see citing works

Widespread expression of perlecan proteoglycan in basement membranes and extracellular matrices of human tissues as detected by a novel monoclonal antibody against domain III and by in situ hybridization.

Murdoch, A. D., Liu, B., Schwarting, R., et al. (1994) · Journal of Histochemistry & Cytochemistry · doi:10.1177/42.2.7507142 · Cited by 182 · see citing works

Structural characterization of human heparanase reveals insights into substrate recognition

Wu, L., Viola, C., Brzozowski, A. M., et al. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3136 · Cited by 174 · see citing works

Stromal Endothelial Cells Directly Influence Cancer Progression

Franses, J. W., Baker, A. B., Chitalia, V. C., & Edelman, E. R. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3001542 · Cited by 166 · see citing works

Membrane-Associated Heparan Sulfate Proteoglycans Are Involved in the Recognition of Cellular Targets by NKp30 and NKp46

Bloushtain, N., Qimron, U., Bar-Ilan, A., et al. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.173.4.2392 · Cited by 166 · see citing works

The C‐Terminal Domain V of Perlecan Promotes β1 Integrin‐Mediated Cell Adhesion, Binds Heparin, Nidogen and Fibulin‐2 and Can be Modified by Glycosaminoglycans

Brown, J. C., Sasaki, T., Göhring, W., Yamada, Y., & Timpl, R. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.t01-1-00039.x · Cited by 164 · see citing works

PG545, a dual heparanase and angiogenesis inhibitor, induces potent anti-tumour and anti-metastatic efficacy in preclinical models

Dredge, K. S., Hammond, E., Handley, P., Gonda, T. J., Smith, M. T., Vincent, C., Brandt, R., Ferro, V., & Bytheway, I. (2011) · British Journal of Cancer · doi:10.1038/bjc.2011.11 · Cited by 163 · see citing works

Not All Perlecans Are Created Equal

Knox, S. M., Merry, C. L. R., Stringer, S. E., Melrose, J., & Whitelock, J. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111826200 · Cited by 159 · see citing works

Border patrol: Insights into the unique role of perlecan/heparan sulfate proteoglycan 2 at cell and tissue borders

Farach-Carson, M. C., Warren, C. R., Harrington, D. A., & Carson, D. D. (2014) · Matrix Biology · doi:10.1016/j.matbio.2013.08.004 · Cited by 155 · see citing works

Age-Related Changes in HAPLN1 Increase Lymphatic Permeability and Affect Routes of Melanoma Metastasis

Ecker, B. L., Kaur, A., Douglass, S. M., Webster, M. R., Almeida, F. V., Marino, G. E., Sinnamon, A. J., Neuwirth, M. G., Alicea, G. M., Ndoye, A., et al. (2019) · Cancer Discovery · doi:10.1158/2159-8290.cd-18-0168 · Cited by 153 · see citing works

Amino acid determinants that drive heparan sulfate assembly in a proteoglycan.

Li, Z., & Esko, J. D. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32166-x · Cited by 152 · see citing works

The Protein Core of the Proteoglycan Perlecan Binds Specifically to Fibroblast Growth Factor-7

Mongiat, M., Taylor, K., Otto, J., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.10.7095 · Cited by 148 · see citing works

Tenascin C Induces Epithelial-Mesenchymal Transition–Like Change Accompanied by SRC Activation and Focal Adhesion Kinase Phosphorylation in Human Breast Cancer Cells

Nagaharu, K., Zhang, X., Yoshida, T., Katoh, D., Hanamura, N., Kozuka, Y., Ogawa, T., Shiraishi, T., & Imanaka‐Yoshida, K. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2010.10.015 · Cited by 143 · see citing works

Mapping of the binding of platelet‐derived growth factor to distinct domains of the basement membrane proteins BM‐40 and perlecan and distinction from the BM‐40 collagen‐binding epitope

Göhring, W., Sasaki, T., Heldin, C., et al. (1998) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1998.2550060.x · Cited by 139 · see citing works

Heparanase promotes growth, angiogenesis and survival of primary breast tumors

Cohen, I., Pappo, O., Elkin, M., San, T., Bar‐Shavit, R., Hazan, R. B., Peretz, T., Vlodavsky, I., & Abramovitch, R. (2005) · International Journal of Cancer · doi:10.1002/ijc.21552 · Cited by 135 · see citing works

Opposing Functions of Heparanase-1 and Heparanase-2 in Cancer Progression

Vlodavsky, I., Gross-Cohen, M., Weissmann, M., Ilan, N., & Sanderson, R. D. (2017) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2017.10.007 · Cited by 135 · see citing works

Perlecan and Tumor Angiogenesis

Jiang, X., & Couchman, J. (2003) · Journal of Histochemistry & Cytochemistry · doi:10.1177/002215540305101101 · Cited by 134 · see citing works

Novel aspects of glypican glycobiology

Fransson, L., Belting, M., Cheng, F., Jnsson, M., Mani, K., & Sandgren, S. (2004) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-3445-0 · Cited by 133 · see citing works

Altered proteoglycan gene expression and the tumor stroma

Iozzo, R. V., & COHEN, I. R. (1993) · Cellular and Molecular Life Sciences · doi:10.1007/bf01923588 · Cited by 133 · see citing works

The Role of Tissue Inhibitors of Metalloproteinases in Tumorigenesis and Metastasis

Cruz‐Muñoz, W., & Khokha, R. (2008) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408360801973244 · Cited by 132 · see citing works

Assembly, heterogeneity, and breaching of the basement membranes

Glentis, A., Gurchenkov, V., & Vignjevic, D. M. (2014) · Cell Adhesion & Migration · doi:10.4161/cam.28733 · Cited by 132 · see citing works

The role of vascular-derived perlecan in modulating cell adhesion, proliferation and growth factor signaling

Lord, M. S., Chuang, C. Y., Melrose, J., Davies, M. J., Iozzo, R. V., & Whitelock, J. M. (2014) · Matrix Biology · doi:10.1016/j.matbio.2014.01.016 · Cited by 130 · see citing works

Deregulation of hyaluronan synthesis, degradation and binding promotes breast cancer

Heldin, P., Basu, K., Olofsson, B., Porsch, H., Kozlova, I., & Kahata, K. (2013) · The Journal of Biochemistry · doi:10.1093/jb/mvt085 · Cited by 129 · see citing works

Heparan Sulfate Undergoes Specific Structural Changes during the Progression from Human Colon Adenoma to Carcinoma in Vitro

Jayson, G. C., Lyon, M., Paraskeva, C., Turnbull, J. E., Deakin, J. A., & Gallagher, J. T. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.1.51 · Cited by 129 · see citing works

ROCK signaling promotes collagen remodeling to facilitate invasive pancreatic ductal adenocarcinoma tumor cell growth

Rath, N., Morton, J. P., Julian, L., Helbig, L., Kadir, S. R., McGhee, E. J., Anderson, K. I., Kalna, G., Mullin, M., Pinho, A. V., et al. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201606743 · Cited by 125 · see citing works

6-O-Sulfation of Heparan Sulfate Differentially Regulates Various Fibroblast Growth Factor-dependent Signalings in Culture

Sugaya, N., Habuchi, H., Nagai, N., Ashikari‐Hada, S., & Kimata, K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m705948200 · Cited by 120 · see citing works

Abnormal expression of perlecan proteoglycan in metastatic melanomas.

COHEN, I. R., Murdoch, A. D., Naso, M. F., et al. (1994) · PubMed · Cited by 119 · see citing works

Identification of Sites in Domain I of Perlecan That Regulate Heparan Sulfate Synthesis

Dolan, M. A., Horchar, T., Rigatti, B. W., & Hassell, J. R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.7.4316 · Cited by 119 · see citing works

Phase I study of the heparanase inhibitor roneparstat: an innovative approach for ultiple myeloma therapy

Galli, M., Chatterjee, M., Grasso, M., et al. (2018) · Haematologica · doi:10.3324/haematol.2017.182865 · Cited by 118 · see citing works

Endorepellin, the Angiostatic Module of Perlecan, Interacts with Both the α2β1 Integrin and Vascular Endothelial Growth Factor Receptor 2 (VEGFR2)

Goyal, A. K., Pal, N., Concannon, M., Paul, M. R., Doran, M., Poluzzi, C., Sekiguchi, K., Whitelock, J. M., Neill, T., & Iozzo, R. V. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.243626 · Cited by 117 · see citing works

Heparanase: A Multitasking Protein Involved in Extracellular Matrix (ECM) Remodeling and Intracellular Events

Masola, V., Bellin, G., Gambaro, G., & Onisto, M. (2018) · Cells · doi:10.3390/cells7120236 · Cited by 117 · see citing works

Caspase-3 Activation Triggers Extracellular Cathepsin L Release and Endorepellin Proteolysis

Cailhier, J., Sirois, I., Laplante, P., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801164200 · Cited by 116 · see citing works

Levels of expression of endothelial markers specific to tumour-associated endothelial cells and their correlation with prognosis in patients with breast cancer

Davies, G., Cunnick, G. H., Mansel, R. E., Mason, M. D., & Jiang, W. G. (2004) · Clinical & Experimental Metastasis · doi:10.1023/b:clin.0000017168.83616.d0 · Cited by 116 · see citing works

Genetic alteration of endothelial heparan sulfate selectively inhibits tumor angiogenesis

Fuster, M. M., Wang, L., Castagnola, J., Sikora, L., Reddi, K., Lee, P. H. A., Radek, K. A., Schuksz, M., Bishop, J. R., Gallo, R. L., et al. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200610086 · Cited by 116 · see citing works

Heparanase-induced shedding of syndecan-1/CD138 in myeloma and endothelial cells activates VEGFR2 and an invasive phenotype: prevention by novel synstatins

Jung, O., Trapp‐Stamborski, V., Purushothaman, A., Jin, H., Wang, H., Sanderson, R. D., & Rapraeger, A. C. (2016) · Oncogenesis · doi:10.1038/oncsis.2016.5 · Cited by 116 · see citing works

The Tumor Suppressor Function of Human Sulfatase 1 (SULF1) in Carcinogenesis

Lai, J.-P., Sandhu, D. S., Shire, A. M., et al. (2008) · Journal of Gastrointestinal Cancer · doi:10.1007/s12029-009-9058-y · Cited by 115 · see citing works

Glycogene Expression Alterations Associated with Pancreatic Cancer Epithelial-Mesenchymal Transition in Complementary Model Systems

Maupin, K. A., Sinha, A., Eugster, E., Miller, J., Ross, J. T. D., Paulino, V. M., Keshamouni, V. G., Tran, N. L., Berens, M. E., Webb, C. P., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013002 · Cited by 113 · see citing works

Benzoxazole derivatives: design, synthesis and biological evaluation

Kakkar, S., Tahlan, S., Lim, S. M., et al. (2018) · Chemistry Central Journal · doi:10.1186/s13065-018-0459-5 · Cited by 110 · see citing works

Dysfunctional endothelial cells directly stimulate cancer inflammation and metastasis

Franses, J. W., Drosu, N. C., Gibson, W. J., Chitalia, V. C., & Edelman, E. R. (2013) · International Journal of Cancer · doi:10.1002/ijc.28146 · Cited by 109 · see citing works

Secreted Protein Acidic and Rich in Cysteine (SPARC) Mediates Metastatic Dormancy of Prostate Cancer in Bone

Sharma, S., Xing, F., Liu, Y., Wu, K., Said, N. A., Pochampally, R. R., Shiozawa, Y., Lin, H., Balaji, K. C., & Watabe, K. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.737379 · Cited by 108 · see citing works

Redirecting T Cells to Glypican-3 with 4-1BB Zeta Chimeric Antigen Receptors Results in Th1 Polarization and Potent Antitumor Activity

Li, W., Guo, L., Rathi, P., Marinova, E., Gao, X., Wu, M.-F., Liu, H., Dotti, G., Gottschalk, S. M., Metelitsa, L. S., et al. (2016) · Human Gene Therapy · doi:10.1089/hum.2016.025 · Cited by 107 · see citing works

Integrin α2β1 Is the Required Receptor for Endorepellin Angiostatic Activity

Woodall, B. P., Nyström, A., Iozzo, R. A., Eble, J. A., Niland, S., Krieg, T., Eckes, B., Pozzi, A., & Iozzo, R. V. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m708364200 · Cited by 106 · see citing works

Promoter methylation profiling of 30 genes in human malignant melanoma

Furuta, J., Umebayashi, Y., Miyamoto, K., et al. (2004) · Cancer Science · doi:10.1111/j.1349-7006.2004.tb03184.x · Cited by 106 · see citing works

Heparan sulfate sulfatase SULF2 regulates PDGFRα signaling and growth in human and mouse malignant glioma

Phillips, J. J., Huillard, E., Robinson, A. E., Ward, A., Lum, D. H., Polley, M. C., Rosen, S. D., Rowitch, D. H., & Werb, Z. (2012) · Journal of Clinical Investigation · doi:10.1172/jci58215 · Cited by 103 · see citing works

Soluble glypican 3 inhibits the growth of hepatocellular carcinoma in vitro and in vivo

Zittermann, S. I., Capurro, M., Shi, W., et al. (2009) · International Journal of Cancer · doi:10.1002/ijc.24941 · Cited by 103 · see citing works

Perlecan, a candidate gene for the CAPB locus, regulates prostate cancer cell growth via the Sonic Hedgehog pathway

Datta, M. W., Hernández, A., Schlicht, M. J., et al. (2006) · Molecular Cancer · doi:10.1186/1476-4598-5-9 · Cited by 101 · see citing works

Force-dependent breaching of the basement membrane

Chang, T. T., Thakar, D., & Weaver, V. M. (2016) · Matrix Biology · doi:10.1016/j.matbio.2016.12.005 · Cited by 100 · see citing works

Invadopodia promote proteolysis of a wide variety of extracellular matrix proteins

Kelly, T. J., Mueller, S. C., Yeh, Y., & Chen, W. (1994) · Journal of Cellular Physiology · doi:10.1002/jcp.1041580212 · Cited by 99 · see citing works

Organ-specific Sulfation Patterns of Heparan Sulfate Generated by Extracellular Sulfatases Sulf1 and Sulf2 in Mice

Nagamine, S., Tamba, M., Ishimine, H., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.290262 · Cited by 97 · see citing works

A Phase I Biological and Pharmacologic Study of the Heparanase Inhibitor PI-88 in Patients with Advanced Solid Tumors

Basche, M., Gustafson, D. L., Holden, S. N., et al. (2006) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-05-2423 · Cited by 97 · see citing works

The role of perlecan in arterial injury and angiogenesis

Segev, A. (2004) · Cardiovascular Research · doi:10.1016/j.cardiores.2004.03.028 · Cited by 97 · see citing works

A Phase I study of the novel immunomodulatory agent PG545 (pixatimod) in subjects with advanced solid tumours

Dredge, K. S., Brennan, T. V., Hammond, E., Lickliter, J. D., Lin, L., Bampton, D., Handley, P., Lankesheer, F., Morrish, G. A., Yang, Y., et al. (2018) · British Journal of Cancer · doi:10.1038/s41416-018-0006-0 · Cited by 97 · see citing works

T Cells Engineered to Express a T-Cell Receptor Specific for Glypican-3 to Recognize and Kill Hepatoma Cells In Vitro and in Mice

Dargel, C., Bassani‐Sternberg, M., Hasreiter, J., et al. (2015) · Gastroenterology · doi:10.1053/j.gastro.2015.05.055 · Cited by 96 · see citing works

Glypican-3-mediated oncogenesis involves the Insulin-like growth factor-signaling pathway

Cheng, W., Tseng, C.-J., Lin, T. T. C., et al. (2008) · Carcinogenesis · doi:10.1093/carcin/bgn091 · Cited by 94 · see citing works

Recent advances in understanding the complexities of metastasis

Chitty, J. L., Filipe, E. C., Lucas, M. C., Herrmann, D., Cox, T. R., & Timpson, P. (2018) · F1000Research · doi:10.12688/f1000research.15064.2 · Cited by 94 · see citing works

Nerve growth factor effects on human and mouse melanoma cell invasion and heparanase production

Marchetti, D., Menter, D., Li, J., et al. (1993) · International Journal of Cancer · doi:10.1002/ijc.2910550430 · Cited by 93 · see citing works

Hyaluronic Acid Binding Protein 2 Is a Novel Regulator of Vascular Integrity

Mambetsariev, N., Mirzapoiazova, T., Mambetsariev, B., et al. (2009) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.109.200451 · Cited by 91 · see citing works

Charting the unexplored extracellular matrix in cancer

Filipe, E. C., Chitty, J. L., & Cox, T. R. (2018) · International Journal of Experimental Pathology · doi:10.1111/iep.12269 · Cited by 91 · see citing works

Isolation and characterization of fibronectin-binding proteoglycan carrying both heparan sulfate and dermatan sulfate chains from human placenta.

Isemura, M., Sato, N., Yamaguchi, Y., et al. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47503-5 · Cited by 90 · see citing works

Proteolysis of extracellular matrix by invadopodiafacilitates human breast cancer cell invasion and ismediated by matrix metalloproteinases

Kelly, T. J., Yan, Y., Osborne, R. L., et al. (1998) · Clinical & Experimental Metastasis · doi:10.1023/a:1006538200886 · Cited by 88 · see citing works

Active and Tissue Inhibitor of Matrix Metalloproteinase-free Gelatinase B Accumulates within Human Microvascular Endothelial Vesicles

Nguyen, M., Arkell, J., & Jackson, C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.9.5400 · Cited by 88 · see citing works

High-molecular-weight hyaluronan is a novel inhibitor of pulmonary vascular leakiness

Singleton, P. A., Mirzapoiazova, T., Guo, Y., Sammani, S., Mambetsariev, N., Lennon, F. E., Moreno‐Vinasco, L., & Garcia, J. G. N. (2010) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00405.2009 · Cited by 88 · see citing works

Chemical Tumor Biology of Heparan Sulfate Proteoglycans

Raman, K., & Kuberan, B. (2010) · Current Chemical Biology · doi:10.2174/187231310790226206 · Cited by 86 · see citing works

Perlecan and Basement Membrane-Chondroitin Sulfate Proteoglycan (Bamacan) Are Two Basement Membrane Chondroitin/Dermatan Sulfate Proteoglycans in the Engelbreth-Holm-Swarm Tumor Matrix

Couchman, J., Kapoor, R., Sthanam, M., & Wu, R. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.16.9595 · Cited by 85 · see citing works

A role for perlecan in the suppression of growth and invasion in fibrosarcoma cells.

Mathiak, M., Yenisey, Ç., Grant, D. S., Sharma, B., & Iozzo, R. V. (1997) · PubMed · Cited by 84 · see citing works

Increased responsiveness of hypoxic endothelial cells to FGF2 is mediated by HIF-1α-dependent regulation of enzymes involved in synthesis of heparan sulfate FGF2-binding sites

Li, J., Shworak, N. W., & Simons, M. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.9.1951 · Cited by 82 · see citing works

Sulfated Glycosaminoglycans Control the Extracellular Trafficking and the Activity of the Metalloprotease Inhibitor TIMP-3

Troeberg, L., Lazenbatt, C., Anower-E-Khuda, M. F., Freeman, C. G., Federov, O., Habuchi, H., Habuchi, O., Kimata, K., & Nagase, H. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2014.07.014 · Cited by 79 · see citing works

Matrilysin/matrix metalloproteinase-7(MMP7) cleavage of perlecan/HSPG2 creates a molecular switch to alter prostate cancer cell behavior

Grindel, B. J., Martinez, J. R., Pennington, C. L., et al. (2014) · Matrix Biology · doi:10.1016/j.matbio.2014.04.005 · Cited by 78 · see citing works

Shift of syndecan-1 expression from epithelial to stromal cells during progression of solid tumours

Mennerich, D., Vogel, A., Klaman, I., et al. (2004) · European Journal of Cancer · doi:10.1016/j.ejca.2004.01.038 · Cited by 78 · see citing works

Decreasing the Metastatic Potential in Cancers - Targeting the Heparan Sulfate Proteoglycans

FJELDSTAD, K., & Kolset, S. O. (2005) · Current Drug Targets · doi:10.2174/1389450054863662 · Cited by 77 · see citing works

Furanyl-1,3-thiazol-2-yl and benzoxazol-5-yl acetic acid derivatives: novel classes of heparanase inhibitor

Courtney, S. M., Hay, P. A., Buck, R. T., et al. (2005) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2005.03.014 · Cited by 76 · see citing works

The Effects of Unfractionated Heparin on Survival in Patients with Malignancy – A Systematic Review

Hettiarachchi, R., Vink, R., Büller, H., et al. (1999) · Thrombosis and Haemostasis · doi:10.1055/s-0037-1614885 · Cited by 76 · see citing works

Modeling Tumor Microenvironment Complexity In Vitro: Spheroids as Physiologically Relevant Tumor Models and Strategies for Their Analysis

Shah, S., & D’Souza, G. G. M. (2025) · Cells · doi:10.3390/cells14100732 · Cited by 66 · see citing works

Multi-faceted substrate specificity of heparanase

Peterson, S. B., & Liu, J. (2013) · Matrix Biology · doi:10.1016/j.matbio.2013.02.006 · Cited by 77 · see citing works

Heparin, Heparan Sulfate and Heparanase in Cancer: Remedy for Metastasis?

Li, J. (2008) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/187152008783330824 · Cited by 46 · see citing works

Identification of Sites in Domain I of Perlecan That Regulate Heparan Sulfate Synthesis

Dolan, M. A., Horchar, T., Rigatti, B. W., & Hassell, J. R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.7.4316 · Cited by 119 · see citing works

Perlecan: a major IL‐2‐binding proteoglycan in murine spleen

Miller, J. D., Stevens, E. T., Smith, D. R., et al. (2007) · Immunology and Cell Biology · doi:10.1038/sj.icb.7100128 · Cited by 19 · see citing works

Reduction of anionic sites in the glomerular basement membrane by heparanase does not lead to proteinuria

van den Hoven, M. J., Wijnhoven, T. J. M., Li, J.-P., Zcharia, E., Dijkman, H. B. P. M., Wismans, R. G., Rops, A. L. W. M. M., Lensen, J. F. M., van den Heuvel, L. P., Kuppevelt, T. H. V., et al. (2007) · Kidney International · doi:10.1038/sj.ki.5002706 · Cited by 79 · see citing works