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Tumor Microenvironment: Extracellular Matrix Alterations Influence Tumor Progression
Open accessAbstract
The tumor microenvironment (TME) is composed of various cell types embedded in an altered extracellular matrix (ECM). ECM not only serves as a support for tumor cell but also regulates cell-cell or cell-matrix cross-talks. Alterations in ECM may be induced by hypoxia and acidosis, by oxygen free radicals generated by infiltrating inflammatory cells or by tumor- or stromal cell-secreted proteases. A poorer diagnosis for patients is often associated with ECM alterations. Tumor ECM proteome, also named cancer matrisome, is strongly altered, and different ECM protein signatures may be defined to serve as prognostic biomarkers. Collagen network reorganization facilitates tumor cell invasion. Proteoglycan expression and location are modified in the TME and affect cell invasion and metastatic dissemination. ECM macromolecule degradation by proteases may induce the release of angiogenic growth factors but also the release of proteoglycan-derived or ECM protein fragments, named matrikines or matricryptins. This review will focus on current knowledge and new insights in ECM alterations, degradation, and reticulation through cross-linking enzymes and on the role of ECM fragments in the control of cancer progression and their potential use as biomarkers in cancer diagnosis and prognosis.
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“In advanced tumors, excessive ECM deposition leads to mechanical compression of adjacent blood and lymphatic vessels, resulting in elevated interstitial fluid pressure (IFP) [87].”
From Modeling Tumor Microenvironment Complexity In Vitro: Spheroids as Physiologically Relevant Tumor Models and Strategies for Their Analysis (2025) · cites this paper as [87]
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1 retracted
Sudhakar, A. (2005) · Journal of Clinical Investigation · doi:10.1172/jci24813 · Cited by 162
RetractedMicroenvironmental regulation of tumor progression and metastasis
Quail, D. F., & Joyce, J. A. (2013) · Nature Medicine · doi:10.1038/nm.3394 · Cited by 7,994
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
The biology and function of fibroblasts in cancer
Kalluri, R. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.73 · Cited by 4,366
Matrix Crosslinking Forces Tumor Progression by Enhancing Integrin Signaling
Levental, K. R., Yu, H., Kass, L., Lakins, J. N., Egeblad, M., Erler, J. T., Fong, S. F. T., Csiszar, K., Giaccia, A., Weninger, W., et al. (2009) · Cell · doi:10.1016/j.cell.2009.10.027 · Cited by 4,101
Microenvironmental regulation of metastasis
Joyce, J. A., & Pollard, J. W. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2618 · Cited by 3,684
Glypican-1 identifies cancer exosomes and detects early pancreatic cancer
Melo, S. A., Luecke, L. B., Kahlert, C., Fernandez, A. F., Gammon, S. T., Kaye, J., LeBleu, V. S., Mittendorf, E. A., Weitz, J., Rahbari, N., et al. (2015) · Nature · doi:10.1038/nature14581 · Cited by 2,880
The tumor microenvironment at a glance
Balkwill, F. R., Capasso, M., & Hagemann, T. (2012) · Journal of Cell Science · doi:10.1242/jcs.116392 · Cited by 1,857
Metabolic Interactions in the Tumor Microenvironment
Lyssiotis, C. A., & Kimmelman, A. C. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.06.003 · Cited by 853 · cited 1×
“By inducing specific gene expression, it alters the cellular metabolism, increasing glycolysis and lactate production (11, 12).”
BackgroundTumor-Associated Neutrophils: New Targets for Cancer Therapy
Gregory, A. D., & Houghton, A. M. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-2583 · Cited by 703
The extracellular matrix in tumor progression and metastasis
Eble, J. A., & Niland, S. (2019) · Clinical & Experimental Metastasis · doi:10.1007/s10585-019-09966-1 · Cited by 613
Therapeutic targeting of the tumor microenvironment
Joyce, J. A. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.05.024 · Cited by 598
Hamano, Y., Zeisberg, M., Sugimoto, H., Lively, J. C., Maeshima, Y., Yang, C., Hynes, R. O., Werb, Z., Sudhakar, A., & Kalluri, R. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00133-8 · Cited by 566
Size Matters: Molecular Weight Specificity of Hyaluronan Effects in Cell Biology
Cyphert, J. M., Trempus, C. S., & Garantziotis, S. (2015) · International Journal of Cell Biology · doi:10.1155/2015/563818 · Cited by 423
Glypican‐3: A promising biomarker for hepatocellular carcinoma diagnosis and treatment
Zhou, F., Shang, W., Yu, X., & Tian, J. (2017) · Medicinal Research Reviews · doi:10.1002/med.21455 · Cited by 401
Lai, X., Wang, M., McElyea, S. D., Sherman, S., House, M. G., & Korc, M. (2017) · Cancer Letters · doi:10.1016/j.canlet.2017.02.019 · Cited by 395
Proteoglycan Chemical Diversity Drives Multifunctional Cell Regulation and Therapeutics
Karamanos, N. K., Piperigkou, Z., Theocharis, A. D., Watanabe, H., Franchi, M., Baud, S., Brézillon, S., Götte, M., Passi, A. G., Vigetti, D., et al. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00354 · Cited by 380
Self-citationEndorepellin, a Novel Inhibitor of Angiogenesis Derived from the C Terminus of Perlecan
Mongiat, M., Sweeney, S. M., Antonio, J. D. S., Fu, J., & Iozzo, R. V. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210445200 · Cited by 341
The High and Low Molecular Weight Forms of Hyaluronan Have Distinct Effects on CD44 Clustering
Yang, C., Cao, M., Liu, H., He, Y., Xu, J., Du, Y., Liu, Y., Wang, W., Cui, L., Hu, J., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.349209 · Cited by 304
Sawada, Y., Yoshikawa, T., Nobuoka, D., Shirakawa, H., Kuronuma, T., Motomura, Y., Mizuno, S., Ishii, H., Nakachi, K., Konishi, M., et al. (2012) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-11-3044 · Cited by 302
Antiangiogenic Activity of Restin, NC10 Domain of Human Collagen XV: Comparison to Endostatin
Ramchandran, R., Dhanabal, M., Volk, R., Waterman, M. J. F., Segal, M. S., Lu, H. A. J., Knebelmann, B., & Sukhatme, V. P. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0248 · Cited by 290
Beauvais, D. M., Ell, B. J., McWhorter, A. R., & Rapraeger, A. C. (2009) · The Journal of Experimental Medicine · doi:10.1084/jem.20081278 · Cited by 290
Zhou, X., Yan, T., Huang, C., Xu, Z., Wang, L., Jiang, E., Wang, H., Yang, C., Liu, K., Shao, Z., et al. (2018) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-018-0911-3 · Cited by 287
ADAMTS Metalloproteases Generate Active Versican Fragments that Regulate Interdigital Web Regression
McCulloch, D. R., Nelson, C. M., Dixon, L. J., Silver, D. L., Wylie, J. D., Lindner, V., Sasaki, T., Cooley, M. A., Argraves, W. S., & Apte, S. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.09.008 · Cited by 258
Robinet, A., Fahem, A., Cauchard, J.-H., Huet, E., Vincent, L., Lorimier, S., Antonicelli, F., Soria, C., Crépin, M., Hornebeck, W., et al. (2005) · Journal of Cell Science · doi:10.1242/jcs.01613 · Cited by 256
Cancer Associated Fibroblasts: The Architects of Stroma Remodeling
Santi, A., Kugeratski, F. G., & Zanivan, S. R. (2017) · PROTEOMICS · doi:10.1002/pmic.201700167 · Cited by 251
Biophysics of tumor microenvironment and cancer metastasis – a mini review
Emon, B., Bauer, J., Jain, Y., Jung, B., & Saif, T. (2018) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2018.07.003 · Cited by 245
Procollagen II Amino Propeptide Processing by ADAMTS-3
Fernandes, R. J., Hirohata, S., Engle, J. M., Colige, A., Cohn, D. H., Eyre, D. R., & Apte, S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103466200 · Cited by 230
Two RGD-independent αvβ3 Integrin Binding Sites on Tumstatin Regulate Distinct Anti-tumor Properties
Maeshima, Y., Colorado, P. C., & Kalluri, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.c000186200 · Cited by 229
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 228
mTORC1 as a Regulator of Mitochondrial Functions and a Therapeutic Target in Cancer
de la Cruz-López, K. G., Toledo-Guzmán, M. E., Sánchez, E. O., & Carrancá, A. G. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.01373 · Cited by 223
Wickström, S. A., Alitalo, K. K., & Keski‐Oja, J. (2002) · PubMed · Cited by 207
Roles and targeting of the HAS/hyaluronan/CD44 molecular system in cancer
Karousou, E. G., Misra, S., Ghatak, S., Dobra, K., Götte, M., Vigetti, D., Passi, A. G., Karamanos, N. K., & Skandalis, S. S. (2016) · Matrix Biology · doi:10.1016/j.matbio.2016.10.001 · Cited by 204
Li, J., Chen, Y., Guo, X., Zhou, L., Jia, Z., Peng, Z., Tang, Y., Liu, W., Zhu, B., Wang, L., et al. (2017) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12941 · Cited by 194
Nandadasa, S., Foulcer, S. J., & Apte, S. (2014) · Matrix Biology · doi:10.1016/j.matbio.2014.01.005 · Cited by 187
Endostatin's emerging roles in angiogenesis, lymphangiogenesis, disease, and clinical applications
Walia, A., Yang, J., Huang, Y.-H., Rosenblatt, M. I., Chang, J., & Azar, D. T. (2015) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2015.09.007 · Cited by 184
Sawada, Y., Yoshikawa, T., Ofuji, K., Yoshimura, M., Tsuchiya, N., Takahashi, M., Nobuoka, D., Gotohda, N., Takahashi, S., Kato, Y., et al. (2016) · OncoImmunology · doi:10.1080/2162402x.2015.1129483 · Cited by 178
Glypican-1 is enriched in circulating-exosomes in pancreatic cancer and correlates with tumor burden
Frampton, A. E., Prado, M. M., López-Jiménez, E. A., Fajardo-Puerta, A. B., Jawad, Z., Lawton, P., Giovannetti, E., Habib, N., Castellano, L., Stebbing, J., et al. (2018) · Oncotarget · doi:10.18632/oncotarget.24873 · Cited by 171
The cancer matrisome: From comprehensive characterization to biomarker discovery
Socovich, A. M., & Naba, A. (2018) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2018.06.005 · Cited by 164
Laminin 332 processing impacts cellular behavior
Rousselle, P., & Beck, K. (2013) · Cell Adhesion & Migration · doi:10.4161/cam.23132 · Cited by 160
Magnon, C., Galaup, A., Mullan, B., Rouffiac, V., Bidart, J., Griscelli, F., Opolon, P., & Perricaudet, M. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-3536 · Cited by 152
Καραμάνου, Κ., Franchi, M., Vynios, D. H., & Brézillon, S. (2019) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2019.08.003 · Cited by 152
Self-citationImmunoregulatory roles of versican proteolysis in the myeloma microenvironment
Hope, C. L., Foulcer, S. J., Jagodinsky, J. C., Chen, S. X., Jensen, J. L., Patel, S., Leith, C. P., Maroulakou, I. G., Callander, N. S., Miyamoto, S., et al. (2016) · Blood · doi:10.1182/blood-2016-03-705780 · Cited by 147
Rebustini, I. T., Myers, C., Lassiter, K. S., Surmak, A. J., Szabova, L., Holmbeck, K., Pedchenko, V. K., Hudson, B. G., & Hoffman, M. P. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.07.016 · Cited by 146
Fragments generated upon extracellular matrix remodeling: Biological regulators and potential drugs
Ricard‐Blum, S., & Vallet, S. D. (2017) · Matrix Biology · doi:10.1016/j.matbio.2017.11.005 · Cited by 145
Role of hyaluronan in pancreatic cancer biology and therapy: Once again in the spotlight
Sato, N., Kohi, S., Hirata, K., & Goggins, M. (2016) · Cancer Science · doi:10.1111/cas.12913 · Cited by 142
Next-Generation Cancer Immunotherapy Targeting Glypican-3
Shimizu, Y., Suzuki, T., Yoshikawa, T., Endo, I., & Nakatsura, T. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.00248 · Cited by 139
Endostatin and endorepellin: A common route of action for similar angiostatic cancer avengers
Poluzzi, C., Iozzo, R. V., & Schaefer, L. (2015) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2015.10.012 · Cited by 134
Laminin-111-derived peptides and cancer
Kikkawa, Y., Hozumi, K., Katagiri, F., Nomizu, M., Kleinman, H. K., & Koblinski, J. E. (2013) · Cell Adhesion & Migration · doi:10.4161/cam.22827 · Cited by 132
Li, N., Wei, L., Liu, X., Bai, H., Ye, Y., Li, D., Li, N., Baxa, U., Wang, Q., Lv, L., et al. (2019) · Hepatology · doi:10.1002/hep.30646 · Cited by 130
The Tumor Microenvironment and Strategies to Improve Drug Distribution
Saggar, J. K., Yu, M., Tan, Q., & Tannock, I. F. (2013) · Frontiers in Oncology · doi:10.3389/fonc.2013.00154 · Cited by 129
Hamano, Y., & Kalluri, R. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.05.130 · Cited by 125
Pedchenko, V. K., Zent, R., & Hudson, B. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311901200 · Cited by 123
Syndecan-1 and Syndecan-4 Are Independent Indicators in Breast Carcinoma
Lendorf, M. E., Manon‐Jensen, T., Kronqvist, P., Multhaupt, H. A. B., & Couchman, J. (2011) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155411405057 · Cited by 123
Matrikines from basement membrane collagens: A new anti-cancer strategy
Monboisse, J., Oudart, J., Ramont, L., Brassart‐Pasco, S., & Maquart, F. X. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.12.029 · Cited by 121
Self-citationLu, H., Niu, F., Liu, F., Gao, J., Sun, Y., & Zhao, X. (2017) · Cancer Medicine · doi:10.1002/cam4.1064 · Cited by 119
The Role of Glypican-3 in Regulating Wnt, YAP, and Hedgehog in Liver Cancer
Kolluri, A., & Ho, M. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.00708 · Cited by 118
Hope, C. L., Emmerich, P. B., Papadas, A., Pagenkopf, A. C., Matkowskyj, K. A., Hey, D. R. V. D., Payne, S. N., Clipson, L. J., Callander, N. S., Hematti, P., et al. (2017) · The Journal of Immunology · doi:10.4049/jimmunol.1700529 · Cited by 117
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
Kehlet, S. N., Pamplona, R. S., Brix, S., Leeming, D. J., Karsdal, M. A., & Moreno, V. R. (2016) · Scientific Reports · doi:10.1038/srep30599 · Cited by 114
Pócza, P., Süli‐Vargha, H., Darvas, Z., & Falus, A. (2007) · International Journal of Cancer · doi:10.1002/ijc.23296 · Cited by 113
Heinz, A., Jung, M. C., Duca, L., Sippl, W., Taddese, S., Ihling, C. H., Rusciani, A., Jahreis, G., Weiss, A. S., Neubert, R. H. H., et al. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07616.x · Cited by 112
Brézillon, S., Pietraszek‐Gremplewicz, K., Maquart, F., & Wegrowski, Y. (2013) · FEBS Journal · doi:10.1111/febs.12210 · Cited by 107
Self-citationRapraeger, A. C. (2013) · FEBS Journal · doi:10.1111/febs.12160 · Cited by 104
Metastatin: a hyaluronan-binding complex from cartilage that inhibits tumor growth.
Liu, N., Lapcevich, R., Underhill, C. B., Han, Z., Gao, F., Swartz, G., Plum, S., Zhang, L., & Green, S. J. (2001) · PubMed · Cited by 101
Altered retinoblastoma protein expression in nonsmall cell lung cancer
Dosaka‐Akita, H., Hu, S., Fujino, M., Harada, M., Kinoshita, I., Xu, H., Kuzumaki, N., Kawakami, Y., & Benedict, W. F. (1997) · Cancer · doi:10.1002/(sici)1097-0142(19970401)79:7 · Cited by 97
Ntayi, C., Labrousse, A.-L., Debret, R., Birembaut, P., Bellon, G., Antonicelli, F. D., Hornebeck, W., & Bernard, P. (2004) · Journal of Investigative Dermatology · doi:10.1046/j.0022-202x.2004.22228.x · Cited by 95
Serum endostatin levels are elevated in patients with soft tissue sarcoma
Feldman, A. L., Pak, H., Yang, J. C., Alexander, H. R., & Libutti, S. K. (2001) · Cancer · doi:10.1002/1097-0142(20010415)91:8 · Cited by 92
Lumican inhibits cell migration through α2β1 integrin
Zeltz, C., Brézillon, S., Käpylä, J., Eble, J. A., Bobichon, H., Terryn, C., Perreau, C., Franz, C. M., Heino, J., Maquart, F., et al. (2010) · Experimental Cell Research · doi:10.1016/j.yexcr.2010.08.002 · Cited by 91
Self-citationRapraeger, A. C., Ell, B. J., Roy, M., Li, X., Morrison, O. R., Thomas, G. M., & Beauvais, D. M. (2013) · FEBS Journal · doi:10.1111/febs.12134 · Cited by 83
Floquet, N., Brassart‐Pasco, S., Ramont, L., Derreumaux, P., Laronze, J. Y., Nuzillard, J., Maquart, F. X., Alix, A. J. P., & Monboisse, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307736200 · Cited by 78
Self-citationLumican Binds ALK5 to Promote Epithelium Wound Healing
Yamanaka, O., Yuan, Y., Coulson‐Thomas, V. J., Gesteira, T. F., Call, M. K., Zhang, Y., Zhang, J., Chang, S., Xie, C., Liu, C., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0082730 · Cited by 77
Lumican: A new inhibitor of matrix metalloproteinase‐14 activity
Pietraszek‐Gremplewicz, K., Chatron-Colliet, A., Brézillon, S., Perreau, C., Jakubiak-Augustyn, A., Krotkiewski, H., Maquart, F., & Wegrowski, Y. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.09.040 · Cited by 77
Self-citationWang, H., Jin, H., & Rapraeger, A. C. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.679084 · Cited by 75
Chang, J. W., Kang, U., Kim, D., Yi, J. K., Lee, J. W., Noh, D., Lee, C., & Yu, M. (2007) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.200780049 · Cited by 75
The action of neutrophil serine proteases on elastin and its precursor
Heinz, A., Jung, M. C., Jahreis, G., Rusciani, A., Duca, L., Debelle, L., Weiss, A. S., Neubert, R. H. H., & Schmelzer, C. E. H. (2011) · Biochimie · doi:10.1016/j.biochi.2011.10.006 · Cited by 72
Douglass, S. M., Goyal, A. K., & Iozzo, R. V. (2015) · Connective Tissue Research · doi:10.3109/03008207.2015.1045297 · Cited by 71
Li, J., Li, B., Ren, C., Chen, Y., Guo, X., Zhou, L., Peng, Z., Tang, Y., Chen, Y., Liu, W., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.20516 · Cited by 71
Small leucine-rich proteoglycans and matrix metalloproteinase-14: Key partners?
Pietraszek‐Gremplewicz, K., Καραμάνου, Κ., Niang, A., Dauchez, M., Belloy, N., Maquart, F., Baud, S., & Brézillon, S. (2017) · Matrix Biology · doi:10.1016/j.matbio.2017.12.006 · Cited by 71
Self-citationWillumsen, N., Bager, C. L., Leeming, D. J., Smith, V., Karsdal, M. A., Dornan, D., & Bay‐Jensen, A. (2013) · BMC Cancer · doi:10.1186/1471-2407-13-554 · Cited by 70
Naboulsi, W., Megger, D. A., Bracht, T., Kohl, M., Turewicz, M., Eisenacher, M., Voss, D. M., Schlaak, J., Hoffmann, A.-C., Weber, F., et al. (2015) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b00420 · Cited by 70
Clinical Significance of Serum COL6A3 in Pancreatic Ductal Adenocarcinoma
Kang, C. Y., Wang, J., Axell‐House, D. B., Soni, P., Chu, M., Chipitsyna, G. I., Sarosiek, K., Sendecki, J. A., Hyslop, T., Zoubi, M. S. A., et al. (2013) · Journal of Gastrointestinal Surgery · doi:10.1007/s11605-013-2326-y · Cited by 67
Glypican-1 in exosomes as biomarker for early detection of pancreatic cancer.
Herreros‐Villanueva, M., & Bujanda, L. (2016) · Europe PMC (PubMed Central) · doi:10.3978/j.issn.2305-5839.2015.10.39 · Cited by 67
Tetrastatin, the NC1 Domain of the α4(IV) Collagen Chain: A Novel Potent Anti-Tumor Matrikine
Brassart‐Pasco, S., Sénéchal, K., Thévenard, J., Ramont, L., Devy, J., Stefano, L. D., Dupont-Deshorgue, A., Brézillon, S., Feru, J., Jazeron, J.-F., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0029587 · Cited by 66
Self-citationKaragiannis, E. D., & Popel, A. S. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.12.231 · Cited by 66
Targeting microenvironment in cancer therapeutics
Martin, M., Han, W., & Lu, T. (2016) · Oncotarget · doi:10.18632/oncotarget.9824 · Cited by 66
Proteoglycans regulate autophagy via outside-in signaling: an emerging new concept
Gubbiotti, M. A., & Iozzo, R. V. (2015) · Matrix Biology · doi:10.1016/j.matbio.2015.10.002 · Cited by 65
Lumican – Derived Peptides Inhibit Melanoma Cell Growth and Migration
Pietraszek‐Gremplewicz, K., Brézillon, S., Perreau, C., Malicka-Błaszkiewicz, M., Maquart, F., & Wegrowski, Y. (2013) · PLoS ONE · doi:10.1371/journal.pone.0076232 · Cited by 65
Self-citationCollagen degradation by superoxide anion in pulse and gamma radiolysis
Monboisse, J., Gardès-Albert, M., Randoux, A., Jp, B., & Ferradini, C. (1988) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(88)90147-x · Cited by 63
Self-citationArresten, a Collagen-Derived Angiogenesis Inhibitor, Suppresses Invasion of Squamous Cell Carcinoma
Aikio, M., Alahuhta, I., Nurmenniemi, S., Suojanen, J., Palovuori, R., Teppo, S., Sorsa, T. A., López-Otı́n, C., Pihlajaniemi, T. A., Salo, T. A., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0051044 · Cited by 61
Devy, J., Duca, L., Cantarelli, B., Joseph‐Pietras, D., Scandolera, A., Rusciani, A., Parent, L., Thévenard, J., Brassart‐Pasco, S., Tarpin, M., et al. (2010) · British Journal of Cancer · doi:10.1038/sj.bjc.6605926 · Cited by 61
Self-citationBrassart‐Pasco, S., Ramont, L., Ventéo, L., Pluot, M., Maquart, F., & Monboisse, J. (2004) · Experimental Cell Research · doi:10.1016/j.yexcr.2004.07.036 · Cited by 59
Self-citationElastokine-mediated up-regulation of MT1-MMP is triggered by nitric oxide in endothelial cells
Fahem, A., Robinet, A., Cauchard, J.-H., Duca, L., Soula-Rothhut, M., Rothhut, B., Soria, C., Guenounou, M., Hornebeck, W., & Bellon, G. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.11.022 · Cited by 59
Koskimaki, J. E., Karagiannis, E. D., Tang, B. C., Hammers, H. J., Watkins, D. N., Пили, Р., & Popel, A. S. (2010) · BMC Cancer · doi:10.1186/1471-2407-10-29 · Cited by 58
Elevated serum endostatin is associated with poor outcome in patients with non‐Hodgkin lymphoma
Bono, P., Teerenhovi, L. M., & Joensuu, H. (2003) · Cancer · doi:10.1002/cncr.11399 · Cited by 57
Hypoxic Signalling in Tumour Stroma
Laitala, A., & Erler, J. T. (2018) · Frontiers in Oncology · doi:10.3389/fonc.2018.00189 · Cited by 55
Kantola, T., Väyrynen, J. P., Klintrup, K., Mäkelä, J. T., Karppinen, S., Pihlajaniemi, T. A., Autio‐Harmainen, H., Karttunen, T. J., Mäkinen, M. J., & Tuomisto, A. (2014) · British Journal of Cancer · doi:10.1038/bjc.2014.456 · Cited by 55
Chida, S., Okayama, H., Noda, M., Saito, K., Nakajima, T., Aoto, K., Hayase, S., Momma, T., Ohki, S., Kono, K., et al. (2016) · Carcinogenesis · doi:10.1093/carcin/bgw069 · Cited by 54
Grahovac, J., & Wells, A. H. (2013) · Laboratory Investigation · doi:10.1038/labinvest.2013.132 · Cited by 53
Oudart, J., Doué, M., Vautrin, A., Brassart, B., Sellier, C., Dupont-Deshorgue, A., Monboisse, J., Maquart, F., Brassart‐Pasco, S., & Ramont, L. (2015) · Oncotarget · doi:10.18632/oncotarget.6399 · Cited by 52
Self-citationZeltz, C., Brézillon, S., Perreau, C., Ramont, L., Maquart, F., & Wegrowski, Y. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.08.012 · Cited by 50
Self-citationMundel, T. M., Yliniemi, A., Maeshima, Y., Sugimoto, H., Kieran, M. W., & Kalluri, R. (2007) · International Journal of Cancer · doi:10.1002/ijc.23269 · Cited by 49
Wang, Z., Bryan, J., Franz, C., Havlioglu, N., & Sandell, L. J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.118521 · Cited by 49
Suzuki, S., Sakata, J., Utsumi, F., Sekiya, R., Kajiyama, H., Shibata, K., Kikkawa, F., & Nakatsura, T. (2016) · OncoImmunology · doi:10.1080/2162402x.2016.1238542 · Cited by 49
Elastin Fragments Induce IL-1β Upregulation via NF-κB Pathway in Melanoma Cells
Debret, R., Naour, R. L., Sallenave, J., Dupont-Deshorgue, A., Hornebeck, W., Guenounou, M., Bernard, P., & Antonicelli, F. D. (2006) · Journal of Investigative Dermatology · doi:10.1038/sj.jid.5700337 · Cited by 48
Nobuoka, D., Yoshikawa, T., Takahashi, M., Iwama, T., Horie, K., Shimomura, M., Suzuki, S., Sakemura, N., Nakatsugawa, M., Sadamori, H., et al. (2012) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-012-1366-6 · Cited by 48
Cortes‐Dericks, L., & Schmid, R. A. (2017) · Respiratory Research · doi:10.1186/s12931-017-0546-5 · Cited by 47
Discovery and Validation of Novel Biomarkers for Detection of Epithelial Ovarian Cancer
Kulbe, H., Otto, R., Darb‐Esfahani, S., Lammert, H., Abobaker, S., Welsch, G., Chekerov, R., Schäfer, R., Dragun, D., Hummel, M., et al. (2019) · Cells · doi:10.3390/cells8070713 · Cited by 46
Endostatin: Current concepts about its biological role and mechanisms of action
Дигтярь, А. В., Pozdniakova, N. V., Feldman, N. B., Lutsenko, S. V., & Severin, E. S. (2007) · Biochemistry (Moscow) · doi:10.1134/s0006297907030017 · Cited by 46
Szarvas, T., László, V., Dorp, F. V., Reis, H., Szendrői, A., Romics, I., Derya Tilki, A., Rubben, H., & Ergün, S. (2011) · International Journal of Cancer · doi:10.1002/ijc.26343 · Cited by 46
A current perspective of canstatin, a fragment of type IV collagen alpha 2 chain
Okada, M., & Yamawaki, H. (2018) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2018.12.001 · Cited by 46
Endorepellin-evoked Autophagy Contributes to Angiostasis
Goyal, A., Gubbiotti, M. A., Chery, D. R., Han, L., & Iozzo, R. V. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.740266 · Cited by 44
Shen, Z., Yao, C., Wang, Z., Yue, L., Fang, Z., Yao, H., Feng, L., Zhao, H., Sun, Y.-J., Bian, X., et al. (2016) · Molecular Therapy · doi:10.1038/mt.2016.56 · Cited by 43
Lumican Peptides: Rational Design Targeting ALK5/TGFBRI
Gesteira, T. F., Coulson‐Thomas, V. J., Yuan, Y., Zhang, J., Nader, H. B., & Kao, W. W. ‐. (2017) · Scientific Reports · doi:10.1038/srep42057 · Cited by 43
Brassart, B., silva, J. D., Donet, M., Seurat, E., Hague, F., Terryn, C., Velard, F., Michel, J., Ouadid‐Ahidouch, H., Monboisse, J., et al. (2019) · British Journal of Cancer · doi:10.1038/s41416-019-0382-0 · Cited by 43
Self-citationAmbesi, A., & McKeown‐Longo, P. J. (2009) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-08-0195 · Cited by 42
Prognostic Value of ADAMTS Proteases and Their Substrates in Epithelial Ovarian Cancer
Lima, M. A., dos Santos, L., Turri, J. A. O., Nonogaki, S., Buim, M. E. C., Lima, J. F., Pinheiro, J. D. J. V., Osório, C. A. B. D. T., Soares, F. A., & Freitas, V. M. (2016) · Pathobiology · doi:10.1159/000446244 · Cited by 40
Tang, C., Liu, Y., Qin, H., Li, X., Guo, W., Li, J., Wang, W., Qu, L., Hu, H., Xu, C., et al. (2013) · Clinica Chimica Acta · doi:10.1016/j.cca.2013.09.011 · Cited by 38
Type XIX collagen: A new partner in the interactions between tumor cells and their microenvironment
Oudart, J., Monboisse, J., Maquart, F., Brassart, B., Brassart‐Pasco, S., & Ramont, L. (2016) · Matrix Biology · doi:10.1016/j.matbio.2016.07.010 · Cited by 38
Self-citationStatus of and prospects for cancer vaccines against hepatocellular carcinoma in clinical trials
Sun, Z., Zhu, Y., Xia, J., Sawakami, T., Kokudo, N., & Zhang, N. (2015) · BioScience Trends · doi:10.5582/bst.2015.01128 · Cited by 37
Nascimento, C. F., de Siqueira, A. S., Pinheiro, J. D. J. V., Freitas, V. M., & Jaeger, R. G. (2011) · Experimental Cell Research · doi:10.1016/j.yexcr.2011.08.022 · Cited by 37
Biomolecular analysis of matrix proteoglycans as biomarkers in non small cell lung cancer
Rangel, M. P., de Sá, V. K., Prieto, T. G., Martins, J. R. M., Olivieri, E. R., Carraro, D. M., Takagaki, T. Y., & Capelozzi, V. L. (2018) · Glycoconjugate Journal · doi:10.1007/s10719-018-9815-x · Cited by 37
Willumsen, N., Bager, C. L., & Karsdal, M. A. (2019) · Translational Oncology · doi:10.1016/j.tranon.2019.02.004 · Cited by 37
IKVAV regulates ERK1/2 and Akt signalling pathways in BMMSC population growth and proliferation
Li, B., Qiu, T., Zhang, P., Wang, X., Yin, Y., & Li, S. (2014) · Cell Proliferation · doi:10.1111/cpr.12094 · Cited by 36
Grindel, B. J., Li, Q., Arnold, R. S., Petros, J. A., Zayzafoon, M., Muldoon, M., Stave, J. W., Chung, L. W. K., & Farach‐Carson, M. C. (2016) · Oncotarget · doi:10.18632/oncotarget.7197 · Cited by 33
Nielsen, S. H., Willumsen, N., Brix, S., Sun, S., Manon‐Jensen, T., Karsdal, M. A., & Genovese, F. (2018) · Translational Oncology · doi:10.1016/j.tranon.2018.02.005 · Cited by 32
Hyaluronic acid-CD44 interactions promote BMP4/7-dependent Id1/3 expression in melanoma cells
Wu, R., Sedlmeier, G., Kyjacová, L., Schmaus, A., Philipp, J., Thiele, W., Garvalov, B. K., & Sleeman, J. P. (2018) · Scientific Reports · doi:10.1038/s41598-018-33337-7 · Cited by 32
Lambert, É., Fuselier, E., Ramont, L., Brassart, B., Dukic, S., Oudart, J., Dupont-Deshorgue, A., Sellier, C., Rodrigues, C. M., Dauchez, M., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-28003-x · Cited by 31
Self-citationLamstatin – a novel inhibitor of lymphangiogenesis derived from collagen IV
Weckmann, M., Moir, L. M., Heckman, C. A., Black, J. L., Oliver, B. G. G., & Burgess, J. K. (2012) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2012.01648.x · Cited by 30
Degradation of tropoelastin and skin elastin by neprilysin
Huertas, A. C. M., Schmelzer, C. E. H., Luise, C., Sippl, W., Pietzsch, M., Hoehenwarter, W., & Heinz, A. (2017) · Biochimie · doi:10.1016/j.biochi.2017.11.018 · Cited by 30
Hendaoui, I., Lavergne, E., Lee, H.-S., Hong, S. H., Kim, H.-Z., Parent, C., Heuzé‐Vourc'h, N., Clément, B., & Musso, O. C. (2012) · PLoS ONE · doi:10.1371/journal.pone.0030601 · Cited by 29
Li, Y., Li, J., Woo, P. Y. M., Shen, Z., Yao, H., Cai, Y., Lin, M. C.-M., & Poon, W. S. (2017) · BMC Cancer · doi:10.1186/s12885-017-3125-8 · Cited by 28
Metabolic adaptation to cancer growth: From the cell to the organism
Escoté, X., & Fajas, L. (2014) · Cancer Letters · doi:10.1016/j.canlet.2014.03.034 · Cited by 27
Structural and Antitumor Properties of the YSNSG Cyclopeptide Derived from Tumstatin
Thévenard, J., Floquet, N., Ramont, L., Prost, É., Nuzillard, J., Dauchez, M., Yezid, H., Alix, A. J. P., Maquart, F., Monboisse, J., et al. (2006) · Chemistry & Biology · doi:10.1016/j.chembiol.2006.10.007 · Cited by 27
Self-citationSaleh, M. E., Gadalla, R., Hassan, H., Afifi, A., Götte, M., El‐Shinawi, M., Mohamed, M. M., & Ibrahim, S. (2019) · PLoS ONE · doi:10.1371/journal.pone.0217550 · Cited by 26
Plasmin releases the anti-tumor peptide from the NC1 domain of collagen XIX
Oudart, J., Brassart‐Pasco, S., Vautrin, A., Sellier, C., Rodrigues, C. M., Dupont-Deshorgue, A., Brassart, B., Baud, S., Dauchez, M., Monboisse, J., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.2849 · Cited by 26
Self-citationAdamia, S., Pilarski, P. M., Belch, A. R., & Pilarski, L. M. (2013) · Current Cancer Drug Targets · doi:10.2174/1568009611313040001 · Cited by 26
Nabeya, Y., Shimada, H., Okazumi, S., Matsubara, H., Gunji, Y., Suzuki, T., & Ochiai, T. (2002) · Cancer · doi:10.1002/cncr.10267 · Cited by 26
Metwaly, H. A., El-Gayar, A. M., & El‐Shishtawy, M. M. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.06.007 · Cited by 26
Jung, O., Beauvais, D. M., Adams, K. M., & Rapraeger, A. C. (2019) · Journal of Cell Science · doi:10.1242/jcs.232645 · Cited by 24
Lu, Z., Jiao, D., Qiao, J., Yang, S., Yan, M., Cui, S., & Liu, Z. (2015) · Molecular Cancer · doi:10.1186/s12943-015-0370-9 · Cited by 24
Neill, T., Andreuzzi, E., Wang, Z., Peiper, S. C., Mongiat, M., & Iozzo, R. V. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.002934 · Cited by 23
Cathepsin S degrades arresten and canstatin in infarcted area after myocardial infarction in rats
Sugiyama, A., Mitsui, A., Okada, M., & Yamawaki, H. (2019) · Journal of Veterinary Medical Science · doi:10.1292/jvms.18-0674 · Cited by 22
Crystal Structure of the LG3 Domain of Endorepellin, an Angiogenesis Inhibitor
Le, B. V., Kim, H., Choi, J., Kim, J.-H., Hahn, M., Lee, C., Kim, K. K., & Hwang, H. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.09.048 · Cited by 20
Urinary laminin fragments as a tumour marker potentially reflecting basement membrane destruction
Katayama, M., Kamihagi, K., Hirai, S., Kurome, T., Murakami, K., Hino, F., & Kato, I. (1992) · British Journal of Cancer · doi:10.1038/bjc.1992.105 · Cited by 20
Non-invasive profiling of protease-specific elastin turnover in lung cancer: biomarker potential
Thorlacius‐Ussing, J., Kehlet, S. N., Rønnow, S. R., Karsdal, M. A., & Willumsen, N. (2018) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-018-2799-x · Cited by 20
Analysis of Syndecan-2 Methylation in Bowel Lavage Fluid for the Detection of Colorectal Neoplasm
Park, Y. S., Kim, D. S., Cho, S. W., Park, J. W., Jeon, S. J., Moon, T. J., Kim, S. H., Son, B. K., Oh, T. J., An, S., et al. (2018) · Gut and Liver · doi:10.5009/gnl17357 · Cited by 19
Iwama, T., Horie, K., Yoshikawa, T., Nobuoka, D., Shimomura, M., SAWADA, Y., & Nakatsura, T. (2013) · International Journal of Oncology · doi:10.3892/ijo.2013.1793 · Cited by 19
Laminin α5-derived peptides modulate the properties of metastatic breast tumour cells
Kusuma, N., Anderson, R. L., & Pouliot, N. (2011) · Clinical & Experimental Metastasis · doi:10.1007/s10585-011-9422-8 · Cited by 19
Tamiya, M., Kobayashi, M., Morimura, O., Yasue, T., Nakasuji, T., Satomu, M., Kohei, O., Shiroyama, T., Morishita, N., Suzuki, H., et al. (2012) · Clinical Lung Cancer · doi:10.1016/j.cllc.2012.03.012 · Cited by 17
Mo, H., Luo, D., Qiu, H.-Z., Liu, H., Chen, Q.-Y., Tang, L., Zhong, Z.-L., Huang, P., Zhao, Z.-J., Zhang, C., et al. (2013) · Clinical Oncology · doi:10.1016/j.clon.2012.11.009 · Cited by 17
You, R., Klein, R. M., Zheng, M., & McKeown‐Longo, P. J. (2009) · Matrix Biology · doi:10.1016/j.matbio.2009.01.003 · Cited by 17
Li, M., Liu, F., Sun, P., Gao, Y., Chen, H., Liu, H., Wang, M., Chen, J., & Zhao, Y.-A. (2012) · PubMed · doi:10.5754/hge10602 · Cited by 16
Elevated serum endostatin levels are associated with favorable outcome in acute myeloid leukemia
Aref, S., El-Sherbiny, M., Azmy, E., Goda, T., Selim, T. E., El-Refaie, M., & Twafik, E. (2008) · Hematology · doi:10.1179/102453308x315898 · Cited by 16
Xing, Y., Deng, P., & Xu, H. (2014) · Bioscience Reports · doi:10.1042/bsr20140012 · Cited by 15
Hwang‐Bo, J., Park, J., Bae, M. G., & Chung, I. S. (2016) · Cancer Medicine · doi:10.1002/cam4.866 · Cited by 15
Serum concentrations of laminin γ2 fragments in patients with head and neck squamous cell carcinoma
Kuratomi, Y., Satoh, S., Monji, M., Shimazu, R., Tanaka, G., Yokogawa, K., Inoue, A., Inokuchi, A., & Katayama, M. (2008) · Head & Neck · doi:10.1002/hed.20838 · Cited by 14
Novel functions for Type II procollagen
Sandell, L. J. (2014) · Connective Tissue Research · doi:10.3109/03008207.2013.867340 · Cited by 11
Liu, B., Zhao, Y. J., Yuan, J., Zeng, L., Sun, R., Meng, X., & Yang, S. (2017) · PLoS ONE · doi:10.1371/journal.pone.0187860 · Cited by 10
Jääskeläinen, A., Jukkola‐Vuorinen, A., Risteli, J., Haapasaari, K., & Karihtala, P. (2019) · Tumor Biology · doi:10.1177/1010428319847081 · Cited by 10
Serum laminin P1 in small cell lung cancer: a valuable indicator of distant metastasis?
Nakano, T., Iwahashi, N., Maeda, J., Hada, T., & Higashino, K. (1992) · British Journal of Cancer · doi:10.1038/bjc.1992.123 · Cited by 9
Farha, K. M. M. A., Menheere, P. P. C. A., Nieman, F. H. M., Janknegt, R. A., & Arends, J. W. (2010) · Urologia Internationalis · doi:10.1159/000282545 · Cited by 9
Syndecan-2 Methylation as a New Biomarker for Early Detection of Colorectal Neoplasm
Kim, J. H., & Park, S. C. (2018) · Gut and Liver · doi:10.5009/gnl18286 · Cited by 9
Jablonka, F., Alves, B. D. C. A., de Oliveira, C. G. B., Wroclawski, M. L., Szwarc, M., Vitória, W. D. O., Fonseca, F., & del Giglio, A. (2014) · Clinica Chimica Acta · doi:10.1016/j.cca.2014.06.025 · Cited by 8
Interaction of Restin with transcription factors
Wu, Y., Lü, F., Qi, Y.-X., Wang, R., Zhang, J., Lu, Z., & Zhao, Z. (2005) · Science in China Series C Life Sciences · doi:10.1007/bf03183619 · Cited by 5
Zhu, Y., Wu, H., & Liu, R. (2017) · Clinical Laboratory · doi:10.7754/clin.lab.2017.170217 · Cited by 5
Grindel, B. J., Li, Q., Arnold, R. S., Petros, J. A., Zayzafoon, M., Muldoon, M., Stave, J. W., Chung, L. W. K., & Farach‐Carson, M. C. (2016) · Oncotarget · doi:10.18632/oncotarget.11976 · Cited by 4
P135 Discovery and validation of novel biomarkers for detection of epithelial ovarian cancer
Kulbe, H., Otto, R., Darb‐Esfahani, S., Lammert, H., Abobaker, S., Welsch, G., Chekerov, R., Schäfer, R., Dragun, D., Hummel, M., et al. (2019) · International Journal of Gynecological Cancer · doi:10.1136/ijgc-2019-esgo.197 · Cited by 1
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Metadata
- Authors
- Brassart-Pasco, S., Brézillon, S., Brassart, B., Ramont, L., Oudart, J.-B., & Monboisse, J. C.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Venue
- Frontiers in Oncology
- Publisher
- Frontiers Media SA
- Published
- 2020-04-15
- Volume
- 10
- Pages
- 397-397
- ISSN
- 2234-943X (ISSN-L)
- PMC
- PMC7174611
- OpenAlex
- W3016553015
- Cited by
- 335
- References
- 168
- Citations by year
- 2026: 48 · 2025: 53 · 2024: 62 · 2023: 46 · 2022: 65 · 2021: 46 · 2020: 13
- FWCI
- 4.69
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Frontiers in Oncology (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- HAL (submittedVersion, other-oa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Centre National de la Recherche Scientifique (UMR 7369)
- Université de Reims Champagne-Ardenne
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
- Keywords
- tumor microenvironment, extracellular matrix, tumor progression, proteoglycans, matrikines, protease degradation, hypoxia, acidosis, cell invasion, metastasis, prognostic factors, angiogenesis
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