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Cell surface proteoglycan syndecan-1 mediates hepatocyte growth factor binding and promotes Met signaling in multiple myeloma
Open accessAbstract
Heparan sulfate proteoglycans (HSPGs) play a crucial role in growth regulation by assembling signaling complexes and presenting growth factors to their cognate receptors. Within the immune system, expression of the HSPG syndecan-1 (CD138) is characteristic of terminally differentiated B cells, ie, plasma cells, and their malignant counterpart, multiple myeloma (MM). This study explored the hypothesis that syndecan-1 might promote growth factor signaling and tumor growth in MM. For this purpose, the interaction was studied between syndecan-1 and hepatocyte growth factor (HGF), a putative paracrine and autocrine regulator of MM growth. The study demonstrates that syndecan-1 is capable of binding HGF and that this growth factor is indeed a potent stimulator of MM survival and proliferation. Importantly, the interaction of HGF with heparan sulfate moieties on syndecan-1 strongly promotes HGF-mediated signaling, resulting in enhanced activation of Met, the receptor tyrosine kinase for HGF. Moreover, HGF binding to syndecan-1 promotes activation of the phosphatidylinositol 3-kinase/protein kinase B and RAS/mitogen-activated protein kinase pathways, signaling routes that have been implicated in the regulation of cell survival and proliferation, respectively. These results identify syndecan-1 as a functional coreceptor for HGF that promotes HGF/Met signaling in MM cells, thus suggesting a novel function for syndecan-1 in MM tumorigenesis.
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“The HS chain of SDC1 has been shown to act as a co-receptor for growth factors, promoting the activation of several RTKs, such as EGFR, c-MET, FGFR, and IGF1R.29,30,31,32”
From Therapeutic targeting of syndecan-1 axis overcomes acquired resistance to KRAS-targeted therapy in gastrointestinal cancers (2025) · cites this paper as [30]
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Cites
Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
Datta, S. R., Dudek, H., Tao, X., Masters, S., Fu, H., Gotoh, Y., & Greenberg, M. E. (1997) · Cell · doi:10.1016/s0092-8674(00)80405-5 · Cited by 5,689
Functions of Cell Surface Heparan Sulfate Proteoglycans
Bernfield, M. R., Götte, M., Park, P. W., Reizes, O., Fitzgerald, M. L., Lincecum, J. M., & Zako, M. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.729 · Cited by 2,722
Yayon, A., Klagsbrun, M., Esko, J. D., Leder, P., & Ornitz, D. M. (1991) · Cell · doi:10.1016/0092-8674(91)90512-w · Cited by 2,440
Interleukin-3-Induced Phosphorylation of BAD Through the Protein Kinase Akt
Peso, L. D., González-Garcı́a, M., Page, C., Herrera, R., & Nuñez, G. (1997) · Science · doi:10.1126/science.278.5338.687 · Cited by 1,797
Schmidt, L. S., Duh, F.-M. C., Chen, F., Kishida, T., Glenn, G. M., Choyke, P. L., Scherer, S. W., Zhuang, Z., Lubensky, I. A., Dean, M. C., et al. (1997) · Nature Genetics · doi:10.1038/ng0597-68 · Cited by 1,517
Requirement of Heparan Sulfate for bFGF-Mediated Fibroblast Growth and Myoblast Differentiation
Rapraeger, A. C., Krufka, A., & Olwin, B. B. (1991) · Science · doi:10.1126/science.1646484 · Cited by 1,508
Ponzetto, C., Bardelli, A., Zhen, Z., Maina, F., Zonca, P. D., Giordano, S., Graziani, A., Panayotou, G., & Comoglio, P. M. (1994) · Cell · doi:10.1016/0092-8674(94)90318-2 · Cited by 994
Multiple Myeloma: Increasing Evidence for a Multistep Transformation Process
Hallek, M. J., Bergsagel, P. L., & Anderson, K. C. (1998) · Blood · doi:10.1182/blood.v91.1.3 · Cited by 750
Regulated Diversity of Heparan Sulfate*
Lindahl, U., Kusche-Gullberg, M., & Kjellén, L. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.39.24979 · Cited by 688
Ets transcription factors: nuclear effectors of the Ras–MAP-kinase signaling pathway
Wasylyk, B., Hagman, J. R., & Gutierrez‐Hartmann, A. (1998) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(98)01211-0 · Cited by 506
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Moreaux, J., Cremer, F. W., Reme, T. X., Raab, M. S., Mahtouk, K., Kaukel, P., Pantesco, V., Vos, J. D., Jourdan, É., Jauch, A. S., et al. (2005) · Blood · doi:10.1182/blood-2004-11-4512 · Cited by 259
Ritchie, J. P., Ramani, V. C., Ren, Y., Naggi, A., Torri, G., Casu, B., Penco, S., Pisano, C., Carminati, P., Tortoreto, M., et al. (2011) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-10-2476 · Cited by 252
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Tai, Y., Li, X., Breitkreutz, I., Song, W., Neri, P. E., Catley, L. P., Podar, K., Hideshima, T., Chauhan, D., Raje, N. S., et al. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-0190 · Cited by 237
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Ikeda, H., Hideshima, T., Fulciniti, M., Lutz, R. J., Yasui, H., Okawa, Y., Kiziltepe, T., Vallet, S., Pozzi, S., Santo, L., et al. (2009) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-2867 · Cited by 203
Hammond, E., Khurana, A., Shridhar, V., & Dredge, K. S. (2014) · Frontiers in Oncology · doi:10.3389/fonc.2014.00195 · Cited by 192
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Self-citationPurushothaman, A., Chen, L., Yang, Y., & Sanderson, R. D. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806266200 · Cited by 180
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Choi, Y., Chung, H., Jung, H., Couchman, J., & Oh, E. (2010) · Matrix Biology · doi:10.1016/j.matbio.2010.10.006 · Cited by 175
Ribatti, D., Nico, B., & Vacca, A. (2006) · Oncogene · doi:10.1038/sj.onc.1209456 · Cited by 175
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Wei, J., Hu, M., Huang, K., Lin, S., & Du, H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21175983 · Cited by 169
Standal, T., Abildgaard, N., Fagerli, U.-M., Stordal, B., Hjertner, Ø., Borset, M., & Sundan, A. (2007) · Blood · doi:10.1182/blood-2006-07-034884 · Cited by 167
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Tatsumi, R. (2009) · Animal Science Journal · doi:10.1111/j.1740-0929.2009.00712.x · Cited by 143
Maeda, T., Alexander, C. M., & Friedl, A. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-2439 · Cited by 141
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Mahtouk, K., Hose, D., Raynaud, P., Hundemer, M., Jourdan, M., Jourdan, É., Pantesco, V., Baudard, M., Vos, J. D., Larroque, M., et al. (2007) · Blood · doi:10.1182/blood-2006-08-043232 · Cited by 137
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Moreaux, J., Sprynski, A. C., Dillon, S. R., Mahtouk, K., Jourdan, M., Ythier, A., Moine, P., Robert, N., Jourdan, É., Rossi, J. F., et al. (2009) · European Journal Of Haematology · doi:10.1111/j.1600-0609.2009.01262.x · Cited by 119
Ramani, V. C., Yang, Y., Ren, Y., Li, N., & Sanderson, R. D. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.183277 · Cited by 115
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Götte, M., Kersting, C., Radke, I., Kiesel, L., & Wülfing, P. (2007) · Breast Cancer Research · doi:10.1186/bcr1641 · Cited by 110
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Mahtouk, K., Cremer, F. W., Rème, T., Jourdan, M., Baudard, M., Moreaux, J., Requirand, G., Fiol, G., De Vos, J., Moos, M., et al. (2006) · Oncogene · doi:10.1038/sj.onc.1209699 · Cited by 105
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Yamada, M., Sankoda, Y., Tatsumi, R., Mizunoya, W., Ikeuchi, Y., Sunagawa, K., & Allen, R. E. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.02.017 · Cited by 107
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Xie, M., & Li, J. (2018) · Cellular Signalling · doi:10.1016/j.cellsig.2018.11.022 · Cited by 96
Theocharis, A. D., Seidel, C., Børset, M., Dobra, K., Baykov, V., Labropoulou, V., Kanakis, I., Dalas, E., Karamanos, N. K., Sundan, A., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601061200 · Cited by 99
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Hov, H., Holt, R. U., Rø, T. B., Fagerli, U., Hjorth‐Hansen, H., Baykov, V., Christensen, J. G., Waage, A., Sundan, A., & Børset, M. (2004) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-04-0874 · Cited by 96
Akl, M. R., Nagpal, P., Ayoub, N. M., Prabhu, S. A., Gliksman, M., Tai, B., Hatipoglu, A., Goy, A. H., & Suh, K. S. (2015) · Oncotarget · doi:10.18632/oncotarget.4981 · Cited by 88
Andersen, N. F., Standal, T., Nielsen, J. L., Heickendorff, L., Børset, M., Sørensen, F. B., & Abildgaard, N. (2004) · British Journal of Haematology · doi:10.1111/j.1365-2141.2004.05299.x · Cited by 91
Tjin, E. P. M., Groen, R. W. J., Vogelzang, I., Derksen, P. W. B., Klok, M. D., Meijer, H. P., van Eeden, S., Pals, S. T., & Spaargaren, M. (2005) · Blood · doi:10.1182/blood-2005-05-1929 · Cited by 95
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Yamada, M., Tatsumi, R., Kikuiri, T., Okamoto, S., Nonoshita, S., Mizunoya, W., Ikeuchi, Y., Shimokawa, H., Sunagawa, K., & Allen, R. E. (2006) · Muscle & Nerve · doi:10.1002/mus.20601 · Cited by 87
Pakula, R., Melchior, A., Denys, A., Vanpouille, C., Mazurier, J., & Allain, F. (2007) · Glycobiology · doi:10.1093/glycob/cwm009 · Cited by 86
The heparan sulfate proteoglycan agrin modulates neurite outgrowth mediated by FGF-2.
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Bonuccelli, G., Casimiro, M. C., Sotgia, F., Wang, C., Liu, M., Katiyar, S., Zhou, J., Dew, E., Capozza, F., Daumer, K. M., et al. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2009.080648 · Cited by 86
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Sayyad, M. R., Puchalapalli, M., Vergara, N. G., Wangensteen, S. M., Moore, M., Mu, L., Edwards, C., Anderson, A., Kall, S. L., Sullivan, M. E., et al. (2019) · Breast Cancer Research and Treatment · doi:10.1007/s10549-019-05347-0 · Cited by 81
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Lopes, C. C., Dietrich, C. P., & Nader, H. B. (2006) · Brazilian Journal of Medical and Biological Research · doi:10.1590/s0100-879x2006000200001 · Cited by 78
Szatmári, T., & Dobra, K. (2013) · Frontiers in Oncology · doi:10.3389/fonc.2013.00310 · Cited by 90
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Reijmers, R. M., Groen, R. W. J., Rozemuller, H., Kuil, A., de Haan-Kramer, A., Csikós, T., Martens, A. C., Spaargaren, M., & Pals, S. T. (2009) · Blood · doi:10.1182/blood-2009-02-204396 · Cited by 81
Self-citationRangarajan, S., Richter, J. R., Richter, R. P., Bandari, S., Tripathi, K. K., Vlodavsky, I., & Sanderson, R. D. (2020) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155420937087 · Cited by 83
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Nikitovic, D., Berdiaki, A., Spyridaki, I., Krasanakis, T., Tsatsakis, A. M., & Tzanakakis, G. N. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00069 · Cited by 78
Tate, A. W., Isotani, S., Bradley, M. J., Sikes, R. A., Davis, R., Chung, L. W. K., & Edlund, M. (2006) · BMC Cancer · doi:10.1186/1471-2407-6-197 · Cited by 75
Munesue, S., Yoshitomi, Y., Kusano, Y., Koyama, Y., Nishiyama, A., Nakanishi, H., Miyazaki, K., Ishimaru, T., Miyaura, S., Okayama, M., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609812200 · Cited by 74
Gao, W., Kim, H., & Ho, M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0137664 · Cited by 74
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Bret, C., Hose, D., Reme, T. X., Sprynski, A. C., Mahtouk, K., Schved, J., Quittet, P., Rossi, J., Goldschmidt, H., & Klein, B. (2009) · British Journal of Haematology · doi:10.1111/j.1365-2141.2009.07633.x · Cited by 76
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Shida, D., Kitayama, J., Yamaguchi, H., Hama, K., Aoki, J., Arai, H., Yamashita, H., Mori, K., Sako, A., Konishi, T., et al. (2004) · Experimental Cell Research · doi:10.1016/j.yexcr.2004.08.008 · Cited by 71
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Taher, T. E. I., Tjin, E. P. M., Beuling, E. A., Borst, J. G., Spaargaren, M., & Pals, S. T. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.169.7.3793 · Cited by 68
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Watson, L. N., Mottershead, D. G., Dunning, K. R., Robker, R. L., Gilchrist, R. B., & Russell, D. L. (2012) · Endocrinology · doi:10.1210/en.2012-1181 · Cited by 64
Wang, Q., Yang, L., Alexander, C. M., & Temple, S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0042883 · Cited by 66
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Gordin, M., Tesio, M., Cohen, S., Gore, Y., Lantner, F., Leng, L., Bucala, R., & Shachar, I. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0902566 · Cited by 57
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Metadata
- Authors
- Derksen, P. W. B., Keehnen, R. M. J., Evers, L. M., van Oers, M. H. J., Spaargaren, M., & Pals, S. T.
- Affiliations
- Amsterdam UMC Location University of Amsterdam (NL)
- Venue
- Blood
- Publisher
- American Society of Hematology
- Published
- 2002-02-15
- Volume
- 99
- Issue
- 4
- Pages
- 1405-1410
- ISSN
- 0006-4971 (ISSN-L)
- 1528-0020
- OpenAlex
- W2009169267
- Cited by
- 274
- References
- 38
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 7 · 2023: 12 · 2022: 7 · 2021: 10 · 2020: 15 · 2019: 9 · 2018: 10 · 2017: 7 · 2016: 9 · 2015: 10 · 2014: 12 · 2013: 14 · 2012: 14
- FWCI
- 5.56
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Blood (publishedVersion)
- PubMed (publishedVersion)
- Pure Amsterdam UMC (publishedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Funders
- KWF Kankerbestrijding
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Health Sciences › Medicine › Hematology › Multiple Myeloma Research and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Keywords
- syndecan-1, hepatocyte growth factor, MET receptor tyrosine kinase, multiple myeloma, heparan sulfate proteoglycans, co-receptors, PI3K/Akt signaling, Ras/MEK/ERK signaling, cell proliferation and survival, tumor growth
- MeSH terms
- Cell Division, Enzyme Activation, Humans, Membrane Glycoproteins, Multiple Myeloma, Protein Binding, Proteoglycans, Proto-Oncogene Proteins, Transfection, Tumor Cells, Cultured, Signal Transduction, Hepatocyte Growth Factor, Protein Serine-Threonine Kinases, ras Proteins, Proto-Oncogene Proteins c-met, Phosphatidylinositol 3-Kinases, MAP Kinase Signaling System, Proto-Oncogene Proteins c-akt, Syndecans, Syndecan-1
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