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DC-STAMP is essential for cell–cell fusion in osteoclasts and foreign body giant cells
Open accessAbstract
Osteoclasts are bone-resorbing cells that play a pivotal role in bone remodeling. Osteoclasts form large multinuclear giant cells by fusion of mononuclear osteoclasts. How cell fusion is mediated, however, is unclear. We identify the dendritic cell–specific transmembrane protein (DC-STAMP), a putative seven-transmembrane protein, by a DNA subtraction screen between multinuclear osteoclasts and mononuclear macrophages. DC-STAMP is highly expressed in osteoclasts but not in macrophages. DC-STAMP–deficient mice were generated, and osteoclast cell fusion was completely abrogated in homozygotes despite normal expression of osteoclast markers and cytoskeletal structure. As osteoclast multinucleation was restored by retroviral introduction of DC-STAMP, loss of cell fusion was directly attributable to a lack of DC-STAMP. Defects in osteoclast multinucleation reduce bone-resorbing activity, leading to osteopetrosis. Similar to osteoclasts, foreign body giant cell formation by macrophage cell fusion was also completely abrogated in DC-STAMP–deficient mice. We have thus identified an essential regulator of osteoclast and macrophage cell fusion, DC-STAMP, and an essential role of osteoclast multinucleation in bone homeostasis.
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“Macrophage fusion was completely abrogated in DC-STAMP deficient mice.[68]”
From Foreign body reaction to biomaterials (2008) · cites this paper as [68]
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“Dendritic cell-specific transmembrane protein (DC-STAMP) is necessary for fusion in the formation of FBGCs.”
From Foreign body reaction to biomaterials (2008) · cites this paper as [68]
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“NPBs induce osteoclasts to acquire a nonresorbing phenotype by inhibiting c-Src, which is essential for cytoskeletal construction,158 and by stimulating dendritic cell-specific transmembrane protein (DC-STAMP),159 which is necessary for cell fusion.”
From Bone remodeling: an operational process ensuring survival and bone mechanical competence (2022) · cites this paper as [159]
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Takayanagi, H., Kim, S., Koga, T., Nishina, H., Isshiki, M., Yoshida, H., Saiura, A., Isobe, M., Yokochi, T., Inoue, J.-I., et al. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00369-6 · Cited by 2,701
Yoshida, H., Hayashi, S.-I., Kunisada, T., Ogawa, M., Nishikawa, S., Okamura, H., Sudo, T., Shultz, L. D., & Nishikawa, S.-I. (1990) · Nature · doi:10.1038/345442a0 · Cited by 1,789
c-Fos: a Key Regulator of Osteoclast-Macrophage Lineage Determination and Bone Remodeling
Grigoriadis, A. E., Wang, Z., Cecchini, M. G., Hofstetter, W., Felix, R., Fleisch, H. A., & Wagner, E. F. (1994) · Science · doi:10.1126/science.7939685 · Cited by 1,264
ER–phagosome fusion defines an MHC class I cross-presentation compartment in dendritic cells
Guermonprez, P., Saveanu, L., Kleijmeer, M. J., Davoust, J. M., Endert, P. V., & Amigorena, S. (2003) · Nature · doi:10.1038/nature01911 · Cited by 753
Arai, F., Miyamoto, T., Ohneda, O., Inada, T., Sudo, T., Brasel, K., Miyata, T., Anderson, D. M., & Suda, T. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.190.12.1741 · Cited by 693
Self-citationNuclear Factor of Activated T-cells (NFAT) Rescues Osteoclastogenesis in Precursors Lacking c-Fos
Matsuo, K., Galson, D. L., Chen, Z., Peng, L., Laplace, C., Wang, K. Z. Q., Bachler, M. A., Amano, H., Aburatani, H., Ishikawa, H., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313973200 · Cited by 570
Requirement of pp60c-src expression for osteoclasts to form ruffled borders and resorb bone in mice.
Boyce, B. F., Yoneda, T., Lowe, C., Soriano, P. M., & Mundy, G. R. (1992) · Journal of Clinical Investigation · doi:10.1172/jci116032 · Cited by 553
RANKL-induced DC-STAMP Is Essential for Osteoclastogenesis
Kukita, T., Wada, N., Kukita, A., Kakimoto, T., Sandra, F., Toh, K., Nagata, K., Iijima, T., Horiuchi, M., Matsusaki, H., et al. (2004) · The Journal of Experimental Medicine · doi:10.1084/jem.20040518 · Cited by 357
(1995) · Europe PMC (PubMed Central) · Cited by 294
Bifurcation of osteoclasts and dendritic cells from common progenitors
Miyamoto, T. K., Ohneda, O., Arai, F., Iwamoto, K., Okada, S., Takagi, K., Anderson, D. M., & Suda, T. (2001) · Blood · doi:10.1182/blood.v98.8.2544 · Cited by 280
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Resolvin E1 regulates osteoclast fusion via DC‐STAMP and NFATc1
Zhu, M., Dyke, T. E. V., & Gyurko, R. (2013) · The FASEB Journal · doi:10.1096/fj.12-220228 · Cited by 62
Cao, Y., Jansen, I. D. C., Sprangers, S., Stap, J., Leenen, P. J. M., Everts, V. E., & de Vries, T. J. (2016) · Journal of Leukocyte Biology · doi:10.1189/jlb.1a1215-543r · Cited by 62
The unfolded protein response in skeletal development and homeostasis
Horiuchi, K., Tohmonda, T., & Morioka, H. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2178-1 · Cited by 62
Sakai, S., Takaishi, H., Matsuzaki, K., Kaneko, H., Furukawa, M., Miyauchi, Y., Shiraishi, A., Saito, K., Tanaka, A., Taniguchi, T., et al. (2009) · Journal of Bone and Mineral Metabolism · doi:10.1007/s00774-009-0084-4 · Cited by 61
Self-citationMolecular and Cellular Mechanisms of Mammalian Cell Fusion
Zhou, X., & Platt, J. L. (2011) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-0763-4_4 · Cited by 60
Groß, C., Weber, M., Creutzburg, K., Möbius, P., Preidl, R. H. M., Amann, K., & Wehrhan, F. (2017) · Journal of Translational Medicine · doi:10.1186/s12967-017-1230-8 · Cited by 63
Vignery, A. (2008) · Methods in molecular biology · doi:10.1007/978-1-59745-250-2_9 · Cited by 59
Kang, H., Viollet, B., & Wu, D. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.430389 · Cited by 60
Regulation of osteoclastogenesis by ganoderic acid DM isolated from Ganoderma lucidum
Miyamoto, I., Liu, J., Shimizu, K., Sato, M., Kukita, A., Kukita, T., & Kondo, R. (2008) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2008.11.005 · Cited by 58
BMP9 Reduces Bone Loss in Ovariectomized Mice by Dual Regulation of Bone Remodeling
Zhou, Y., Yang, Y., Jing, Y., Yuan, T.-J., Sun, L., Tao, B., Liu, J., & Zhao, H. (2020) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.3957 · Cited by 59
Sotillo, J. E., Mansky, K. C., Jensen, E. D., Carlson, A. E., Schwarz, T. M., Pham, L., MacKenzie, B., Prasad, H., Rohrer, M. D., Petryk, A., et al. (2009) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.090507 · Cited by 62
Choi, J., Choi, S. Y., Lee, S. Y., Lee, S. W., Kim, H. S., Lee, S. Y., & Lee, N. K. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.02.015 · Cited by 59
The elementary fusion modalities of osteoclasts
Søe, K., Hobolt-Pedersen, A.-S., & Delaissé, J. (2014) · Bone · doi:10.1016/j.bone.2014.12.010 · Cited by 57
Chung, P. Y. J., Beyens, G., Boonen, S., Papapoulos, S. E., Geusens, P., Karperien, M., Vanhoenacker, F. M. H. M., Verbruggen, L., Fransén, E., Offel, J. V., et al. (2010) · Human Genetics · doi:10.1007/s00439-010-0888-2 · Cited by 57
Skokos, E. A., Charokopos, A., Khan, K., Wanjala, J., & Kyriakides, T. R. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2011.01.045 · Cited by 55
Strawberry notch homologue 2 regulates osteoclast fusion by enhancing the expression of DC-STAMP
Maruyama, K., Uematsu, S., Kondo, T., Takeuchi, O., Martino, M. M., Kawasaki, T., & Akira, S. (2013) · The Journal of Experimental Medicine · doi:10.1084/jem.20130512 · Cited by 56
Ohyama, Y., Ito, J., Kitano, V. J. F., Shimada, J., & Hakeda, Y. (2018) · PLoS ONE · doi:10.1371/journal.pone.0191192 · Cited by 57
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Iwasaki, R., Ninomiya, K., Miyamoto, K., Suzuki, T., Sato, Y., Kawana, H., Nakagawa, T., Suda, T., & Miyamoto, T. K. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.10.076 · Cited by 57
Self-citationChen, I., Wang, L., Jiang, X., Aguila, H. L., & Reichenberger, E. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq541 · Cited by 56
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Ralston, S. H., & Albagha, O. (2012) · Elsevier eBooks · doi:10.1007/s11914-014-0219-y · Cited by 56
Søe, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21207717 · Cited by 62
Nomura, M., Yoshimura, Y., Kikuiri, T., Hasegawa, T., Taniguchi, Y., Deyama, Y., Koshiro, K., Sano, H., Suzuki, K., & Inoue, N. (2011) · Journal of Pharmacological Sciences · doi:10.1254/jphs.11099fp · Cited by 54
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Oursler, M. J. (2010) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22640 · Cited by 54
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Stattin, E., Henning, P., Klar, J., McDermott, E., STECKSÉN‐BLICKS, C., Sandström, P., Kellgren, T. G., Rydén, P., Hallmans, G., Lönnerholm, T., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-02533-2 · Cited by 54
Yu, M., Qi, X., Moreno, J. L., Färber, D. L., & Keegan, A. D. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1002628 · Cited by 53
Lemaire, I. B., Falzoni, S., Zhang, B., Pellegatti, P., & Virgilio, F. D. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1002780 · Cited by 53
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Kanagawa, H., Masuyama, R., Morita, M., Sato, Y., Niki, Y., Kobayashi, T., Katsuyama, E., Fujie, A., Wu, H., Tando, T., et al. (2015) · Journal of Bone and Mineral Metabolism · doi:10.1007/s00774-015-0702-2 · Cited by 52
Self-citationTakegahara, N., Kim, H., Mizuno, H., Sakaue-Sawano, A., Miyawaki, A., Tomura, M., Kanagawa, O., Ishii, M., & Choi, Y. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.677427 · Cited by 54
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Go, M., Shin, E.-J., Jang, S. Y., Nam, M., Hwang, G., & Lee, S. Y. (2022) · Experimental & Molecular Medicine · doi:10.1038/s12276-022-00775-3 · Cited by 50
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Gennari, L., Rendina, D., Merlotti, D., Cavati, G., Mingiano, C., Cosso, R., Materozzi, M., Pirrotta, F., Abate, V., Calabrese, M., et al. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.932065 · Cited by 56
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Morissette, M. C., Lamontagne, M., Bérubé, J., Gaschler, G. J., Williams, A., Yauk, C. L., Couture, C., Laviolette, M., Hogg, J. C., Timens, W., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0092498 · Cited by 51
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Otero, J. E., Dai, S., Foglia, D., Alhawagri, M., Vacher, J., Pasparakis, M., & Abu‐Amer, Y. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800434200 · Cited by 51
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Takito, J., & Nakamura, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186629 · Cited by 50
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Verma, S. K., Leikina, E., Melikov, K., & Chernomordik, L. (2014) · Biochemical Journal · doi:10.1042/bj20141233 · Cited by 50
Park, H.-J., Son, H.-J., Sul, O., Suh, J., & Choi, H. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2018.02.019 · Cited by 48
Molecular signaling in bone cells: Regulation of cell differentiation and survival
Plotkin, L. I., & Bruzzaniti, A. (2019) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2019.01.002 · Cited by 50
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Ninomiya, K., Miyamoto, T. K., Imai, J., Fujita, N., Suzuki, T., Iwasaki, R., Yagi, M., Watanabe, S., Toyama, Y., & Suda, T. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.07.193 · Cited by 52
Self-citationSøe, K., Delaisse, J.-M., & Borggaard, X. G. (2021) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2020.05.016 · Cited by 49
Arriero, M. D. M., Ramis, J. M., Perelló, J., & Monjo, M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0043187 · Cited by 49
Courtial, N., Smink, J. J., Kuvardina, O. N., Leutz, A., Göthert, J. R., & Lausen, J. (2011) · The FASEB Journal · doi:10.1096/fj.11-190850 · Cited by 50
Abdelmagid, S. M., Sondag, G. R., Moussa, F. M., Belcher, J., Yu, B., Stinnett, H., Novak, K. M., Mbimba, T., Khol, M., Hankenson, K. D., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.624270 · Cited by 49
Møller, A. M. J., Delaissé, J., Olesen, J. B., do Canto, L. M., Rogatto, S. R., Madsen, J. S., & Søe, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176368 · Cited by 51
Choi, S., Son, Y., Yun, J., & Kim, S. H. (2012) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2012/810563 · Cited by 48
Leung, R., Cuddy, K., Wang, Y., Rommens, J. M., & Glogauer, M. (2010) · Blood · doi:10.1182/blood-2010-05-282574 · Cited by 49
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Yang, J., Tang, R., Jin, Y., Chen, Y., Li, X., Yu, T., & Fei, J. (2019) · The FASEB Journal · doi:10.1096/fj.201802172r · Cited by 48
Ishii, T., Ruiz‐Torruella, M., Ikeda, A., Shindo, S., Movilă, A., Mawardi, H. H., Albassam, A., Kayal, R. A., Al-Dharrab, A. A., Egashira, K., et al. (2018) · The FASEB Journal · doi:10.1096/fj.201701424r · Cited by 47
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de Vries, T. J., Schoenmaker, T., Aerts, D., Grevers, L. C., de Souza, P. C., Nazmi, K., van de Wiel, M. A., Ylstra, B., van Lent, P. L., Leenen, P. J. M., et al. (2014) · Journal of Cellular Physiology · doi:10.1002/jcp.24702 · Cited by 49
Xu, J., Yue, F., Wang, J., Chen, L., & QI, W. (2014) · Molecular Medicine Reports · doi:10.3892/mmr.2014.2807 · Cited by 47
Osteoblast-specific Angiopoietin 1 overexpression increases bone mass
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Clinical and Genetic Advances in Paget’s Disease of Bone: a Review
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Kulkarni, R. N., Voglewede, P. A., & Liu, D. (2013) · Bone · doi:10.1016/j.bone.2013.08.020 · Cited by 44
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Cicek, M., Vrabel, A. M., Sturchio, C., Pederson, L. G., Hawse, J. R., Subramaniam, M., Spelsberg, T. C., & Oursler, M. J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017522 · Cited by 45
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Remen, K. M. R., Henning, P., Lerner, U. H., Gustafsson, J.-Α., & Andersson, G. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.235937 · Cited by 44
Maruyama, K., Kawagoe, T., Kondo, T., Akira, S., & Takeuchi, O. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.347799 · Cited by 44
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Zhao, H., Zhang, J., Shao, H., Liu, J., Jin, M., Chen, J., & Huang, Y. (2017) · Molecules and Cells · doi:10.14348/molcells.2017.2303 · Cited by 45
Ha, B. G., Hong, J. M., Park, J. Y., Ha, M., Kim, T., Cho, J., Ryoo, H., Choi, J., Shin, H., Chun, S. Y., et al. (2008) · PROTEOMICS · doi:10.1002/pmic.200701192 · Cited by 45
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Nakashima, Y., & Haneji, T. (2013) · PLoS ONE · doi:10.1371/journal.pone.0072033 · Cited by 42
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Takito, J., Nakamura, M., Yoda, M., Tohmonda, T., Uchikawa, S., Horiuchi, K., Toyama, Y., & Chiba, K. (2012) · Journal of Cell Science · doi:10.1242/jcs.090886 · Cited by 45
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Metadata
- Authors
- Yagi, M., Miyamoto, T., Sawatani, Y., Iwamoto, K., Hosogane, N., Fujita, N., Morita, K., Ninomiya, K., Suzuki, T., Miyamoto, K., Oike, Y., Takeya, M., Toyama, Y., & Suda, T.
- Affiliations
- Keio University (JP)
- Kumamoto University (JP)
- Kyushu University (JP)
- 1Department of Cell Differentiation, The Sakaguchi Laboratory
- ORCID
- Venue
- The Journal of Experimental Medicine
- Publisher
- Rockefeller University Press
- Published
- 2005-08-01
- Volume
- 202
- Issue
- 3
- Pages
- 345-351
- ISSN
- 0022-1007 (ISSN-L)
- 1540-9538
- PMC
- PMC2213087
- OpenAlex
- W2111239144
- Cited by
- 890
- References
- 24
- Citations by year
- 2026: 36 · 2025: 35 · 2024: 33 · 2023: 36 · 2022: 56 · 2021: 48 · 2020: 60 · 2019: 39 · 2018: 40 · 2017: 52 · 2016: 48 · 2015: 48 · 2014: 50 · 2013: 37 · 2012: 46
- FWCI
- 11.80
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Experimental Medicine (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bone Metabolism and Diseases
- Life Sciences › Immunology and Microbiology › Immunology › Phagocytosis and Immune Regulation
- Health Sciences › Medicine › Rheumatology › Osteomyelitis and Bone Disorders Research
- Keywords
- DC-STAMP, cell fusion, osteoclasts, foreign body giant cells, multinucleation, osteoclastogenesis, bone resorption, osteopetrosis, macrophages, bone homeostasis, seven-transmembrane proteins
- MeSH terms
- Animals, Bone and Bones, Bone Resorption, Cell Fusion, Homeostasis, Macrophages, Membrane Proteins, Nerve Tissue Proteins, Osteoclasts, Giant Cells, Mice, Knockout, Mice
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