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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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Research works printed but not linked: 1
- 1995, Am. J. Pathol., 147, 1487
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Items 401–500 of 892
Mullin, B. H., Zhu, K., Brown, S. J., Mullin, S., Tickner, J. C., Pavlos, N. J., Dudbridge, F., Xu, J., Walsh, J. P., & Wilson, S. G. (2019) · Scientific Reports · doi:10.1038/s41598-018-37609-0 · Cited by 26
A trans-eQTL network regulates osteoclast multinucleation and bone mass
Pereira, M., Ko, J., Logan, J. G., Protheroe, H., Kim, K., Tan, A. L. M., Croucher, P. I., Park, K.-S., Rotival, M., Petretto, E. G., et al. (2020) · eLife · doi:10.7554/elife.55549 · Cited by 28
Dionisio-Santos, D. A., Karaahmet, B., Belcher, E. K., Owlett, L. D., Trojanczyk, L., Olschowka, J. A., & O’Banion, M. K. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.758677 · Cited by 27
The Actin Binding Protein Adseverin Regulates Osteoclastogenesis
Hassanpour, S., Jiang, H., Wang, Y., Kuiper, J. W., & Glogauer, M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0109078 · Cited by 26
ATP6v0d2 deficiency increases bone mass, but does not influence ovariectomy-induced bone loss
Kim, T. S., Ha, H., Kim, N., Park, E., Rho, J., Kim, E. C., Lorenzo, J., Choi, Y., & Lee, S. H. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.10.117 · Cited by 26
Genetic deficiency of Wnt5a diminishes disease severity in a murine model of rheumatoid arthritis
MacLauchlan, S., Zuriaga, M. A., Fuster, J. J., Cuda, C. M., Jonason, J. H., Behzadi, F., Parker, J., Haines, G. K., Aprahamian, T. R., Perlman, H., et al. (2017) · Arthritis Research & Therapy · doi:10.1186/s13075-017-1375-0 · Cited by 26
Pata, M., & Vacher, J. (2018) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.3378 · Cited by 27
Wilson, L. D., Obakpolor, O. A., Jones, A. M., Richie, A. L., Mieczkowski, B. D., Fall, G. T., Hall, R. W., Rumbley, J. N., & Kroft, T. L. (2018) · Molecular Reproduction and Development · doi:10.1002/mrd.22992 · Cited by 26
Kim, B. H., Oh, J., & Lee, N. K. (2017) · Molecules and Cells · doi:10.14348/molcells.2017.0098 · Cited by 26
Queval, C. J., Fearns, A., Botella, L., Smyth, A., Schnettger, L., Mitermite, M., Wooff, E. E., Villarreal‐Ramos, B., García‐Jiménez, W., Heunis, T. D. J., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009410 · Cited by 26
Cutting Edge: MicroRNA Regulation of Macrophage Fusion into Multinucleated Giant Cells
Sissons, J. R., Peschon, J. J., Schmitz, F., Suen, R., Gilchrist, M., & Aderem, A. A. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1102477 · Cited by 25
Jeong, S., Lee, S., Kim, K., Lee, Y., Lee, J., Oh, S., Choi, J., Kim, S. W., Hwang, K., & Lim, S. (2020) · Molecules · doi:10.3390/molecules25173908 · Cited by 25
Moradifard, S., Hoseinbeyki, M., Emam, M. M., Parchiniparchin, F., & Ebrahimi‐Rad, M. (2020) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2020.108339 · Cited by 24
Programmed cell fusion in development and homeostasis
Iosilevskii, Y., & Podbilewicz, B. (2021) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2020.12.013 · Cited by 25
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Huang, Z., Luo, R., Yang, L., Chen, H., Zhang, X., Han, J., Wang, H., Zhou, Z., Wang, Z., & Shao, L. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.838664 · Cited by 30
Ihn, H. J., Lee, D., Lee, T., Shin, H., Bae, Y. C., Kim, S., & Park, E. K. (2015) · Experimental Biology and Medicine · doi:10.1177/1535370215576310 · Cited by 25
Kim, H., Kim, K., Yeon, J., Kim, S. H., Won, D. H., Choi, H., Nam, S., Son, Y., & Kang, H. (2014) · Marine Drugs · doi:10.3390/md12042054 · Cited by 25
Heusschen, R., Muller, J., Binsfeld, M., Marty, C., Plougonven, E., Dubois, S., Mahli, N., Moermans, K., Carmeliet, G., Léonard, A., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.8750 · Cited by 25
Anderson, J. M. (2009) · Springer eBooks · doi:10.1007/978-0-387-98161-1_11 · Cited by 25
Choi, Y.-J., Yoo, J. H., Lee, J., Lee, Y., Bae, M., Kim, Y., & Kim, H. J. (2020) · International Journal of Medical Sciences · doi:10.7150/ijms.41075 · Cited by 25
MicroRNA-mediated immune modulation as a therapeutic strategy in host-implant integration
Ong, S., Biswas, S. K., & Wong, S. C. (2015) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2015.05.013 · Cited by 25
Osteoclasts, no longer osteoblast slaves
Boyce, B. F., & Xing, L. (2006) · Nature Medicine · doi:10.1038/nm1206-1356 · Cited by 25
Oh, J., & Lee, N. K. (2017) · Molecules and Cells · doi:10.14348/molcells.2017.0025 · Cited by 24
Enhancement of RANKL‐induced MITF‐E expression and osteoclastogenesis by TGF‐β
Asai, K., Funaba, M., & Murakami, M. (2014) · Cell Biochemistry and Function · doi:10.1002/cbf.3028 · Cited by 24
The Vitamin D Analogue ED71 but Not 1,25(OH)2D3 Targets HIF1α Protein in Osteoclasts
Sato, Y., Miyauchi, Y., Yoshida, S., Morita, M., Kobayashi, T., Kanagawa, H., Katsuyama, E., Fujie, A., Wu, H., Tando, T., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0111845 · Cited by 24
Self-citationMolecules and signaling pathways involved in the expression of OC-STAMP during osteoclastogenesis
Kim, M. H., Park, M., Baek, S., Kim, H. J., & Kim, S. H. (2010) · Amino Acids · doi:10.1007/s00726-010-0755-4 · Cited by 24
KAMEYAMA, S., Yoshimura, Y., Kameyama, T., Kikuiri, T., Matsuno, M., Deyama, Y., Suzuki, K., & Iida, J. (2012) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2012.1220 · Cited by 24
Matsubara, R., Kukita, T., Ichigi, Y., Takigawa, I., Qu, P. F., Funakubo, N., Miyamoto, H., Nonaka, K., & Kukita, A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0047930 · Cited by 24
Chiou, W., Liao, J., Huang, C.-Y., & Chen, C. (2010) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2010.00823.x · Cited by 24
Multifunctional Properties of RANKL/RANK in Cell Differentiation, Proliferation and Metastasis
Kukita, A., & Kukita, T. (2013) · Future Oncology · doi:10.2217/fon.13.115 · Cited by 24
Ferulic acid impairs osteoclast fusion and exacerbates survival of mature osteoclasts
Sagar, T., Rantlha, M., Kruger, M. C., Coetzee, M., & Deepak, V. (2016) · Cytotechnology · doi:10.1007/s10616-016-0009-8 · Cited by 24
Bone Development and Remodeling
Maes, C., & Kronenberg, H. M. (2015) · Elsevier eBooks · doi:10.1016/b978-0-323-18907-1.00060-3 · Cited by 26
Champion, T., Partridge, L. J., Ong, S., Malleret, B., Wong, S. C., & Monk, P. N. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01247 · Cited by 24
Switch of macrophage fusion competency by 3D matrices
Fang, J. Y., Yang, Z. G., & Han, B. (2020) · Scientific Reports · doi:10.1038/s41598-020-67056-9 · Cited by 27
Substrates, regulation, cellular functions, and disease associations of P4-ATPases
Shin, H., & Takatsu, H. (2025) · Communications Biology · doi:10.1038/s42003-025-07549-3 · Cited by 23
DLX3 negatively regulates osteoclastic differentiation through microRNA-124
Zhao, N., Han, D. K., Liu, Y., Li, Y., Zeng, L., Wang, Y., & Feng, H. (2016) · Experimental Cell Research · doi:10.1016/j.yexcr.2016.01.018 · Cited by 23
Effect of the release from mechanical stress on osteoclastogenesis in RAW264.7 cells
Yoshimura, Y. (2011) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2011.675 · Cited by 23
Cegielski, M., Iżykowska, I., Podhorska‐Okołów, M., Zabel, M., & Dzięgiel, P. (2008) · PubMed · Cited by 23
Ye, F., Zhou, Q., Tian, L., Lei, F., & Feng, D. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.7338 · Cited by 23
Huang, L., Chen, Y., Huang, W., & Wu, H. (2018) · Lab on a Chip · doi:10.1039/c7lc01131h · Cited by 23
Advances in the understanding of the role of type-H vessels in the pathogenesis of osteoporosis
Ding, W., Xu, C., Zhang, Y., & Chen, H. (2020) · Archives of Osteoporosis · doi:10.1007/s11657-019-0677-z · Cited by 23
Hou, H., Peng, Q., Wang, S., Zhang, Y., Cao, J., Deng, Y., Wang, Y., Sun, W., & Wang, H. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01696 · Cited by 24
Bagnall, J., Rowe, W., Alachkar, N., Roberts, J., England, H., Clark, C. I., Platt, M., Jackson, D. A., Muldoon, M. R., & Paszek, P. (2020) · Cell Systems · doi:10.1016/j.cels.2020.08.007 · Cited by 22
Miyamoto, T. K. (2013) · JAK-STAT · doi:10.4161/jkst.24777 · Cited by 24
Self-citationKuroda, Y., Hisatsune, C., Mizutani, A., Ogawa, N., Matsuo, K., & Mikoshiba, K. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.05611-11 · Cited by 22
Xu, Q., Zhan, P., Li, X., Mo, F., Xu, H., Liu, Y., Lai, Q., Zhang, B., Dai, M., & Liu, X. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.16949 · Cited by 22
Essentiality of Nfatc1 short isoform in osteoclast differentiation and its self-regulation
Omata, Y., Tachibana, H., Aizaki, Y., Mimura, T., & Sato, K. (2023) · Scientific Reports · doi:10.1038/s41598-023-45909-3 · Cited by 23
Oral microbiota–host interaction: the chief culprit of alveolar bone resorption
Xu, J., Yu, L., Ye, S., Ye, Z., Yang, L., & Xu, X. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1254516 · Cited by 22
Identification of rare genetic variants in novel loci associated with Paget’s disease of bone
Beauregard, M., Gagnon, É., Guay-Bélanger, S., Morissette, J., Brown, J. P., & Michou, L. (2013) · Human Genetics · doi:10.1007/s00439-013-1409-x · Cited by 22
Role of miR-222-3p in c-Src-Mediated Regulation of Osteoclastogenesis
Takigawa, S., Chen, A. B., Wan, Q., Na, S., Sudo, A., Yokota, H., & Hamamura, K. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17020240 · Cited by 22
Proteomic approaches to study osteoclast biology
Segeletz, S., & Hoflack, B. (2016) · PROTEOMICS · doi:10.1002/pmic.201500519 · Cited by 21
Ihn, H. J., Lee, T., Kim, J. A., Lee, D., Kim, N. D., Shin, H., Bae, Y. C., & Park, E. K. (2017) · PLoS ONE · doi:10.1371/journal.pone.0170159 · Cited by 22
Coudert, A. E., Redelsperger, F., Chabbi-Achengli, Y., Vernochet, C., Marty, C., Decrouy, X., Heidmann, T., de Vernejoul, M. C., & Dupressoír, A. (2019) · Bone Reports · doi:10.1016/j.bonr.2019.100214 · Cited by 22
Inhibitory effect of minocycline on osteoclastogenesis in mouse bone marrow cells
Nagasawa, T., Arai, M., & Togari, A. (2011) · Archives of Oral Biology · doi:10.1016/j.archoralbio.2011.02.002 · Cited by 22
An, D., Kim, K., & Lu, W. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.563817 · Cited by 21
Lazebnik, Y. A. (2021) · Oncotarget · doi:10.18632/oncotarget.28088 · Cited by 22
Lysophosphatidic acid stimulates osteoclast fusion through OC-STAMP and P2X7 receptor signaling
Hwang, Y., Ma, G.-T., Park, K.-K., & Chung, W.-Y. (2013) · Journal of Bone and Mineral Metabolism · doi:10.1007/s00774-013-0470-9 · Cited by 20
Adseverin plays a role in osteoclast differentiation and periodontal disease‐mediated bone loss
Jiang, H., Wang, Y., Viniegra, A., Sima, C., McCulloch, C. A., & Glogauer, M. (2015) · The FASEB Journal · doi:10.1096/fj.14-265744 · Cited by 21
Lee, W., Lee, E., Sung, M.-S., Choi, Y., & Yoo, W. (2017) · The Korean Journal of Internal Medicine · doi:10.3904/kjim.2015.244 · Cited by 21
Kondo, T., Otsuka, Y., Aoki, H., Goto, Y., Kawaguchi, Y., Waguri‐Nagaya, Y., Miyazawa, K., Goto, S., & Aoyama, M. (2021) · American Journal Of Pathology · doi:10.1016/j.ajpath.2021.08.014 · Cited by 21
Tada, T., Shin, M., Fukushima, H., Okabe, K., Ozeki, S., Okamoto, M., & Jimi, E. (2008) · Cancer Letters · doi:10.1016/j.canlet.2008.09.015 · Cited by 21
Cellular and Molecular Dynamics in the Foreign Body Reaction
Luttikhuizen, D. T., Harmsen, M. C., & van Luyn, M. J. A. (2006) · Tissue Engineering · doi:10.1089/ten.2006.12.ft-126 · Cited by 22
P2 receptors in macrophage fusion and osteoclast formation
Steinberg, T. H., & Hiken, J. (2007) · Purinergic Signalling · doi:10.1007/s11302-006-9036-9 · Cited by 21
Kotake, S., Nanke, Y., Kawamoto, M., Yago, T., Udagawa, N., Ichikawa, N., Kobashigawa, T., Saito, S., Momohara, S., Kamatani, N., et al. (2009) · Bone · doi:10.1016/j.bone.2009.06.019 · Cited by 21
Differentiation analyses of adult suspension mononucleated peripheral blood cells of Mus musculus
Ariffin, S. H. Z., Abidin, I. Z. Z., Yazid, M. D., & Wahab, R. M. A. (2010) · Cell Communication and Signaling · doi:10.1186/1478-811x-8-29 · Cited by 20
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Choi, Y., Faccio, R., Teitelbaum, S. L., & Takayanagi, H. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800571-2.00004-9 · Cited by 21
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Poudel, S., Martins, G., Cancela, M. L., & Gavaia, P. J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232315160 · Cited by 20
Nakamura, H., Nakashima, T., Hayashi, M., Izawa, N., Yasui, T., Aburatani, H., Tanaka, S., & Takayanagi, H. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.11.009 · Cited by 20
Ihn, H. J., Lee, T., Lee, D., Bae, J., Kim, S., Jang, I. H., Bae, Y. C., Shin, H., & Park, E. K. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00367 · Cited by 20
Hoshi, H., Monoe, F., Ohsawa, I., Ohta, S., & Miyamoto, T. K. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.04.013 · Cited by 20
Self-citationFertilization in C. elegans requires an intact C-terminal RING finger in sperm protein SPE-42
Wilson, L. D., Sackett, J. M., Mieczkowski, B. D., Richie, A. L., Thoemke, K., Rumbley, J. N., & Kroft, T. L. (2011) · BMC Developmental Biology · doi:10.1186/1471-213x-11-10 · Cited by 21
Identification of Differentially Expressed Genes in Papillary Thyroid Cancers
Lee, K., Huang, S. M., Li, S., & Kim, J. (2009) · Yonsei Medical Journal · doi:10.3349/ymj.2009.50.1.60 · Cited by 20
Lorenzo, J. A., CANALIS, E. M., & Raisz, L. G. (2011) · Elsevier eBooks · doi:10.1016/b978-1-4377-0324-5.00029-8 · Cited by 20
Multinucleation resets human macrophages for specialized functions at the expense of their identity
Ahmadzadeh, K., Pereira, M., Vanoppen, M., Bernaerts, E., Ko, J., Mitera, T., Maksoudian, C., Manshian, B. B., Soenen, S. J., Rosé, C. D., et al. (2023) · EMBO Reports · doi:10.15252/embr.202256310 · Cited by 22
Oh, J., Lee, S. W., Joung, S. H., Oh, Y. T., Kim, H. S., & Lee, N. K. (2015) · Cellular Signalling · doi:10.1016/j.cellsig.2015.09.002 · Cited by 20
Cell Fusion In Tumor Development: Accelerated Genetic Evolution
Harkness, T., Weaver, B. A. A., Alexander, C. M., & Ogle, B. M. (2012) · Critical Reviews™ in Oncogenesis · doi:10.1615/critrevoncog.v18.i1-2.30 · Cited by 19
United we stand: Adhesion and molecular mechanisms driving cell fusion across species
Zito, F., Lampiasi, N., Kireev, I. I., & Russo, R. (2016) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2016.09.002 · Cited by 18
Ceglie, I. D., van den Akker, G., Ascone, G., ten Harkel, B., Häcker, H., van de Loo, F. A. J., Koenders, M. I., van der Kraan, P. M., de Vries, T. J., Vogl, T. J., et al. (2016) · Journal of Leukocyte Biology · doi:10.1189/jlb.1ab0416-180rr · Cited by 19
Natural uranium impairs the differentiation and the resorbing function of osteoclasts
Gritsaenko, T., Pierrefite‐Carle, V., Lorivel, T., Breuil, V., Carle, G. F., & Santucci‐Darmanin, S. (2017) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2017.01.008 · Cited by 19
Sakaguchi, Y., Nishikawa, K., Seno, S., Matsuda, H., Takayanagi, H., & Ishii, M. (2018) · Scientific Reports · doi:10.1038/s41598-018-25748-3 · Cited by 19
Zhao, K., Jia, Y., Peng, J., Pang, C., Zhang, T., Han, W., Jiang, J., Lu, X., Zhu, J., & Qian, Y. (2019) · The FASEB Journal · doi:10.1096/fj.201802575rr · Cited by 20
CircRNAs and LncRNAs in Osteoporosis
He, T., Liu, W., Cao, L., Liu, Y., Zi, Z., Zhong, Y., Wang, H., Mo, Y., Peng, S., & Shuai, C. (2020) · Differentiation · doi:10.1016/j.diff.2020.10.002 · Cited by 18
Tsukazaki, H., Kikuta, J., Ao, T., Morimoto, A., Fukuda, C., Tsuda, E., Minoshima, M., Kikuchi, K., Kaito, T., & Ishii, M. (2021) · Bone · doi:10.1016/j.bone.2021.116095 · Cited by 19
Zeng, Z., Zhang, C., & Chen, J. (2013) · Journal of Bone and Mineral Metabolism · doi:10.1007/s00774-013-0434-0 · Cited by 19
Zhang, J.-Q., Takahashi, A., Gu, J.-Y., Zhang, X., Kyumoto‐Nakamura, Y., Kukita, A., Uehara, N., Hiura, H., Yamaza, T., & Kukita, T. (2021) · Laboratory Investigation · doi:10.1038/s41374-021-00656-9 · Cited by 20
Noda, K., Lu, S.-L., Chen, S., Tokuda, K., Li, Y., Hao, F., Wada, Y., Sun‐Wada, G., Murakami, S., Fukuda, M., et al. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105191 · Cited by 18
Tm4sf19 deficiency inhibits osteoclast multinucleation and prevents bone loss
Park, S., Heo, J. S., Mizuno, S., Kim, M., An, H., Hong, E., Kang, M. G., Kim, J., Yun, R., Park, H., et al. (2023) · Metabolism · doi:10.1016/j.metabol.2023.155746 · Cited by 18
Binder, F., Hayakawa, M., Choo, M., Sano, Y., & Park, J. M. (2012) · Molecular Immunology · doi:10.1016/j.molimm.2012.12.004 · Cited by 18
Moon, S., Choi, S., & Kim, S. H. (2015) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2015.06.008 · Cited by 18
Melphalan modifies the bone microenvironment by enhancing osteoclast formation
Chai, R. C. C., McDonald, M. M., Terry, R. L., Kovačić, N., Down, J. M., Pettitt, J. A., Mohanty, S. T., Shah, S., Haffari, G., Xu, J., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.19152 · Cited by 18
Pmepa1 induced by RANKL‐p38 MAPK pathway has a novel role in osteoclastogenesis
Funakubo, N., Xu, X., Kukita, T., Nakamura, S., Miyamoto, H., & Kukita, A. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.26147 · Cited by 18
Narahara, H., Sakai, E., Yamaguchi, Y., Narahara, S., Iwatake, M., Okamoto, K., Yoshida, N., & Tsukuba, T. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.26605 · Cited by 18
Lin, X., Xiao, Y., Chen, Z., Ma, J., Qiu, W., Zhang, K., Xu, F., Dang, K., & Qian, A. (2019) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2019.110494 · Cited by 18
Rivera, A., & Swanson, W. J. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.827454 · Cited by 21
Sanecka-Duin, A., Ansems, M., Prosser, A., Danielski, K., Warner, K., den Brok, M. H., Jansen, B., Eleveld-Trancikova, D., & Adema, G. J. (2011) · BMC Immunology · doi:10.1186/1471-2172-12-57 · Cited by 18
Possible role of IRTKS in Tks5-driven osteoclast fusion
Oikawa, T., & Matsuo, K. (2012) · Communicative & Integrative Biology · doi:10.4161/cib.21252 · Cited by 18
Innate type 2 lymphocytes trigger an inflammatory switch in alveolar macrophages
Verwaerde, S., Hastir, J., Schetters, S. T. T., Smole, U., Seys, L., Baptista, A. P., English, K., Schuijs, M. J., Aegerter, H., Damme, K. F. A. V., et al. (2025) · Immunity · doi:10.1016/j.immuni.2025.11.015 · Cited by 20
Inhibitory effects of orthosilicic acid on osteoclastogenesis in RANKL ‐stimulated RAW264 .7 cells
Magnusson, C., Uribe, P., Jugdaohsingh, R., Powell, J. J., Johansson, A., & Ransjö, M. (2021) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.37189 · Cited by 17
Cheng, C.-P., Huang, H., Hsu, Y.-C., Sheu, M.-J., & Chang, D. (2012) · Journal of Clinical Immunology · doi:10.1007/s10875-012-9660-9 · Cited by 17
Commensal gut bacterium critically regulates alveolar bone homeostasis
Hathaway‐Schrader, J. D., Carson, M. D., Gerasco, J. E., Warner, A. J., Swanson, B. A., Aguirre, J. I., Westwater, C., Liu, B., & Novince, C. M. (2021) · Laboratory Investigation · doi:10.1038/s41374-021-00697-0 · Cited by 17
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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