Sialylation of TLR2 initiates osteoclast fusion
Open accessAbstract
The molecular control of osteoclast formation is still not clearly elucidated. Here, we show that a process of cell recognition mediated by Siglec15-TLR2 binding is indispensable and occurs prior to cell fusion in RANKL-mediated osteoclastogenesis. Siglec15 has been shown to regulate osteoclastic bone resorption. However, the receptor for Siglec15 has not been identified, and the signaling mechanism involving Siglec15 in osteoclast function remains unclear. We found that Siglec15 bound sialylated TLR2 as its receptor and that the binding of sialylated TLR2 to Siglec15 in macrophages committed to the osteoclast-lineage initiated cell fusion for osteoclast formation, in which sialic acid was transferred by the sialyltransferase ST3Gal1. Interestingly, the expression of Siglec15 in macrophages was activated by M-CSF, whereas ST3Gal1 expression was induced by RANKL. Both Siglec15-specific deletion in macrophages and intrafemoral injection of sialidase abrogated cell recognition and reduced subsequent cell fusion for the formation of osteoclasts, resulting in increased bone formation in mice. Thus, our results reveal that cell recognition mediated by the binding of sialylated TLR2 to Siglec15 initiates cell fusion for osteoclast formation.
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Molecules affecting osteoclast fusion and angiogenesis, such as SIGLEC15, L-plastin, and TLR2, have been successively discovered.
“Since then, molecules affecting osteoclast fusion and angiogenesis, such as SIGLEC15, L-plastin, and TLR2, have been successively discovered52–54.”
From Targeting Msx2 as a brake in the fusion fate of osteoclasts and an anabolic therapy in pre-clinical models of osteoporosis (2025) · cites this paper as [54]
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Dou, C., Ding, N., Luo, F., Hou, T., Cao, Z., Bai, Y., Liu, C., Xu, J., & Dong, S. (2017) · Advanced Science · doi:10.1002/advs.201700578 · Cited by 105 · see citing works
Self-citationRetractedOsteoclast differentiation and activation
Boyle, W. J., Simonet, W. S., & Lacey, D. L. (2003) · Nature · doi:10.1038/nature01658 · Cited by 6,670 · cited 3× · see citing works
“Together, M-CSF and RANKL effectively induce the expression of osteoclast lineagespecific genes and lead to the development of osteoclast maturation marked by cell fusion-mediated multinucleation.(1,3) The requirement for cell fusion in osteoclast formation has been studied for decades, and numerous fusogenic molecule…”
BackgroundOsteoprotegerin ligand is a cytokine that regulates osteoclast differentiation and activation.
Lacey, D. L., Timms, E., Tan, H.-L., Kelley, M. J., Dunstan, C. R., Burgess, T., Elliott, R., Colombero, A., Elliott, G., Scully, S., et al. (1998) · Cell · doi:10.1016/s0092-8674(00)81569-x · Cited by 5,439 · see citing works
Toll-like receptors and innate immunity
Medzhitov, R. (2001) · Nature Reviews Immunology · doi:10.1038/35100529 · Cited by 4,308 · see citing works
Yasuda, H., Shima, N., Nakagawa, N., Yamaguchi, K., Kinosaki, M., Mochizuki, S.-I., Tomoyasu, A., Yano, K., Goto, M., Murakami, A., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.7.3597 · Cited by 4,224 · see citing works
Manolagas, S. C. (2000) · Endocrine Reviews · doi:10.1210/edrv.21.2.0395 · Cited by 2,575 · see citing works
Sato, K., Suematsu, A., Okamoto, K., Yamaguchi, A., Morishita, Y., Kadono, Y., Tanaka, S., Kodama, T., Akira, S., Iwakura, Y., et al. (2006) · The Journal of Experimental Medicine · doi:10.1084/jem.20061775 · Cited by 1,554 · see citing works
Dai, X.-M., Ryan, G. R., Hapel, A. J., Dominguez, M. G., Russell, R. G., Kapp, S., Sylvestre, V., & Stanley, E. R. (2002) · Blood · doi:10.1182/blood.v99.1.111 · Cited by 1,184 · see citing works
Sialic acids in human health and disease
Varki, A. P. (2008) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2008.06.002 · Cited by 1,003 · see citing works
PDGF-BB secreted by preosteoclasts induces angiogenesis during coupling with osteogenesis
Xie, H., Cui, Z., Wang, L., Xia, Z., Hu, Y., Xian, L., Li, C., Xie, L., Crane, J., Wan, M., et al. (2014) · Nature Medicine · doi:10.1038/nm.3668 · Cited by 951 · see citing works
Self-citationCostimulatory signals mediated by the ITAM motif cooperate with RANKL for bone homeostasis
Koga, T., Inui, M., Inoue, K., Kim, S., Suematsu, A., Kobayashi, E., Iwata, T., Ohnishi, H., Matozaki, T., Kodama, T., et al. (2004) · Nature · doi:10.1038/nature02444 · Cited by 826 · see citing works
TRANCE/RANKL knockout mice are protected from bone erosion in a serum transfer model of arthritis.
Pettit, A. R., Ji, H., von Stechow, D., Müller, R., Goldring, S. R., Choi, Y., Benoist, C., & Gravallese, E. M. (2001) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)63016-7 · Cited by 807 · see citing works
Estrogen, cytokines, and pathogenesis of postmenopausal osteoporosis
Pacifici, R. (1996) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.5650110802 · Cited by 741 · see citing works
Siglec-15 as an immune suppressor and potential target for normalization cancer immunotherapy
Wang, J., Sun, J., Liu, L. N., Flies, D. B., Nie, X., Toki, M. I., Zhang, J., Song, C. C., Zarr, M. A., Zhou, X., et al. (2019) · Nature Medicine · doi:10.1038/s41591-019-0374-x · Cited by 676 · see citing works
TLR2 is expressed on activated T cells as a costimulatory receptor.
Komai-Koma, M., Jones, L., Ogg, G., Xu, D.-M., & Liew, F. (2004) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0400171101 · Cited by 556 · see citing works
Subchondral bone osteoclasts induce sensory innervation and osteoarthritis pain
Zhu, S., Zhu, J., Zhen, G., Hu, Y., An, S., Li, Y., Zheng, Q., Chen, Z., Yang, Y., Wan, M., et al. (2019) · Journal of Clinical Investigation · doi:10.1172/jci121561 · Cited by 456 · see citing works
Self-citationOsteoclasts recycle via osteomorphs during RANKL-stimulated bone resorption
McDonald, M. M., Khoo, W. H., Ng, P. Y., Xiao, Y., Zamerli, J., Thatcher, P., Kyaw, W., Pathmanandavel, K., Grootveld, A. K., Moran, I., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.002 · Cited by 433 · see citing works
Hernandez, R. K., Wade, S. W., Reich, A., Pirolli, M. A., Liede, A., & Lyman, G. H. (2018) · BMC Cancer · doi:10.1186/s12885-017-3922-0 · Cited by 385 · see citing works
Myc-binding-site recognition in the human genome is determined by chromatin context
Guccione, E., Martinato, F., Finocchiaro, G., Luzi, L., Tizzoni, L., Olio, V. D., Zardo, G., Nervi, C., Bernard, L., & Amati, B. B. (2006) · Nature Cell Biology · doi:10.1038/ncb1434 · Cited by 365 · see citing works
Witten, P. E., & Huysseune, A. (2009) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/j.1469-185x.2009.00077.x · Cited by 364 · see citing works
The Role of TLRs in Anti-cancer Immunity and Tumor Rejection
Urban‐Wójciuk, Z., Khan, M. M., Oyler, B. L., Fåhræus, R., Marek-Trzonkowska, N. M., Nita‐Lazar, A., Hupp, T. R., & Goodlett, D. R. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02388 · Cited by 307 · see citing works
αvβ3and macrophage colony‐stimulating factor: partners in osteoclast biology
Ross, F. P., & Teitelbaum, S. L. (2005) · Immunological Reviews · doi:10.1111/j.0105-2896.2005.00331.x · Cited by 303 · see citing works
Regulation of the metastatic cell phenotype by sialylated glycans
Schultz, M., Swindall, A. F., & Bellis, S. L. (2012) · Cancer and Metastasis Reviews · doi:10.1007/s10555-012-9359-7 · Cited by 302 · see citing works
Sialic Acid Blockade Suppresses Tumor Growth by Enhancing T-cell–Mediated Tumor Immunity
Büll, C., Boltje, T. J., Balneger, N., Weischer, S., Wassink, M., van Gemst, J. J., Bloemendal, V. R. L. J., Boon, L., van der Vlag, J., Heise, T., et al. (2018) · Cancer Research · doi:10.1158/0008-5472.can-17-3376 · Cited by 272 · see citing works
Cao, L., Yu, Y., Bilke, S., Walker, R. L., Mayeenuddin, L. H., Azorsa, D. O., Yang, F., Pineda, M. A., Helman, L. J., & Meltzer, P. S. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-0582 · Cited by 238 · see citing works
Stimulation by Toll-Like Receptors Inhibits Osteoclast Differentiation1
Takami, M., Kim, N., Rho, J., & Choi, Y. (2002) · Journal of Immunology · doi:10.4049/jimmunol.169.3.1516 · Cited by 204 · see citing works
The Effects of TLR Activation on T-Cell Development and Differentiation
Jin, B., Sun, T., Yu, X., Yang, Y., & Yeo, A. E. T. (2012) · Clinical and Developmental Immunology · doi:10.1155/2012/836485 · Cited by 202 · see citing works
Amith, S. R., Jayanth, P., Franchuk, S. L., Finlay, T. M., Seyrantepe, V., Beyaert, R., Pshezhetsky, A. V., & Szewczuk, M. R. (2009) · Cellular Signalling · doi:10.1016/j.cellsig.2009.09.038 · Cited by 194 · see citing works
Takamiya, R., Ohtsubo, K., Takamatsu, S., Taniguchi, N., & Angata, T. (2012) · Glycobiology · doi:10.1093/glycob/cws139 · Cited by 191 · see citing works
Dou, C., Ding, N., Zhao, C., Hou, T., Kang, F., Cao, Z., Liu, C., Bai, Y., Dai, Q., Ma, Q., et al. (2017) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.3364 · Cited by 166 · see citing works
Self-citationChen, G., Brown, N. K., Wu, W., Khedri, Z., Yu, H., Chen, X., van de Vlekkert, D., d’Azzo, A., Zheng, P., & Liu, Y. (2014) · eLife · doi:10.7554/elife.04066 · Cited by 150 · see citing works
Weber, A., Morse, M., & Gay, N. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403830200 · Cited by 149 · see citing works
Kameda, Y., Takahata, M., Komatsu, M., Mikuni, S., Hatakeyama, S., Shimizu, T., Angata, T., Kinjo, M., Minami, A., & Iwasaki, N. (2013) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.1989 · Cited by 128 · see citing works
Cell-based glycan arrays for probing glycan–glycan binding protein interactions
Briard, J. G., Jiang, H., Moremen, K. W., Macauley, M. S., & Wu, P. (2018) · Nature Communications · doi:10.1038/s41467-018-03245-5 · Cited by 123 · see citing works
Osteoclast-derived apoptotic bodies couple bone resorption and formation in bone remodeling
Ma, Q., Liang, M., Wu, Y., Luo, F., Ma, Z., Dong, S., Xu, J., & Dou, C. (2021) · Bone Research · doi:10.1038/s41413-020-00121-1 · Cited by 117 · see citing works
Self-citationKeppler, O. T., Peter, M. E., Hinderlich, S., Moldenhauer, G., Stehling, P., Schmitz, I., Schwartz‐Albiez, R., Reutter, W. G., & Pawlita, M. (1999) · Glycobiology · doi:10.1093/glycob/9.6.557 · Cited by 101 · see citing works
Dou, C., Zhang, C., Kang, F., Yang, X., Jiang, H., Bai, Y., Xiang, J., Xu, J., & Dong, S. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.08.002 · Cited by 100 · see citing works
Self-citationSialic Acid Metabolism: A Key Player in Breast Cancer Metastasis Revealed by Metabolomics
Teoh, S. T., Ogrodzinski, M. P., Ross, C. R., Hunter, K. W., & Lunt, S. Y. (2018) · Frontiers in Oncology · doi:10.3389/fonc.2018.00174 · Cited by 98 · see citing works
Hiruma, Y., Hirai, T., & Tsuda, E. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.05.015 · Cited by 95 · see citing works
Chatani, M., Takano, Y., & Kudō, A. (2011) · Developmental Biology · doi:10.1016/j.ydbio.2011.09.013 · Cited by 92 · see citing works
Bone-targeted pH-responsive cerium nanoparticles for anabolic therapy in osteoporosis
Dou, C., Li, J., He, J., Luo, F., Yu, T., Dai, Q., Chen, Y., Xu, J., Yang, X., & Dong, S. (2021) · Bioactive Materials · doi:10.1016/j.bioactmat.2021.04.038 · Cited by 84 · see citing works
Self-citationHiruma, Y., Tsuda, E., Maeda, N., Okada, A., Kabasawa, N., Miyamoto, M., Hattori, H., & Fukuda, C. (2012) · Bone · doi:10.1016/j.bone.2012.11.036 · Cited by 79 · see citing works
Identification of Siglec Ligands Using a Proximity Labeling Method
Chang, L., Chen, Y., Fan, C.-Y., Tang, C.-J., Chen, Y.-H., Low, P.-Y., Ventura, A., Lin, C., Chen, Y., & Angata, T. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00625 · Cited by 76 · see citing works
Stuible, M., Moraitis, A. N., Fortin, A., Saragosa, S., Kalbakji, A., Filion, M., & Tremblay, G. B. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.494542 · Cited by 71 · see citing works
CD22 Regulates Adaptive and Innate Immune Responses of B Cells
Kawasaki, N., Rademacher, C., & Paulson, J. (2010) · Journal of Innate Immunity · doi:10.1159/000322375 · Cited by 66 · see citing works
Zanin‐Zhorov, A., & Cohen, I. R. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00211 · Cited by 64 · see citing works
Stamatos, N. M., Curreli, S., Zella, D., & Cross, A. S. (2003) · Journal of Leukocyte Biology · doi:10.1189/jlb.0503241 · Cited by 49 · see citing works
Sialylation of cell surface glycoconjugates is essential for osteoclastogenesis
Takahata, M., Iwasaki, N., Nakagawa, H., Abe, Y., Watanabe, T., Ito, M., Majima, T., & Minami, A. (2007) · Bone · doi:10.1016/j.bone.2007.03.016 · Cited by 42 · see citing works
Baroukh, B., Cherruau, M., Dobigny, C., Guez, D., & Jl, S. (2000) · Bone · doi:10.1016/s8756-3282(00)00372-0 · Cited by 37 · see citing works
Increased Serum Sialic Acid Levels in Primary Osteoarthritis and Inactive Rheumatoid Arthritis
Alturfan, A. A., Uslu, E., Emekli‐Alturfan, E., Hatemi, G., Fresko, İ., & Kökoǧlu, E. (2007) · The Tohoku Journal of Experimental Medicine · doi:10.1620/tjem.213.241 · Cited by 35 · see citing works
Siglec-E Negatively Regulates the Activation of TLR4 by Controlling Its Endocytosis
Wu, Y., Ren, D., & Chen, G. (2016) · The Journal of Immunology · doi:10.4049/jimmunol.1600772 · Cited by 33 · see citing works
Elevated Serum Sialic Acid Levels Predict Prostate Cancer As Well As Bone Metastases
Zhang, C., Yan, L., Song, H., Ma, Z., Chen, D., Yang, F., Fang, L., Li, Z., Li, K., Li, D., et al. (2019) · Journal of Cancer · doi:10.7150/jca.27700 · Cited by 31 · see citing works
Regulation of Osteoclastogenesis by Integrated Signals From Toll‐Like Receptors
Krisher, T., & Bar‐Shavit, Z. (2014) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24891 · Cited by 29 · see citing works
Cell replication in craniofacial periosteum: appositional vs. resorptive sites
Ochareon, P., & Herring, S. W. (2011) · Journal of Anatomy · doi:10.1111/j.1469-7580.2010.01336.x · Cited by 29 · see citing works
N‐linked sialyated sugar receptors support haematopoietic cell‐osteoblast adhesions
Crean, S. M., Meneski, J. P., Hullinger, T. G., Reilly, M., DeBoever, E. H., & Taichman, R. S. (2004) · British Journal of Haematology · doi:10.1046/j.1365-2141.2003.04786.x · Cited by 22 · see citing works
Carmona-Fernandes, D., Santos, M. J., Perpetuo, I. P., Fonseca, J. E., & Canhão, H. M. (2011) · Arthritis Research & Therapy · doi:10.1186/ar3500 · Cited by 21 · see citing works
Investigation of the Potential Use of Sialic Acid as a Biomarker for Rheumatoid Arthritis.
Li, W. S., Liu, Y., Zheng, X., Gao, J., Wang, L., & Li, Y. (2019) · PubMed · Cited by 14 · see citing works
Liou, L.-B., & Huang, C.-C. (2016) · PLoS ONE · doi:10.1371/journal.pone.0151669 · Cited by 13 · see citing works
Serum sialic acid estimation in various bone disorders.
Gs, V., Sk, L., Pm, S., & Rk, V. (1982) · PubMed · Cited by 1 · see citing works
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Oxylipin-PPARγ-initiated adipocyte senescence propagates secondary senescence in the bone marrow
Liu, X., Gu, Y., Kumar, S., Amin, S., Guo, Q., Wang, J., Fang, C.-L., Cao, X., & Wan, M. (2023) · Cell Metabolism · doi:10.1016/j.cmet.2023.03.005 · Cited by 137 · see citing works
Self-citationRoles of Toll-like Receptor Signaling in Inflammatory Bone Resorption
Tominari, T., Matsumoto, C., Tanaka, Y., Shimizu, K., Takatoya, M., Sugasaki, M., Karouji, K., Kasuga, U., Miyaura, C., Miyata, S., et al. (2024) · Biology · doi:10.3390/biology13090692 · Cited by 42 · see citing works
Sympathetic Innervation Regulates Osteocyte‐Mediated Cortical Bone Resorption during Lactation
Guo, Q., Chen, N., Cheng, Q., Qi, C., Noller, K., Wan, M., Liu, X., Zhang, W., Cahan, P., & Cao, X. (2023) · Advanced Science · doi:10.1002/advs.202207602 · Cited by 41 · see citing works
Self-citationWu, Y., Ai, H., Xi, Y., Tan, J., Qu, Y., Xu, J., Luo, F., & Dou, C. (2023) · Cell Reports Medicine · doi:10.1016/j.xcrm.2023.101165 · Cited by 37 · see citing works
Self-citationLi, Y., Wang, X., Hu, B., Sun, Q., Wan, M., Carr, A. J., Liu, S., & Cao, X. (2023) · Bone Research · doi:10.1038/s41413-023-00252-1 · Cited by 33 · see citing works
Self-citationYe, P., Yang, Y., Qu, Y., Yang, W., Tan, J., Zhang, C., Sun, D., Zhang, J., Zhao, W., Guo, S., et al. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.134091 · Cited by 25 · see citing works
Self-citationShu, Y., Tan, Z., Pan, Z., Chen, Y., Wang, J., He, J., Wang, J., & Wang, Y. (2024) · Cell Death and Differentiation · doi:10.1038/s41418-024-01368-5 · Cited by 24 · see citing works
Atsttrin regulates osteoblastogenesis and osteoclastogenesis through the TNFR pathway
Liu, K., Wang, Z., Liu, J., Zhao, W. H., Qiao, F., He, Q., Shi, J., Meng, Q., Wei, J., & Cheng, L. (2023) · Communications Biology · doi:10.1038/s42003-023-05635-y · Cited by 24 · see citing works
Osteoclasts in Osteosarcoma: Mechanisms, Interactions, and Therapeutic Prospects
Gao, Y.-M., Pei, Y., Zhao, F.-F., & Wang, L. (2023) · Cancer Management and Research · doi:10.2147/cmar.s431213 · Cited by 23 · see citing works
Glycobiology in osteoclast differentiation and function
Yang, S., He, Z., Wu, T., Wang, S., & Dai, H. (2023) · Bone Research · doi:10.1038/s41413-023-00293-6 · Cited by 21 · see citing works
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Liu, Y., Chen, H., Chen, T., Qiu, G., & Yu, H. (2024) · Frontiers in Oncology · doi:10.3389/fonc.2024.1445025 · Cited by 17 · see citing works
Chen, Z., Yang, W., Tang, Y. M., Dong, Q., Huang, K., Tan, J., Zhang, J., Cai, J., Yu, Q., Dai, Q., et al. (2025) · Advanced Science · doi:10.1002/advs.202415895 · Cited by 16 · see citing works
Self-citationMa, Q., Wang, S., Xue, H., Ni, L., Yuan, P., Shen, Y., Zheng, B., Wang, Q., Zhang, J., Wang, H., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-61938-0 · Cited by 15 · see citing works
“Since then, molecules affecting osteoclast fusion and angiogenesis, such as SIGLEC15, L-plastin, and TLR2, have been successively discovered 52 – 54 .”
RANK+TLR2+ myeloid subpopulation converts autoimmune to joint destruction in rheumatoid arthritis
Zhang, W., Noller, K., Crane, J. L., Wan, M., Wu, X., Cahan, P., & Cao, X. (2023) · eLife · doi:10.7554/elife.85553 · Cited by 15 · see citing works
Self-citationXue, P., Zhang, W., Shen, M., Yang, J., Chu, J., Wang, S., Wan, M., Zheng, J., Qiu, Z., & Cao, X. (2024) · Journal of Clinical Investigation · doi:10.1172/jci168155 · Cited by 14 · see citing works
Self-citationZhang, Y., Sun, H., Huang, F., Chen, Y., Ding, X., Zhou, C., Wu, Y. T., Zhang, Q., Ma, X., Wang, J., et al. (2024) · Journal of Bone and Mineral Research · doi:10.1093/jbmr/zjae042 · Cited by 12 · see citing works
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Feng, J., Fu, D., Sandeth, P., Hu, X., & Xing, Q. (2025) · International Dental Journal · doi:10.1016/j.identj.2025.103941 · Cited by 9 · see citing works
Ai, H., Dou, C., Wu, Y., Zhang, D., Zhang, Z., Zhang, C., Xi, Y., Qu, Y., Tan, J., Yin, P., et al. (2025) · Journal of Orthopaedic Translation · doi:10.1016/j.jot.2025.01.004 · Cited by 8 · see citing works
Self-citationLi, H., Yang, J., Deng, W., Zhou, T., Guo, D., Li, Y., Mo, G., Wen, G., Xu, J., Lai, Y., et al. (2025) · Phytomedicine · doi:10.1016/j.phymed.2025.156867 · Cited by 7 · see citing works
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Mechanistic and Therapeutic Implications of Protein and Lipid Sialylation in Human Diseases
Zhong, X., D’Antona, A. M., & Rouse, J. C. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252211962 · Cited by 2 · see citing works
Wang, Z., Sun, X., Chen, Z., Yu, J., Nie, Q., Ma, Z., Zhou, S., Li, T., Yao, H., Zhao, B., et al. (2025) · American Journal Of Pathology · doi:10.1016/j.ajpath.2025.10.011 · Cited by 2 · see citing works
Osteoclastogenesis Responds to STING Inhibition in a Non‐Monotonic Manner
Huang, L., Lu, W., Liu, H., Hu, J., Fan, J., Song, S., Cao, G., Ding, G., He, T., Li, Z. A., et al. (2026) · The FASEB Journal · doi:10.1096/fj.202502905rr · Cited by 2 · see citing works
Yu, Q., Qu, Y., Zhang, J., (223533), Z. Z., Guo, S., Luo, F., & Dou, C. (2026) · Bone Research · doi:10.1038/s41413-026-00571-z · Cited by 2 · see citing works
Self-citationChen, K. H., Hagino, T., & Qiu, Z. (2025) · Annual Review of Physiology · doi:10.1146/annurev-physiol-022724-105357 · Cited by 1 · see citing works
Qu, Y., Yu, Q., Chen, Y., Ai, H., Wu, Y., Ye, P., Tan, J., Dai, Q., Zhang, Z., Yang, W., et al. (2026) · Genes & Diseases · doi:10.1016/j.gendis.2026.102142 · Cited by 1 · see citing works
Self-citationLi, Y., Li, Z., Guo, X., Lai, S., Ma, J., Shan, T., Mei, L., Li, B., Lan, F., & Cheng, L. (2026) · Dental Materials · doi:10.1016/j.dental.2026.04.007 · Cited by 1 · see citing works
Unraveling the mechanisms behind joint damage
Fu, W., & Liu, C.-J. (2023) · eLife · doi:10.7554/elife.89778
Shu, Y., Tan, Z., Pan, Z., Chen, Y., Wang, J., He, J., Wang, J., & Wang, Y. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.05.21.595143
Jiang, Z., Zhang, Z., Zhang, D., Yu, Q., Deng, J., Qu, Y., Yang, Y., Zhang, Z., Guo, S., Zhang, J., et al. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1738896
Self-citationLei, Y., Qu, Y., (223533), Z. Z., Chen, Z., Zhang, D., Zhang, J., Tan, J., Dai, Q., Xu, J., Luo, F., et al. (2026) · Acta Biomaterialia · doi:10.1016/j.actbio.2026.04.045
Self-citationYi, J., Xiao, X., Zhang, H., Xu, X., Chen, K., Cai, X., Zhu, Y., Mo, X., Xiong, S., Chen, Z., et al. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2537622123
Wang, B., Wang, C., Zhang, Y., Yu, Y. P., Yuan, J., Chen, P., Chen, J., Tang, Y., Wang, Q.-P., & Tang, K. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1864484
The skeletal connectome: From molecular circuitry to systemic network medicine
Liu, W., Liu, D., Liu, Q., & Sun, Y. (2026) · Pharmacological Reviews · doi:10.1016/j.pharmr.2026.100154
Ispas, S., Maggio, V., Wali, A. F., Talath, S., Rabbani, S. A., Bhongade, B. A., Rangraze, I. R., Satyam, S. M., Арманович, А. А., Hoffmann, K., et al. (2026) · Nutrients · doi:10.3390/nu18182967
Zhang, D., Ai, H., Tang, Y., Qu, Y., Yang, Q., Zhang, Z., Xu, J., Wu, Y., & Dou, C. (2026) · Genes & Diseases · doi:10.1016/j.gendis.2026.102499
Self-citationRoles of sialoglycans in vertebrate development
Hildebrandt, H., & Münster-Kühnel, A. K. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.113650
- Authors
- Dou, C., Zhen, G., Dan, Y., Wan, M., Limjunyawong, N., & Cao, X.
- Affiliations
- Johns Hopkins University (US)
- Corresponding author
- Cao, Xu
- Venue
- Bone Research
- Published
- 2022-03-02
- Volume
- 10
- Issue
- 1
- Pages
- 24-24
- ISSN
- 2095-4700 (ISSN-L)
- 2095-6231
- PMC
- PMC8888621
- OpenAlex
- W4214826194
- Cited by
- 46
- References
- 59
- Citations by year
- 2026: 15 · 2025: 10 · 2024: 10 · 2023: 11
- FWCI
- 2.53
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Bone Research (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Johns Hopkins University
- National Institutes of Health
- National Institute on Aging (RF1AG068997, P01AG066603, R01AG076783)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01AR071432)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bone Metabolism and Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Immunology and Microbiology › Immunology › Phagocytosis and Immune Regulation
- Keywords
- osteoclastogenesis, osteoclast fusion, Siglec-15, sialic acid, ST3GAL1, sialyltransferase, RANKL, macrophage colony-stimulating factor, macrophages, cell recognition, bone resorption, bone formation
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