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Osteoclast-mediated bone resorption is controlled by a compensatory network of secreted and membrane-tethered metalloproteinases
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Independent of cathepsin K, the osteoclast-derived matrix metalloproteinases MMP9 and MMP14 codependently drive bone resorption.
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“Only the deletion of both MMP9 and MMP14 generated a reduction in bone resorption areas and in type I collagenolysis activity.153”
From Bone remodeling: an operational process ensuring survival and bone mechanical competence (2022) · cites this paper as [153]
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Cites
Exploration, normalization, and summaries of high density oligonucleotide array probe level data
Irizarry, R. A. (2003) · Biostatistics · doi:10.1093/biostatistics/4.2.249 · Cited by 10,603
Osteoclast differentiation and activation
Boyle, W. J., Simonet, W. S., & Lacey, D. L. (2003) · Nature · doi:10.1038/nature01658 · Cited by 6,670 · cited 1×
“In addition, alkaline shifts have been predicted to occur within the osteoclast-bone matrix interface during the demineralization process (3).”
BackgroundMacrophage biology in development, homeostasis and disease
Wynn, T. A., Chawla, A., & Pollard, J. W. (2013) · Nature · doi:10.1038/nature12034 · Cited by 4,684 · cited 1×
“Although Csf1r-Cre expression extends beyond osteoclasts to include a number of myeloid cell–derived cell populations (30, 65, 66), each of the defects we”
BackgroundRemodelling the extracellular matrix in development and disease
Bonnans, C., Chou, J., & Werb, Z. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3904 · Cited by 4,367 · cited 8×
“Coincident with this process, osteoclasts mobilize proteinases whose functions are most commonly linked to the degradation of triple-helical type I collagen, the dominant extracellular matrix (ECM) component found in the bone (1).”
BackgroundMethodInfluentialOsteoporosis: now and the future
Rachner, T. D., Khosla, S., & Hofbauer, L. C. (2011) · The Lancet · doi:10.1016/s0140-6736(10)62349-5 · Cited by 2,696
Dempster, D. W., Compston, J. E., Drezner, M. K., Glorieux, F. H., Kanis, J. A., Malluche, H., Meunier, P. J., Ott, S. M., Recker, R. R., & Parfitt, A. M. (2013) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.1805 · Cited by 2,543
Osteoimmunology: shared mechanisms and crosstalk between the immune and bone systems
Takayanagi, H. (2007) · Nature Reviews Immunology · doi:10.1038/nri2062 · Cited by 1,878
Monocytes and macrophages: developmental pathways and tissue homeostasis
Ginhoux, F., & Jung, S. (2014) · Nature Reviews Immunology · doi:10.1038/nri3671 · Cited by 1,840
Vu, T. H., Shipley, J. M., Bergers, G., Berger, J. E., Helms, J. A., Hanahan, D., Shapiro, S. D., Senior, R. M., & Werb, Z. (1998) · Cell · doi:10.1016/s0092-8674(00)81169-1 · Cited by 1,737
Genetic regulation of osteoclast development and function
Teitelbaum, S. L., & Ross, F. P. (2003) · Nature Reviews Genetics · doi:10.1038/nrg1122 · Cited by 1,720
Cited by
Sorted by citations
Osteoblast-Osteoclast Communication and Bone Homeostasis
Kim, J., Lin, C., Stavre, Z., Greenblatt, M. B., & Shim, J. (2020) · Cells · doi:10.3390/cells9092073 · Cited by 1,266
A guide to the composition and functions of the extracellular matrix
Karamanos, N. K., Theocharis, A. D., Piperigkou, Z., Manou, D., Passi, A. G., Skandalis, S. S., Vynios, D. H., Orian‐Rousseau, V., Ricard‐Blum, S., Schmelzer, C. E. H., et al. (2021) · FEBS Journal · doi:10.1111/febs.15776 · Cited by 1,177
Matrix Metalloproteinases Shape the Tumor Microenvironment in Cancer Progression
Niland, S., Riscanevo, A. X., & Eble, J. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010146 · Cited by 546
Bone remodeling: an operational process ensuring survival and bone mechanical competence
Bolamperti, S., Villa, I., & Rubinacci, A. (2022) · Bone Research · doi:10.1038/s41413-022-00219-8 · Cited by 482
“Only the deletion of both MMP9 and MMP14 generated a reduction in bone resorption areas and in type I collagenolysis activity.(153) The fusion of the earliest osteoclast precursors into multinucleated, mature osteoclasts is a critical process in osteoclastogenesis, as the number of nuclei per cell determines osteoclas…”
BackgroundOsteoimmunity‐Regulating Biomimetically Hierarchical Scaffold for Augmented Bone Regeneration
Zhang, J. C., Tong, D., Song, H., Ruan, R., Sun, Y., Lin, Y., Wang, J., Hou, L., Dai, J., Ding, J., et al. (2022) · Advanced Materials · doi:10.1002/adma.202202044 · Cited by 350
Mukherjee, A., & Das, B. (2024) · Biomaterials and Biosystems · doi:10.1016/j.bbiosy.2024.100090 · Cited by 212
“(1) Matrix metalloproteinase-1 (MMP-1) MMP-1 is considered the prototype for all interstitial collagenases and fibroblast collagenases [22,191,208,209].”
BackgroundChen, M., Wang, D., Li, M., He, Y., He, T., Chen, M., Hu, Y., Luo, Z. Y., & Cai, K. (2022) · ACS Nano · doi:10.1021/acsnano.2c07200 · Cited by 149
Hu, L., Liu, R., & Zhang, L. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.109095 · Cited by 137
Jann, J., Gascon, S., Roux, S., & Faucheux, N. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21207597 · Cited by 133
“Furthermore, it was recently shown that the deletion of both Mmp9 and Mmp14 genes in bone-marrow-derived myeloid cells altered the bone resorption activity of osteoclasts [85].”
BackgroundRANKL-responsive epigenetic mechanism reprograms macrophages into bone-resorbing osteoclasts
Bae, S., Kim, K., Kang, K., Kim, H., Lee, M. J., Oh, B., Kaneko, K., Ma, S., Choi, J., Kwak, H., et al. (2022) · Cellular and Molecular Immunology · doi:10.1038/s41423-022-00959-x · Cited by 104
“Notably, SEs formed after RANKL treatment were located in the vicinity of NFATC1, a master regulator of osteoclastogenesis [15], and key regulators of osteoclast differentiation, such as MYC [54], PR/SET domain 1 (PRDM1) [55], and matrix metalloproteinase-9 (MMP9) [56] (Fig.”
BackgroundEpigenetic and transcriptional regulation of osteoclast differentiation
Kurotaki, D., Yoshida, H., & Tamura, T. (2020) · Bone · doi:10.1016/j.bone.2020.115471 · Cited by 101
The osteoclast cytoskeleton – current understanding and therapeutic perspectives for osteoporosis
Blangy, A., Bompard, G., Guerit, D., Marie, P., Maurin, J., Morel, A., & Vives, V. (2020) · Journal of Cell Science · doi:10.1242/jcs.244798 · Cited by 76
Mazzoni, E., Mazziotta, C., Iaquinta, M. R., Lanzillotti, C., Fortini, F., D’Agostino, A., Trevisiol, L., Nocini, R., Bròdano, G. B., Mescola, A., et al. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.610570 · Cited by 67
Radzki, D., Negri, A., Kusiak, A., & Obuchowski, M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25052763 · Cited by 77
“…in bone ECM degradation; however, it was found that in CTSK-null mice as well as CTSK-mutant humans, collagen degradation is continued, which is a result of a CTSK-independent collagenolytic sys-tem in osteoclasts, associated with MMP-9 and MMP-14, as Zhu and colleagues found in their study [283].”
BackgroundSARS-CoV-2 infection induces inflammatory bone loss in golden Syrian hamsters
Qiao, W., Lau, H. E., Xie, H., Poon, V. K., Chan, C. C., Chu, H., Yuan, S., Yuen, T. T., Chik, K. K., Tsang, J. O., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-30195-w · Cited by 62
Xu, F., Deng, T., Li, W., Ai, Y., Wu, J., Yang, Y., He, C., Yang, K., Li, L., Dai, F., et al. (2023) · Chemical Engineering Journal · doi:10.1016/j.cej.2023.147195 · Cited by 64
An integrated multi-omics analysis reveals osteokines involved in global regulation
Liang, W., Wei, T., Hu, L., Chen, M., Tong, L., Zhou, W., Duan, X., Zhao, X., Zhou, W., Jiang, Q., et al. (2024) · Cell Metabolism · doi:10.1016/j.cmet.2024.03.006 · Cited by 67
Integrated Osteoinductive Factors─Exosome@MicroRNA-26a Hydrogel Enhances Bone Regeneration
Kuang, H., Ma, J., Chi, X., Fu, Q., Zhu, Q., Cao, W., Zhang, P., & Xie, X. (2023) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.2c21933 · Cited by 56
Nørregaard, K. S., Jürgensen, H. J., Gårdsvoll, H., Engelholm, L. H., Behrendt, N., & Søe, K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22136865 · Cited by 56
Mathavan, N., Singh, A., Marques, F. C., Günther, D., Kuhn, G. A., Wehrle, E., & Müller, R. (2025) · Science Advances · doi:10.1126/sciadv.adp8496 · Cited by 59
Acetylcholine‐synthesizing macrophages in subcutaneous fat are regulated by β2‐adrenergic signaling
Knights, A. J., Liu, S., Ma, Y., Nudell, V., Perkey, E., Sorensen, M. J., Kennedy, R. T., Maillard, I. P., Li, Y., Jun, H., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2020106061 · Cited by 47
“BMDMs were cultured based on previously performed protocols (Knights et al , 2016; Knights et al , 2020b; Zhu et al , 2020).”
Shi, Y., Shu, H., Wang, X., Zhao, H., Lu, C. C., Lü, A., & He, X. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.561962 · Cited by 43
Redefining metalloproteases specificity through network proteolysis
Kollet, Ó., Das, A., Karamanos, N. K., Keller, U. A. D., & Sagi, I. (2023) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2023.11.001 · Cited by 43
Antimicrobial and enzyme-responsive multi-peptide surfaces for bone-anchored devices
Fischer, N. G., Chen, X., Astleford, K., He, J., Mullikin, A. F., Mansky, K. C., & Aparicio, C. (2021) · Materials Science and Engineering C · doi:10.1016/j.msec.2021.112108 · Cited by 39
Li, Y., Chen, C., Trinh‐Minh, T., Zhu, H., Matei, A., Györfi, A., Kuwert, F., Hubel, P., Ding, X., Manh, C. T., et al. (2022) · Bone Research · doi:10.1038/s41413-022-00218-9 · Cited by 46
Bone metabolism regulation: Implications for the treatment of bone diseases
Yao, D., Huang, L., Ke, J., Zhang, M., Xiao, Q., & Zhu, X. M. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110494 · Cited by 41
Redox signaling and antioxidant defense in osteoclasts
Tao, H., Li, X., Wang, Q., Yu, L., Peng, Y., Chen, W., Yang, X., Zhou, J., & Geng, D. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.12.043 · Cited by 40
Self-citationZhang, Y., Ma, S., Nie, J., Liu, Z., Chen, F., Li, A., & Pei, D. (2023) · Small · doi:10.1002/smll.202207951 · Cited by 35
Ng, P. Y., Ribet, A. B. P., Guo, Q., Mullin, B. H., Tan, J., Landao‐Bassonga, E., Stephens, S., Chen, K., Yuan, J., Abudulai, L. N., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36484-2 · Cited by 36
Yang, R., Yu, W., Lu, L., Cui, Z., Tang, J., Li, G., Jin, M., Gu, Y., & Lu, E. (2024) · Journal of Advanced Research · doi:10.1016/j.jare.2024.07.031 · Cited by 31
“And no significant difference in bone formation was observed among the three groups within each model (Supplementary Data 3).”
InfluentialInsights into the mechanism of vascular endothelial cells on bone biology
Yin, Y., Tang, Q., Xie, M., Li, H., & Chen, L. (2021) · Bioscience Reports · doi:10.1042/bsr20203258 · Cited by 29
Membrane-type I matrix metalloproteinase (MT1-MMP), lipid metabolism and therapeutic implications.
Xia, X.-D., Alabi, A., Wang, M., Gu, H.-M., Yang, R. Z., Wang, G.-Q., & Zhang, D.-W. (2021) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjab048 · Cited by 29
Zheng, H., Deng, Y., Ли, Б., Huang, J., Liu, J., Yang, Y., Chen, Y., Mao, L., Li, Y., Liu, Y., et al. (2025) · Bone and Joint Research · doi:10.1302/2046-3758.1411.bjr-2025-0259.r1 · Cited by 32
“46 CTSK, the most abundantly expressed and potent cysteine protease in osteoclasts, serves as a key enzyme during bone resorption.”
Mouse mutant phenotyping at scale reveals novel genes controlling bone mineral density
Swan, A., Schütt, C., Rozman, J., Moreno, M. D. M. M., Brandmaier, S., Simon, M., Leuchtenberger, S., Griffiths, M. N. D., Brommage, R., Keskivali-Bond, P., et al. (2020) · PLoS Genetics · doi:10.1371/journal.pgen.1009190 · Cited by 27
“Our final selection of bone turnover genes was supported by published data [60–62].”
Bone sialoprotein promotes lung cancer osteolytic bone metastasis via MMP14-dependent mechanisms
Chen, W.-C., Chang, A., Tsai, H., Liu, P., Huang, C., Guo, J., Liu, C., Liu, J., Thuong, L. H. H., & Tang, C. (2023) · Biochemical Pharmacology · doi:10.1016/j.bcp.2023.115540 · Cited by 28
Jia, Z., Zhang, S., & Li, W. (2023) · International Journal of Nanomedicine · doi:10.2147/ijn.s424731 · Cited by 27
“When osteoclastic activity surpasses osteoblastic bone formation over an extended period, there is a net loss of bone tissue, mineral content, and matrix proteins such as collagen.(101) Consequently, the microarchitectural structure of bones deteriorates, compromising their strength and load-bearing capacity.”
BackgroundA functional three-dimensional microphysiological human model of myeloma bone disease
Visconti, R. J., Kolaja, K. L., & Cottrell, J. A. (2020) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.4404 · Cited by 29
“Two proteolytic enzymes, Cathepsin K, the major protease secreted fromOCs during bone resorption,((34,35)) andmatrixmetalloproteinase 9 (MMP-9), a collagenase essential for osteoclastic invasion,((34,36,37)) were >100-fold higher in OCs and were sevenfold and 30-fold higher respectively in 3D-NBFs (p ≤ 0.”
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Krasnova, O. A., & Neganova, I. E. (2023) · Stem Cell Reviews and Reports · doi:10.1007/s12015-023-10558-6 · Cited by 26
“Western Blot Cathepsin K MMP9 alpha(v)beta(3) integrin [201, 207, 208]”
BackgroundLee, C.-G., Kim, J., Yun, S. H., Hwang, S., Jeon, H., Park, E., & Jeong, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910642 · Cited by 25
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BackgroundBone Health Management in the Continuum of Prostate Cancer Disease
Boopathi, E., Birbe, R., Shoyele, S., Den, R. B., & Thangavel, C. (2022) · Cancers · doi:10.3390/cancers14174305 · Cited by 24
Salehi, S., Brambilla, S., Rasponi, M., Lopa, S., & Moretti, M. (2024) · Advanced Healthcare Materials · doi:10.1002/adhm.202402350 · Cited by 25
Wang, P., Husch, J. F. A., Arntz, O. J., van der Kraan, P. M., van de Loo, F. A. J., & van den Beucken, J. J. J. P. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02156-5 · Cited by 24
“Recently, Lingxin et al . observed that the double knockout of Mmp9/conditional Mmp14 mice exhibited decreased homeostatic bone turnover and were shielded from pathological bone loss [64].”
Huang, Q., Liu, M.-C., Zhang, D., Lin, B.-B., Fu, X., Zhang, Z., Zhang, B., & Dong, J. (2023) · BMC Medicine · doi:10.1186/s12916-023-02763-4 · Cited by 26
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Zhu, L., Tang, Y., Li, X., Kerk, S. A., Lyssiotis, C. A., Feng, W., Sun, X., Hespe, G. E., Wang, Z., Stemmler, M. P., et al. (2023) · The EMBO Journal · doi:10.15252/embj.2022111148 · Cited by 25
Self-citationIngvarsen, S., Gårdsvoll, H., van Putten, S., Nørregaard, K. S., Krigslund, O., Meilstrup, J. A., Tran, C. L., Jürgensen, H. J., Melander, M. C., Nielsen, C. H., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-75995-6 · Cited by 23
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
“55 MMP9 is expressed by osteoclasts and is an essential type of gelatinase associated with osteoclast migration.”
BackgroundLysosomal biogenesis and function in osteoclasts: a comprehensive review
Jiang, J., Ren, R., Fang, W., Miao, J., Wen, Z., Wang, X., Xu, J., & Jin, H. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1431566 · Cited by 23
Chu, T. L., Chen, P., Yu, A. X., Kong, M., Tan, Z., Tsang, K. Y., Zhou, Z., & Cheah, K. S. E. (2023) · eLife · doi:10.7554/elife.82142 · Cited by 20
Feng, S., Huang, Y., Yeh, K., & Pan, S. (2020) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/clinem/dgaa864 · Cited by 22
Rana, N., Suliman, S., Mohamed‐Ahmed, S., Gavasso, S., Gjertsen, B. T., & Mustafa, K. (2021) · Acta Biomaterialia · doi:10.1016/j.actbio.2021.12.027 · Cited by 22
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Jehan, F., Zarka, M., de la Houssaye, G., Véziers, J., Ostertag, A., Cohen-Solal, M. E., & Geoffroy, V. (2022) · FASEB BioAdvances · doi:10.1096/fba.2021-00092 · Cited by 22
Liang, M., Zhou, L., Li, J., Liang, B., Zhou, L.-Y., Xue, F., Jiang, L., & Hong, W. (2025) · Regenerative Biomaterials · doi:10.1093/rb/rbaf028 · Cited by 20
“MMP9 and CTSK have been established as osteo-clast marker proteins [17–19].”
Osteoclasts control endochondral ossification via regulating acetyl-CoA availability
Deng, D., Liu, X., Huang, W., Yuan, S., Liu, G., Ai, S., Fu, Y., Xu, H., Zhang, X., Li, S., et al. (2024) · Bone Research · doi:10.1038/s41413-024-00360-6 · Cited by 22
Comparative antler proteome of sika deer from different developmental stages
Zhang, R.-R., Li, Y., & Xing, X.-M. (2021) · Scientific Reports · doi:10.1038/s41598-021-89829-6 · Cited by 19
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Lin, Y., Jiang, S., Yao, Y., Li, H., Jin, H., Yang, G., Ji, B., & Li, Y. (2025) · MedComm · doi:10.1002/mco2.70159 · Cited by 18
“Osteoclasts, responsible for bone resorption, are derived from hematopoietic stem cells [18].”
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Kalev‐Altman, R., Janssen, J. N., Ben-Haim, N., Levy, T., Shitrit-Tovli, A., Milgram, J., Shahar, R., Sela‐Donenfeld, D., & Ornan, E. M. (2022) · Matrix Biology · doi:10.1016/j.matbio.2022.10.002 · Cited by 18
Krishna, V. S., Subashini, V., Hariharan, A., Chidambaram, D., Raaju, A. L., Gopichandran, N., Nanthanalaxmi, M., Lekhavadhani, S., Shanmugavadivu, A., & Selvamurugan, N. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.137625 · Cited by 17
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Zhu, L., Tang, Y., Li, X.-Y., Kerk, S. A., Lyssiotis, C. A., Sun, X., Wang, Z., Cho, J., Ma, J., & Weiss, S. J. (2023) · The Journal of Cell Biology · doi:10.1083/jcb.202206121 · Cited by 18
“However, whereas wild-type osteoclasts retain significant bone collagenolytic activity in the absence of CTSK activity, the cysteine proteinase inhibitor E-64d almost completely inhibits the collagen-degradative activity of GCS-100 – or RAP-treated DKO osteoclasts as assessed by the release of the type I collagen cros…”
InfluentialSelf-citationTang, Y., Zhu, L.-X., Cho, J., Li, X.-Y., & Weiss, S. (2022) · Developmental Cell · doi:10.1016/j.devcel.2022.01.015 · Cited by 13
Self-citationHuang, M.-L., Liu, H., Zhu, L., Li, X., Li, J., Yang, S., Liu, D., Song, X., Yokota, H., & Zhang, P. (2021) · Journal of Cellular Physiology · doi:10.1002/jcp.30314 · Cited by 15
“induced osteoclastogenesis by decreasing the activities of cathepsin K and matrix metalloproteinases that are mostly secreted by mature osteoclasts (Zhu et al., 2020).”
BackgroundSelf-citationOstm1 from Mouse to Human: Insights into Osteoclast Maturation
Vacher, J., Bruccoleri, M., & Pata, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21165600 · Cited by 15
“In the lacunae, rel ase from secretory lys som s of tartrate resistant acid phosphatase (Trap), matrix metallo eptidases (Mmp 9,14) [19], and cathepsin K (Ctsk) result in steoid degradation which is principally type I collagen [20] whereas high acidity potentiates dissolution of hydroxy patite, the bone mineral comp n…”
BackgroundPark, E., Sozański, T., Lee, C.-G., Kucharska, A. Z., Przybylska, D., Piórecki, N., & Jeong, S. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/4122253 · Cited by 15
“Bone resorption resulting from osteoclast di ff erentiation is regulated by osteoclast-related enzymes, such as tartrate-resistant acid phosphatase 5 (Acp5) and cathepsin K (Ctsk) [41].”
Ye, W., Liao, Y.-L., Liu, X., Wang, Y., Li, T., Zhao, Y., He, Z., Chen, J., Yin, M., Sheng, Y., et al. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.01.011 · Cited by 14
Wang, Y., Li, X., Deng, F., & Yin, R. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.734539 · Cited by 14
“…expression levels of osteoclast differentiation markers RANKL, RANK (Park et al., 2017), and TRAF6/ NFATc1/c-fos pathway (Kim et al., 2012; Chen et al., 2021), and decreased the protein expression levels of osteolysis related proteins CTSK (Lotinun et al., 2013), and MMP-9 (Zhu et al., 2020).”
BackgroundInfluentialSelf-citationYu, F., Huo, F., Li, F., Zuo, Y., Wang, C., & Ye, L. (2022) · International Journal of Oral Science · doi:10.1038/s41368-022-00159-3 · Cited by 14
“Matrix metalloproteinases (Mmps) and Cathepsin K (Ctsk) constitute a compensatory but parallel network to orchestrate OCs-mediated bone resorption.(12) But with respect to the roles of Mmps and Ctsk in pulp-dentin remodeling or inflammatory resorption, evidences and mechanisms are far unclear.”
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A novel method to efficiently differentiate human osteoclasts from blood-derived monocytes
Chandrabalan, S., Dang, L., Hansen, U. J., Timmen, M., Wehmeyer, C., Stange, R., Beißbarth, T., Binder, C. R., Bleckmann, A., & Menck, K. (2024) · Biological Procedures Online · doi:10.1186/s12575-024-00233-6 · Cited by 13
“Increased expression of MMP9 , MMP14 and ATP6V0A1 has been associated with late stage osteoclastogenesis and all genes are essential for the bone resorption activity of osteoclasts [24, 47].”
BackgroundXu, C., Qiu, S., Yuan, Z., Qiu, C., Xu, W., Guo, J., Wen, G., Liu, S., Yan, W., Xu, H., et al. (2025) · Advanced Science · doi:10.1002/advs.202500144 · Cited by 12
Liu, R., Imangali, N., Ethiraj, L. P., Carney, T. J., & Winkler, C. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.775512 · Cited by 11
Castro, D. M., Lamana, A., Arribas‐Castaño, P., Gutiérrez‐Cañas, I., Villanueva‐Romero, R., Pérez‐García, S., Martínez, C., Juarranz, Y., de Córdoba‐Oñate, S. F., González‐Álvaro, I., et al. (2021) · Biomedicines · doi:10.3390/biomedicines9121880 · Cited by 11
Jun, H., Liu, S., Knights, A. J., Zhu, K., Ma, Y., Gong, J., Lenhart, A. E., Peng, X., Huang, Y., Ginder, J. P., et al. (2024) · PLoS Biology · doi:10.1371/journal.pbio.3002728 · Cited by 11
Huang, J., Zheng, J., Dadihanc, T., Gao, Y., Zhang, Y., Li, Z., Wang, X., Yu, L., Mijiti, W., Xie, Z., et al. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116214 · Cited by 10
Knapinska, A. M., Singh, C., Drotleff, G., Blanco, D., Chai, C., Schwab, J., Herd, A., & Fields, G. (2020) · ChemMedChem · doi:10.1002/cmdc.202000911 · Cited by 10
The emerging role of tranexamic acid and its principal target, plasminogen, in skeletal health
Xie, W., Donat, A., Jiang, S., Baranowsky, A., & Keller, J. (2024) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2024.03.033 · Cited by 9
Steinberg, T., Jung, B. A., Husari, A., Bai, S., & Tomakidi, P. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26178203 · Cited by 9
Xin, Y., Zhao, N., & Wang, Y. (2022) · Archives of Oral Biology · doi:10.1016/j.archoralbio.2022.105484 · Cited by 10
Bone Material Properties in Bone Diseases Affecting Children
Raimann, A., Misof, B. M., Fratzl, P., & Fratzl‐Zelman, N. (2023) · Current Osteoporosis Reports · doi:10.1007/s11914-023-00822-6 · Cited by 9
MMP-9 Expression in bone cells in the developing femur
Mustafa, F. E. A., Abd‐Elhafeez, H. H., Taha, R. S., Osman, A., Almaki, M. M., Baker, Z. M., Alghamdi, A. A. A., Massoud, D., Elmasry, M., Soliman, S. A., et al. (2025) · Tissue and Cell · doi:10.1016/j.tice.2025.102862 · Cited by 8
Tong, X., Min, W., Li, S., Chen, M., Song, R., Bian, J., Gu, J., & Liu, Z. (2021) · Differentiation · doi:10.1016/j.diff.2021.08.003 · Cited by 8
Ji, L., Kong, R., Yu, Y., Wan, W., Zhao, D., & Gao, J. (2025) · Molecular Immunology · doi:10.1016/j.molimm.2025.06.002 · Cited by 8
Osteoporotic Fractures of the Proximal Humerus: an In-Depth Review of Current Management Options
Girgin, A. B., Acar, A., Torun, Ö., & Çevi̇k, H. B. (2025) · Current Osteoporosis Reports · doi:10.1007/s11914-025-00945-y · Cited by 7
Marx, D., Anglicheau, D., Caillard, S., Moulin, B., Kochman, A., Mischak, H., Latosińska, A., Bienaimé, F., Prié, D., Marquet, P., et al. (2023) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.202200118 · Cited by 7
“COL1A1 is also a known substrate of MMP9 a protease required for bone repair following fractures and involved in bone resorption in combination with other matrix metalloproteinases [74, 75].”
BackgroundCoding and noncoding RNA profile of human heterotopic ossifications - Risk factors and biomarkers
Mierzejewski, B., Pulik, Ł., Grabowska, I., Sibilska, A., Ciemerych, M. A., Łęgosz, P., & Brzóska, E. (2023) · Bone · doi:10.1016/j.bone.2023.116883 · Cited by 7
Domingues, M. F., Silva, J. C., & Sanjuan‐Alberte, P. (2024) · Advanced Therapeutics · doi:10.1002/adtp.202400047 · Cited by 8
Yang, D., Tan, Y., Xi, X., Xiao, W., & Kang, J. U. (2023) · International Immunopharmacology · doi:10.1016/j.intimp.2023.109720 · Cited by 7
Martiniaková, M., Kováčová, V., Bíro, R., Mondočková, V., Šarocká, A., Pénzes, N., Folwarczna, J., & Omelka, R. (2025) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.118063 · Cited by 9
Bauer, J., Duero, J., & Lindsay, A. D. (2025) · Current Osteoporosis Reports · doi:10.1007/s11914-025-00922-5 · Cited by 6
“Osteoclasts are derived from hematopoietic stem cells and are primarily responsible for resorption of old bone [28–31].”
Protein Ca2+-Sites Prone to Sr2+ Substitution: Implications for Strontium Therapy
Mazmanian, K., Grauffel, C., Dudev, T., & Lim, C. (2023) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.3c01637 · Cited by 8
Lv, X., Lin, Y., Zhang, Z., Li, B., Zeng, Z., Jiang, X., Zhao, Q., Li, W., Wang, Z., Yang, C., et al. (2023) · BMC Genomics · doi:10.1186/s12864-023-09449-4 · Cited by 6
“[42] identified a cathepsin K-independent collagenolytic system in osteoclasts, which was composed of a functionally redundant network of the secreted matrix metalloproteinase MMP9 and the membrane-anchored matrix metalloproteinase MMP14.”
BackgroundIngwersen, L.-C., Ahlhelm, M., Schwarzer-Fischer, E., Kurz, S., Riemer, E., Naujokat, H., Loger, K., Bader, R., & Jonitz‐Heincke, A. (2024) · Materials & Design · doi:10.1016/j.matdes.2024.112687 · Cited by 6
Yang, G., Ye, J., Wang, J., Liu, H., Long, Y., Jiang, J., Miao, X., Deng, J., Wu, T., Li, T., et al. (2024) · Materials Today Bio · doi:10.1016/j.mtbio.2024.101179 · Cited by 6
“Among them, osteoclasts play a key role in the development of OP, as they are not only responsible for bone resorption, but also for destroying bone minerals and collagen by secreting acids and catabolic enzymes [4,5], which in turn leads to severe bone mineral loss.”
BackgroundKim, J., Lee, C.-G., Yun, S.-H., Hwang, S., Jeon, H., Park, E., & Jeong, S. (2022) · Medicina · doi:10.3390/medicina58040466 · Cited by 6
“The bone resorption process is regulated by various osteoclastogenesis genes, such as cathepsin K (Ctsk), tartrate-resistant acid phosphatase (Acp5, TRAP) and matrix metalloproteinase 9 (Mmp9) [43].”
BackgroundWang, C., Wang, L., Li, Q., Wu, W., Yuan, J., Wang, H., & Lu, X. (2023) · World Neurosurgery · doi:10.1016/j.wneu.2023.01.092 · Cited by 6
Brevilin A inhibits RANKL-induced osteoclast differentiation and bone resorption
Wei, J., Lin, Z., Dai, Z., Zhou, Z., Bi, Y., Zheng, R., Hu, X., Xu, Z., Yuan, G., & Wang, W. (2023) · In Vitro Cellular & Developmental Biology - Animal · doi:10.1007/s11626-023-00783-1 · Cited by 6
The HOXC10/NOD1/ERK axis drives osteolytic bone metastasis of pan-KRAS-mutant lung cancer
Li, K., Yang, B., Du, Y., Ding, Y., Shen, S., Sun, Z., Liu, Y., Wang, Y., Cao, S., Ren, W., et al. (2024) · Bone Research · doi:10.1038/s41413-024-00350-8 · Cited by 5
“24 Furthermore, qPCR was performed and substantial 67.9% – 76.3% reductions in MMP9 transcription was observed from HOXC10 knockdown cancer cells conditioned medium induced osteoclasts (Fig.”
BackgroundInfluentialPollen‐Inspired Aptamer Delivery System for Multi‐Target Therapy in Rheumatoid Arthritis
Yang, W., Chen, Z., Qu, Y., Ye, P., Tang, Y., Yu, Q., Zhang, Z., Dai, Q., Dou, C., & Luo, F. (2025) · Advanced Functional Materials · doi:10.1002/adfm.202425323 · Cited by 5
Self-citationMadel, M., Ibáñez, L., Ciucci, T., Halper, J., Boutin, A., Beldi, G., Lavanant, A. C., Garchon, H., Rouleau, M., Mueller, C. G., et al. (2024) · Mucosal Immunology · doi:10.1016/j.mucimm.2024.09.005 · Cited by 5
Echinococcus granulosus promotes bone resorption by increasing osteoclasts differentiation
Sun, H., Wang, S., Tan, W., Li, Y., Ren, Q., Liu, Y., Huang, Y., Shi, C., & Li, J. (2023) · Acta Tropica · doi:10.1016/j.actatropica.2023.107027 · Cited by 5
Chordoma cells possess bone-dissolving activity at the bone invasion front
Kawaai, K., Oishi, Y., Kuroda, Y., Tamura, R., Toda, M., & Matsuo, K. (2024) · Cellular Oncology · doi:10.1007/s13402-024-00946-6 · Cited by 5
Unraveling the Mechanisms That Regulate Osteoclast Differentiation: A Review of Current Advances
Zhang, S., Gao, M., Song, S., Zhao, T., Zhou, B.-H., Wang, H., Tian, W., Zhao, W., & Zhao, J. (2025) · genesis · doi:10.1002/dvg.70012 · Cited by 7
“These proteases, encompassing CTSK and MMP-9 that facilitate collagen fiber hydrolysis, culminate in the formation of bone resorption pits (Motyckova et al. 2001; Zhu et al. 2020).”
Metadata
- Authors
- Zhu, L., Tang, Y., Li, X.-Y., Keller, E. T., Yang, J., Cho, J.-S., Feinberg, T. Y., & Weiss, S. J.
- Affiliations
- University of Michigan (US)
- Division of Genetic Medicine, Department of Internal Medicine, University of Michigan, Ann Arbor, MI 48109, USA.
- Corresponding author
- Zhu, Lingxin
- Weiss, Stephen J.
- ORCID
- Venue
- Science Translational Medicine
- Published
- 2020-02-05
- Volume
- 12
- Issue
- 529
- ISSN
- 1946-6234 (ISSN-L)
- 1946-6242
- PMC
- PMC7603424
- OpenAlex
- W3005525925
- Cited by
- 178
- References
- 89
- Citations by year
- 2026: 30 · 2025: 31 · 2024: 34 · 2023: 25 · 2022: 24 · 2021: 18 · 2020: 15
- FWCI
- 6.65
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science Translational Medicine (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (AI105068, CA093900, CA071699, AR075168)
- Breast Cancer Research Foundation
- National Natural Science Foundation of China (81970919)
- Margolies Family Discovery Fund for Cancer Research
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bone Metabolism and Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Bone and Dental Protein Studies
- Keywords
- osteoclasts, bone resorption, metalloproteinases, MMP-9, MMP-14, collagen degradation, bone mineral density, parathyroid hormone, ovariectomy, bone loss, therapeutic target
- MeSH terms
- Animals, Bone and Bones, Bone Resorption, Cathepsins, Female, Humans, Osteoclasts, Osteoporosis, Ovariectomy, Mice
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