Proteolysis of the collagen fibril in osteoarthritis
Abstract
The development of cartilage pathology in osteoarthritis involves excessive damage to the collagen fibrillar network, which appears to be mediated primarily by the chondrocyte-generated cytokines interleukin-1 and tumour necrosis factor α and the collagenases matrix metalloproteinase-1 (MMP-1) and MMP-13. The damage to matrix caused by these and other MMPs can result in the production of sufficient degradation products that can themselves elicit further degradation, leading to chondrocyte differentiation and eventually matrix mineralization and cell death. Knowledge of these MMPs, cellular receptors and cytokine pathways, and the ability to selectively antagonize them by selective blockade of function, may provide valuable therapeutic opportunities in the treatment of osteoarthritis and other joint diseases involving cartilage resorption, such as rheumatoid arthritis. The ability to detect the products of these degradative events released into body fluids of patients may enable us to monitor disease activity, predict disease progression and determine more rapidly the efficacy of new therapeutic agents.
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ADAMTS-4 and ADAMTS-5 are implicated prominently in cartilage breakdown during OA.
“During OA, ADAMTS-4 (aggrecanase 1) [28] and ADAMTS-5 (aggrecanase 2) [29,30] have been implicated prominently in cartilage breakdown.”
From Arthropod steroid hormone (20-Hydroxyecdysone) suppresses IL-1β- induced catabolic gene expression in cartilage (2015) · cites this paper as [28]
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Roos, E. M., & Dahlberg, L. (2005) · Arthritis & Rheumatism · doi:10.1002/art.21415 · Cited by 475 · see citing works
“as in cartilage disease, insufficient viscoelasticity may cause progressive denaturation of collagen molecules, collagen loss, and subsequent development of OA (37).”
BackgroundSelf-citationRole of matrix vesicles in biomineralization
Golub, E. E. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.09.006 · Cited by 394 · see citing works
Dreier, R. (2010) · Arthritis Research & Therapy · doi:10.1186/ar3117 · Cited by 357 · see citing works
Reciprocal inhibition of YAP/TAZ and NF-κB regulates osteoarthritic cartilage degradation
Deng, Y.-J., Lu, J., Li, W., Wu, A.-L., Zhang, X., Tong, W.-X., Ho, K., Qin, L., Song, H., & Mak, K. K. (2018) · Nature Communications · doi:10.1038/s41467-018-07022-2 · Cited by 305 · see citing works
Syndecan-4 regulates ADAMTS-5 activation and cartilage breakdown in osteoarthritis
Echtermeyer, F. G., Bertrand, J., Dreier, R., Meinecke, I., Neugebauer, K., Fuerst, M. E., Lee, Y. J., Song, Y. W., Herzog, C., Theilmeier, G., et al. (2009) · Nature Medicine · doi:10.1038/nm.1998 · Cited by 318 · see citing works
Caveolin-1-dependent β1 integrin endocytosis is a critical regulator of fibronectin turnover
Shi, F., & Sottile, J. (2008) · Journal of Cell Science · doi:10.1242/jcs.014977 · Cited by 238 · see citing works
“Impaired or abnormal degradation and removal of ECM components contributes to the onset and progression of many diseases, including fibrosis, arthritis and cancer (Hotary et al., 2003; Kurban et al., 2006; Liotta and Kohn, 2001; Mutsaers et al., 1997; Poole et al., 2003).”
BackgroundOxidative-stress and IL-6 mediate the fibrogenic effects of rodent Kupffer cells on stellate cells
Nieto, N. (2006) · Hepatology · doi:10.1002/hep.21427 · Cited by 227 · see citing works
Young, D. A., Lakey, R., Pennington, C. J., Jones, D., Kevorkian, L., Edwards, D. R., Cawston, T. E., & Clark, I. M. (2005) · Arthritis Research & Therapy · doi:10.1186/ar1702 · Cited by 191 · see citing works
Sheu, S.-Y., Ho, S.-R., Sun, J.-S., Chen, C.-Y., & Ke, C.-J. (2015) · BMC Complementary and Alternative Medicine · doi:10.1186/s12906-015-0520-z · Cited by 181 · see citing works
“During OA, ADA MTS-4 (aggrecanase 1) [28] and ADAMTS-5 (aggrecanase 2) [29,30] have been implicated prominently in cartilage breakdown.”
BackgroundOverview of Rheumatoid Arthritis and Scientific Understanding of the Disease
Jahid, M., Khan, K., Rehan-Ul-Haq, & Ahmed, R. S. (2023) · Mediterranean Journal of Rheumatology · doi:10.31138/mjr.20230801.oo · Cited by 158 · see citing works
“78 TNF-α is considered an autocrine stimulator and a paracrine inducer of IL-1 and granulocyte macrophage colony stimulating factor (GM-CSF).”
BackgroundManicourt, D., Azria, M., Mindeholm, L., Thonar, E. J. ‐., & Devogelaer, J. (2006) · Arthritis & Rheumatism · doi:10.1002/art.22075 · Cited by 135 · see citing works
Effect of oral glucosamine on cartilage degradation in a rabbit model of osteoarthritis
Tiraloche, G., Girard, C. A., Chouinard, L., et al. (2005) · Arthritis & Rheumatism · doi:10.1002/art.20951 · Cited by 125 · see citing works
Self-citationWhat are the roles of metalloproteinases in cartilage and bone damage?
Murphy, G., & Lee, M. H. (2005) · Annals of the Rheumatic Diseases · doi:10.1136/ard.2005.042465 · Cited by 119 · see citing works
Collagen I matrix turnover is regulated by fibronectin polymerization
Shi, F., Harman, J. J., Fujiwara, K., et al. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00341.2009 · Cited by 115 · see citing works
The Future of Osteoarthritis Therapeutics: Targeted Pharmacological Therapy
Mobasheri, A. (2013) · Current Rheumatology Reports · doi:10.1007/s11926-013-0364-9 · Cited by 109 · see citing works
“This mechanism causes the extensive damage to the collagen fibrillar network observed in OA cartilage pathology which seems to be mediated primarily by the collagenases MMP-1 and MMP-13 [88].”
BackgroundGarcía-Arnandis, I., Guillén, M. I., Sancho, F. G., Pelletier, J., Martel‐Pelletier, J., & Alcaraz, M. J. (2010) · Arthritis Research & Therapy · doi:10.1186/ar3124 · Cited by 106 · see citing works
“As MMP-1 degrades collagens in the extracellular matrix [46-48] and MMP-3 activity leads to activation of collagenases [49], our results suggest the amplification of catabolic responses by HMGB1 during joint inflammation.”
BackgroundCharni, N., Juillet, F., & Garnero, P. (2005) · Arthritis & Rheumatism · doi:10.1002/art.20930 · Cited by 95 · see citing works
Céleste, C., Ionescu, M., Poole, A. R., et al. (2004) · Journal of Orthopaedic Research® · doi:10.1016/j.orthres.2004.10.003 · Cited by 95 · see citing works
Self-citationDevelopmental Mechanisms in Articular Cartilage Degradation in Osteoarthritis
Tchetina, E. V. (2010) · Arthritis · doi:10.1155/2011/683970 · Cited by 93 · see citing works
“This suggests common regulatory mechanisms of matrix degradation in OA and in the development and can provide new approaches for the treatment of the disease by targeting reparation of chondrocyte phenotype.”
BackgroundSelf-citationTRPV4 as a therapeutic target for joint diseases
McNulty, A. L., Leddy, H. A., Liedtke, W., & Guilak, F. (2014) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-014-1078-x · Cited by 94 · see citing works
“Proteolytic pathogenesis has been elucidated in rheumatoid arthritis, as well as in osteoarthritis (Opdenakker et al. 1991; Poole et al. 2003; Rannou et al. 2006; Connor et al. 2012; Troeberg and Nagase 2012).”
BackgroundMolecular mechanisms of cartilage remodelling in osteoarthritis
Bertrand, J., Cromme, C., Umlauf, D., Frank, S., & Pap, T. (2010) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2010.06.022 · Cited by 92 · see citing works
What's New in Orthopaedic Research
Rodeo, S. A. (2005) · Journal of Bone and Joint Surgery · doi:10.2106/jbjs.e.00569 · Cited by 89 · see citing works
Cao, K., Wei, L., Zhang, Z.-Q., Guo, L., Zhang, C.-M., Li, Y.-P., Sun, C.-Q., Sun, X.-J., Wang, S.-W., Li, P., et al. (2014) · Arthritis Research & Therapy · doi:10.1186/s13075-014-0491-3 · Cited by 84 · see citing works
“Type X collagen and MMP-13 are markers for chondrocyte hypertrophy, and MMP-13 is a primary player in OA cartilage damage [32,34-36].”
BackgroundWest, P. A., Torzilli, P. A., Chen, C., et al. (2005) · Journal of Biomedical Optics · doi:10.1117/1.1854131 · Cited by 81 · see citing works
Venkatesha, S. H., Berman, B., & Moudgil, K. D. (2010) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2010.10.053 · Cited by 80 · see citing works
Bay‐Jensen, A., Andersen, T. L., Tabassi, N. C.-B., Kristensen, P. W., Kjærsgaard‐Andersen, P., Sandell, L. J., Garnero, P., & Delaissé, J. (2007) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2007.09.006 · Cited by 78 · see citing works
Cao, C., Shi, Y., Zhang, X., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34830-4 · Cited by 75 · see citing works
Biomarkers of cartilage turnover. Part 1: Markers of collagen degradation and synthesis
Garvican, E. R., Vaughan‐Thomas, A., Innes, J., et al. (2010) · The Veterinary Journal · doi:10.1016/j.tvjl.2010.04.011 · Cited by 75 · see citing works
Mormone, E., Lu, Y., Ge, X., Fiel, M. I., & Nieto, N. (2011) · Gastroenterology · doi:10.1053/j.gastro.2011.11.029 · Cited by 73 · see citing works
Collins, C. D., Purohit, S. B., Podolsky, R. H., Zhao, H., Schatz, D., Eckenrode, S., Yang, P., Hopkins, D., Muir, A., Hoffman, M., et al. (2006) · Vascular Pharmacology · doi:10.1016/j.vph.2006.08.003 · Cited by 65 · see citing works
“, 2000), hormonal imbalance (insulin, thyroxine, adrenaline, pituitary hormones), tissue damage (SGOTand SGPT for liver and heart, collagen for joints) (Conigrave et al., 2003; Collier and Bassendine, 2002; Poole et al., 2003), cancer (CA15.”
BackgroundGronau, T., Krüger, K., Prein, C., et al. (2016) · Annals of the Rheumatic Diseases · doi:10.1136/annrheumdis-2016-209319 · Cited by 63 · see citing works
Zhang, L., Ma, S., Su, H., & Cheng, J. (2018) · Molecular Therapy: Methods & Clinical Development · doi:10.1016/j.omtm.2018.02.006 · Cited by 58 · see citing works
Lü, G., Li, L., Wang, B., et al. (2020) · Aging · doi:10.18632/aging.102801 · Cited by 61 · see citing works
“Degradation of the collagen network a critical event in OA may result in impaired tensile strength [32, 33].”
BackgroundPattoli, M. A., MacMaster, J. F., Gregor, K. R., & Burke, J. R. (2005) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.105.087569 · Cited by 56 · see citing works
“Metalloproteinases such as MMP-1 and MMP-13 have major roles in the degradation of collagen (Poole et al., 2003), whereas the aggrecanases ADAMTS-4 and ADAMTS-5 appear to mediate the aggrecan degradation (Arner, 2002).”
BackgroundHaem oxygenase‐1 regulates catabolic and anabolic processes in osteoarthritic chondrocytes
Guillen, M. I., Megías, J., Gomar, F., & Alcaraz, M. (2008) · The Journal of Pathology · doi:10.1002/path.2313 · Cited by 55 · see citing works
Maskos, K., Lang, R., Tschesche, H., & Bode, W. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.11.072 · Cited by 55 · see citing works
Hosseininia, S., Lindberg, L., & Dahlberg, L. (2013) · BMC Musculoskeletal Disorders · doi:10.1186/1471-2474-14-18 · Cited by 54 · see citing works
“The extractable collagen pool is expressed as percentage of the total collagen amount, as previously reported [23].”
BackgroundResultSelf-citationβ1 Integrin Deficiency Results in Multiple Abnormalities of the Knee Joint
Raducanu, A., Hunziker, E. B., Drosse, I., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.039347 · Cited by 54 · see citing works
Yeh, T., Wen, Z., Lee, H.-S., et al. (2008) · European Spine Journal · doi:10.1007/s00586-008-0594-0 · Cited by 54 · see citing works
“Such damage to the matrix can lead to the production of sufficient degradation products that can cause further degradation, resulting in chondrocyte dedifferentiation, and eventually matrix mineralization and cell death [16].”
BackgroundADAM‐8 isolated from human osteoarthritic chondrocytes cleaves fibronectin at Ala 271
Zack, M. D., Malfait, A., Skepner, A. P., Yates, M. P., Griggs, D. W., Hall, T., Hills, R. L., Alston, J. T., Nemirovskiy, O. V., Radabaugh, M. R., et al. (2009) · Arthritis & Rheumatism · doi:10.1002/art.24753 · Cited by 51 · see citing works
Ryu, B., Qian, Z., & Kim, S. (2009) · Peptides · doi:10.1016/j.peptides.2009.10.019 · Cited by 51 · see citing works
Willard, V. P., Diekman, B., Sanchez‐Adams, J., Christoforou, N., Leong, K., & Guilak, F. (2014) · Arthritis & Rheumatology · doi:10.1002/art.38780 · Cited by 55 · see citing works
“These catabolic enzymes include matrix metalloproteinases (MMPs), which disrupt collagen fibers (8,9), and members of the ADAMTS family, which degrade aggrecan and release GAGs (10,11).”
BackgroundZhang, L.-Q., Zhao, G., Xu, X., et al. (2015) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2015.2114 · Cited by 49 · see citing works
“The qualitative and quantitative changes in type II collagen and proteoglycan synthesis are the direct cause of articular cartilage losing its normal biomechanical properties, having a close association with OA (25,26).”
Burton, D. W., Foster, M., Johnson, K., et al. (2005) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2005.01.002 · Cited by 46 · see citing works
Role of S100A12 in the pathogenesis of osteoarthritis
Nakashima, M., Sakai, T., Hiraiwa, H., et al. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.05.036 · Cited by 45 · see citing works
Syndecan-4 in intervertebral disc and cartilage: Saint or synner?
Binch, A. L. A., Shapiro, I. M., & Risbud, M. V. (2016) · Matrix Biology · doi:10.1016/j.matbio.2016.01.005 · Cited by 43 · see citing works
Nicoliche, T., Maldonado, D. C., Faber, J., et al. (2020) · PLoS ONE · doi:10.1371/journal.pone.0230228 · Cited by 42 · see citing works
“[5] postulated that MMP-13 activity, collagen proteolysis, and chondrocyte hypertrophy are related and that the degradation of Col2 tended to induce collagenase activity mediated by MMP-1 and MMP-13, as well as IL-1 and TNFα production.”
BackgroundAdler, N., Schoeniger, A., & Fuhrmann, H. (2017) · Journal of Animal Physiology and Animal Nutrition · doi:10.1111/jpn.12804 · Cited by 42 · see citing works
“Among these, the ADAMTSs (Tortorella et al., 2001) and the MMPs (Poole et al., 2003) play an important part.”
BackgroundInfluentialRationale for the potential use of calcitonin in osteoarthritis.
Manicourt, D.-H., Devogelaer, J. P., Azria, M., & Silverman, S. L. (2005) · PubMed · Cited by 39 · see citing works
5-aminosalicylic acid suppresses osteoarthritis through the OSCAR-PPARγ axis
Kim, J., Ryu, G., Seo, J., Go, M., Kim, G., Yi, S., Kim, S., Lee, H., Lee, J.-Y., Kim, H., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-45174-6 · Cited by 34 · see citing works
Hui, W., Barksby, H. E., Young, D. A., et al. (2005) · Annals of the Rheumatic Diseases · doi:10.1136/ard.2004.028191 · Cited by 37 · see citing works
Lysosomal Trafficking of TGFBIp via Caveolae-Mediated Endocytosis
Choi, S., Maeng, Y., Kim, T., Lee, Y., Kim, Y., & Kim, E. K. (2015) · PLoS ONE · doi:10.1371/journal.pone.0119561 · Cited by 35 · see citing works
Yang, Y., Li, P., Zhu, S., & Bi, R. (2020) · PeerJ · doi:10.7717/peerj.8934 · Cited by 33 · see citing works
“, 1996); (3) the damage process in cartilage matrix produces sufficient degradation products (MMP-13), and these products promote further degradation, resulting in matrix mineralization and death of chondrocytes (Poole et al., 2003).”
BackgroundManicourt, D.-H., Bevilacqua, M. T., Righini, V., Famaey, J. P., & Devogelaer, J. (2005) · Drugs in R&D · doi:10.2165/00126839-200506050-00002 · Cited by 32 · see citing works
García-Arnandis, I., Guillén, M. I., Castejón, M. A., et al. (2010) · Lara D. Veeken · doi:10.1093/rheumatology/kep463 · Cited by 31 · see citing works
Danalache, M., Umrath, F., Riester, R., Schwitalle, M., Guilak, F., & Hofmann, U. K. (2024) · Acta Biomaterialia · doi:10.1016/j.actbio.2024.05.002 · Cited by 31 · see citing works
Transcriptional profiling of synovium in a porcine model of early post‐traumatic osteoarthritis
Sieker, J. T., Proffen, B. L., Waller, K. A., Chin, K. E., Karamchedu, N. P., Akelman, M. R., Perrone, G. S., Kiapour, A. M., Konrad, J., Fleming, B. C., et al. (2018) · Journal of Orthopaedic Research® · doi:10.1002/jor.23876 · Cited by 28 · see citing works
Influence of age on osteoarthritis progression after anterior cruciate ligament transection in rats
Ferrándiz, M. L., Terencio, M. C., Ruhí, R., et al. (2014) · Experimental Gerontology · doi:10.1016/j.exger.2014.03.010 · Cited by 26 · see citing works
“Pro-inflammatory cytokines such as interleukin(IL)-1β and IL-17 can synergise to damage the collagen fibril network leading to degradation products that can induce further degradation and chondrocyte death (Honorati et al., 2002; Koshy et al., 2002; Poole et al., 2003).”
Age impacts extracellular matrix metabolism in chondrocytes encapsulated in degradable hydrogels
Skaalure, S. C., Milligan, I. L., & Bryant, S. J. (2012) · Biomedical Materials · doi:10.1088/1748-6041/7/2/024111 · Cited by 26 · see citing works
Fibronectin remodelling: cell-mediated regulation of the microenvironment
Wolanska, K. I., & Morgan, M. R. (2015) · Biochemical Society Transactions · doi:10.1042/bst20140313 · Cited by 25 · see citing works
Houtman, E., van Hoolwerff, M., Lakenberg, N., et al. (2021) · Rheumatology and Therapy · doi:10.1007/s40744-021-00287-y · Cited by 24 · see citing works
Therapeutic ultrasound effects on interleukin-1β stimulated cartilage construct in vitro
Park, K., Hoffmeister, B. K., Han, D. K., et al. (2007) · Ultrasound in Medicine & Biology · doi:10.1016/j.ultrasmedbio.2006.08.009 · Cited by 24 · see citing works
“Also known as collagenase-1 and 3, respectively, they destroy the architecture of collagen fibrillar network in cartilage (Poole et al. 2003).”
BackgroundCollagen biosynthesis of mechanically loaded articular cartilage explants
Ackermann, B., & Steinmeyer, J. (2005) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2005.06.001 · Cited by 21 · see citing works
Wang, Z., Qiu, Y., Lu, J., et al. (2013) · Molecular Medicine Reports · doi:10.3892/mmr.2013.1570 · Cited by 20 · see citing works
E-Health towards ecumenical framework for personalized medicine via Decision Support System
Kouris, I., Tsirmpas, C., Mougiakakou, S. G., Iliopoulou, D., & Koutsouris, D. (2010) · Annual International Conference of the IEEE Engineering in Medicine and Biology Society (EMBC) · doi:10.1109/iembs.2010.5626308 · Cited by 20 · see citing works
Samuel, S., Twizere, J., Beifuss, K. K., & Bernstein, L. R. (2007) · Molecular Carcinogenesis · doi:10.1002/mc.20358 · Cited by 16 · see citing works
“in healthy tissues is restricted to circumstances in which rapid remodeling of ECM within target tissue is required [64], particularly in development and tissue remodeling in bone and cartilage [65].”
BackgroundWHATʼS NEW IN ORTHOPAEDIC RESEARCH
Rodeo, S. A., Maher, S. A., & Hidaka, C. (2004) · Journal of Bone and Joint Surgery · doi:10.2106/00004623-200409000-00034 · Cited by 15 · see citing works
Yabluchanskiy, A., CHILTON, R. J., & Lindsey, M. L. (2013) · Congestive Heart Failure · doi:10.1111/chf.12023 · Cited by 14 · see citing works
Inhibition of hyaluronan export reduces collagen degradation in interleukin-1 treated cartilage
Deiters, B., & Prehm, P. (2008) · Arthritis Research & Therapy · doi:10.1186/ar2357 · Cited by 13 · see citing works
“Key events in osteoarthritic cartilage are increased hyaluronan, decreased aggrecan synthesis [19,21], and proteolytic cleavage of collagen type II and aggrecan core protein [22,23].”
Telomerase-transduced osteoarthritic fibroblast-like synoviocyte cell line
Sun, Y., Firestein, G. S., Wenger, L., et al. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.09.005 · Cited by 12 · see citing works
Synergetic role of TRPV4 inhibitor and mechanical loading on reducing inflammation
Babaniamansour, P., Jacho, D., Rabino, A., García‐Mata, R., & Yildirim-Ayan, E. D. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1456042 · Cited by 11 · see citing works
Xiong, X., Liu, L., Xu, F., et al. (2021) · ACS Omega · doi:10.1021/acsomega.0c06212 · Cited by 11 · see citing works
Mobasheri, A., & Henrotin, Y. E. (2011) · Recent Patents on Biomarkerse · doi:10.2174/2210309011101010025 · Cited by 11 · see citing works
“Therefore, the development of cartilage pathology in OA involves excessive damage to the collagen fibrillar network, which appears to be mediated primarily by the chondrocyte-generated cytokines IL-1 and TNF- and the collagenases matrix metalloproteinase-1 (MMP-1) and MMP-13 [80].”
BackgroundEl‐Ghazaly, M. A., Abdel‐Naby, D. H., & Khayyal, M. T. (2010) · International Journal of Radiation Biology · doi:10.3109/09553002.2011.530337 · Cited by 11 · see citing works
“The latter is known to stimulate synovial fibroblasts and cartilage chondrocytes to secrete MMPs which play a major role in the degradation of collagen (Arend and Dayer 1995, Poole et al. 2003).”
BackgroundKumar, K. S., Ravichandiran, V., & Roy, K. K. (2019) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2019.1651221 · Cited by 11 · see citing works
“…article can be accessed online at https://doi.org/10.1080/07391102.2019.1651221 2019 Informa UK Limited, trading as Taylor & Francis Group the irreversible degradation of the cartilage and bone has been established (Kevorkian et al., 2004; Mengshol, Mix, & Brinckerhoff, 2002; Poole et al., 2003).”
BackgroundInfluentialC2K77 ELISA detects cleavage of type II collagen by cathepsin K in equine articular cartilage
Noé, B., Poole, A. R., Mort, J. S., et al. (2017) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2017.08.011 · Cited by 10 · see citing works
Self-citationKuhi, L., Tamm, A. E., Tamm, A. O., & Kisand, K. (2020) · Osteoarthritis and Cartilage Open · doi:10.1016/j.ocarto.2020.100096 · Cited by 8 · see citing works
Frisch, J., & Cucchiarini, M. (2016) · Stem Cells and Development · doi:10.1089/scd.2016.0106 · Cited by 7 · see citing works
Products of Cartilage Metabolism
Manicourt, D.-H., Devogelaer, J., & Thonar, E. J. ‐. A. (2006) · Elsevier eBooks · doi:10.1016/b978-012088562-6/50026-1 · Cited by 12 · see citing works
Yao, W., Qu, N., Shi-xun, Y., et al. (2014) · Clinical Interventions in Aging · doi:10.2147/cia.s65871 · Cited by 5 · see citing works
The clinical utility of gene expression examination in rheumatology
Tchetina, E. V., & Markova, G. A. (2017) · Mediterranean Journal of Rheumatology · doi:10.31138/mjr.28.3.116 · Cited by 4 · see citing works
Self-citationMonocyte Chemotactic Proteins Mediate the Effects of Hyperglycemia in Chondrocytes: In Vitro Studies
Quincey, A., Mohan, S., & Edderkaoui, B. (2022) · Life · doi:10.3390/life12060836 · Cited by 5 · see citing works
“However, in OA conditions, the cells enter a cascade of proliferation and hypertrophic differentiation stages accompanied by markers of differentiation such as collagen 10 [26], and MMP-13 [27], with subsequent apoptotic death [28] and mineralization of articular cartilage [29].”
BackgroundDegradation of Proteoglycans and Collagen in Equine Meniscal Tissues
Dubuc, J., Schneider, M. J., Dubuc, V., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25126439 · Cited by 4 · see citing works
“They identify unique footprints of aggrecanolytic (DIPEN-MMPs; NITEGE-ADAMTS) and collagenase (C1,2C) enzymes [27] in the meniscal ECM.”
BackgroundSelf-citationHeinegård, D. K. (2007) · Springer eBooks · doi:10.1007/978-1-84628-701-5_5 · Cited by 4 · see citing works
“Collagen is broken down [57,64,65] primarily by three collagenases, MMP-1, -8, and -13 (collagenases 1, 2, and 3, respectively), all cleaving at the same three-quarters to one-quarter site.”
BackgroundLaFlamme, S. E., Shi, F., & Sottile, J. (2008) · doi:10.1002/9783527622092.ch5 · Cited by 4 · see citing works
Dimeric PKM2 in chondrocytes impairs mitochondrial homeostasis in osteoarthritis
Liu, B., Liang, Y., Wang, C., Weng, Z., Yang, Y., Shi, Y., & Zhang, C. (2026) · Cell Death and Disease · doi:10.1038/s41419-026-08621-4 · Cited by 2 · see citing works
Physiopathologie de l'arthrose
Chevalier, X. (2008) · EMC - Appareil locomoteur · doi:10.1016/s0246-0521(08)45638-3 · Cited by 2 · see citing works
Chevalier, X. (2009) · EMC - Aparato Locomotor · doi:10.1016/s1286-935x(09)70905-0 · Cited by 2 · see citing works
Sawada, Y., Sugimoto, A., Hananouchi, T., et al. (2017) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2017.5064 · Cited by 2 · see citing works
“It has been reported that MMP‑13 may be induced by inflammatory cytokines (18), whereas ADE exhibits an anti‑inflammatory action on an arthritis model (7).”
Padmanaban, D., & Krishnan, M. V. (2026) · Molecular Biology Reports · doi:10.1007/s11033-026-11862-3 · Cited by 1 · see citing works
Evidence for the Effectiveness of Soy in Aging and Improving Quality of Life
Arjmandi, B. H., & Foley, E. M. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.85664 · Cited by 1 · see citing works
Tuska, P., Tóth, B. I., Vásárhelyi, G., et al. (2016) · Acta Veterinaria Hungarica · doi:10.1556/004.2016.017 · Cited by 1 · see citing works
“The product of the primary initiating event of this cleavage can be measured by immunoassay of a C1,2C neoepitope (Billinghurst et al., 1997; Poole et al., 2003; Celeste et al., 2005).”
BackgroundAntioxidant and Antiinflammatory Properties of Heme Oxygenase-1 in Osteoarthritic Articular Cells
Guillén, M. I., García-Arnandis, I., Clérigues, V., et al. (2012) · Springer eBooks · doi:10.1007/978-1-4614-6166-1_11
Le rôle de la cathepsine K dans le développement de l'ostéoarthrose équine
Vinardell, T. (2007) · doi:10.71781/3959
Selecting dietary-derived bioactives which protect cartilage from destruction in osteoarthritis
Green, J. A. (2015) · UEA Digital Repository (University of East Anglia)
Molecular Biology Techniques in Musculoskeletal Research
von Rechenberg, B., & Hottiger, M. O. (2006) · Elsevier eBooks · doi:10.1016/b1-41-600123-9/50081-4
Upcoming value of gene expression analysis in rheumatology
Chetina, E. V., & Markova, G. A. (2018) · Biomeditsinskaya Khimiya · doi:10.18097/pbmc20186403221
Prospects for the Use of Gene Expression Analysis in Rheumatology
Chetina, E. V., & Markova, G. A. (2019) · Biochemistry (Moscow) Supplement Series B Biomedical Chemistry · doi:10.1134/s1990750819010049
- Authors
- Poole, A. R., Nelson, F., Dahlberg, L., Tchetina, E., Kobayashi, M., Yasuda, T., Laverty, S., Squires, G., Kojima, T., Wu, W., & Billinghurst, R. C.
- Affiliations
- Shriners Hospitals for Children - Canada (CA)
- Corresponding author
- Nelson, Fred
- Dahlberg, Leif
- Tchetina, Elena
- Kobayashi, Masahiko
- Yasuda, Tadashi
- Laverty, Sheila
- Squires, Ginette
- Kojima, Toshihisa
- Wu, William
- ORCID
- Venue
- Biochemical Society Symposia
- Publisher
- Portland Press Ltd.
- Published
- 2003-09-01
- Volume
- 70
- Issue
- 70
- Pages
- 115-123
- ISSN
- 0067-8694 (ISSN-L)
- 1744-1439
- OpenAlex
- W1804092355
- Cited by
- 103
- References
- 0
- Citations by year
- 2026: 4 · 2025: 1 · 2024: 3 · 2023: 2 · 2022: 2 · 2021: 2 · 2020: 4 · 2019: 3 · 2018: 4 · 2017: 4 · 2016: 4 · 2015: 5 · 2014: 5 · 2013: 4 · 2012: 4
- FWCI
- 4.76
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical Society Symposia (publishedVersion)
- PubMed (publishedVersion)
- Lund University Publications (Lund University) (submittedVersion)
- Topics
- Health Sciences › Medicine › Rheumatology › Osteoarthritis Treatment and Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Keywords
- osteoarthritis, collagen fibril degradation, matrix metalloproteinases, MMP-1, MMP-13, interleukin-1, TNF-α, chondrocytes, cartilage degeneration, chondrogenic differentiation, matrix mineralization, biomarkers, disease activity monitoring, rheumatoid arthritis, matrix metalloproteinase inhibitors
- MeSH terms
- Aging, Cartilage, Articular, Collagen, Humans, Hydrolysis, Osteoarthritis, Matrix Metalloproteinases
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