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Alternative splicing in the aggrecan G3 domain influences binding interactions with tenascin-C and other extracellular matrix proteins.
Open accessAbstract
The proteoglycans aggrecan, versican, neurocan, and brevican bind hyaluronan through their N-terminal G1 domains, and other extracellular matrix proteins through the C-type lectin repeat in their C-terminal G3 domains. Here we identify tenascin-C as a ligand for the lectins of all these proteoglycans and map the binding site on the tenascin molecule to fibronectin type III repeats, which corresponds to the proteoglycan lectin-binding site on tenascin-R. In the G3 domain, the C-type lectin is flanked by epidermal growth factor (EGF) repeats and a complement regulatory protein-like motif. In aggrecan, these are subject to alternative splicing. To investigate if these flanking modules affect the C-type lectin ligand interactions, we produced recombinant proteins corresponding to aggrecan G3 splice variants. The G3 variant proteins containing the C-type lectin showed different affinities for various ligands, including tenascin-C, tenascin-R, fibulin-1, and fibulin-2. The presence of an EGF motif enhanced the affinity of interaction, and in particular the splice variant containing both EGF motifs had significantly higher affinity for ligands, such as tenascin-R and fibulin-2. The mRNA for this splice variant was shown by reverse transcriptase-PCR to be expressed in human chondrocytes. Our findings suggest that alternative splicing in the aggrecan G3 domain may be a mechanism for modulating interactions and extracellular matrix assembly.
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“Tenascins are fibrous, matricellular proteins, which bind to the C-terminal domain of lecticans (Aspberg et al., 1997; Day et al., 2004).”
From The Perineuronal ‘Safety’ Net? Perineuronal Net Abnormalities in Neurological Disorders (2018) · cites this paper as Day et al., 2004
Citations
Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Towbin, H., Staehelin, T., & Gordon, J. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.9.4350 · Cited by 53,218
Multiple domains of the large fibroblast proteoglycan, versican.
Zimmermann, D., & Ruoslahti, E. I. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb08447.x · Cited by 652
Iozzo, R. V., & Murdoch, A. D. (1996) · The FASEB Journal · doi:10.1096/fasebj.10.5.8621059 · Cited by 647
Self-citationStructure and biology of cartilage and bone matrix noncollagenous macromolecules
Heinegård, D. K., & Oldberg, Å. (1989) · The FASEB Journal · doi:10.1096/fasebj.3.9.2663581 · Cited by 567
Bonaventure, J., Kadhom, N., Cohen-Solal, L., Ng, K. H., Bourguignon, J., Benoist-Lasselin, C., & Freisinger, P. (1994) · Experimental Cell Research · doi:10.1006/excr.1994.1123 · Cited by 520
Fibulins: a versatile family of extracellular matrix proteins
Timpl, R., Sasaki, T., Kostka, G., & Chu, M.-L. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1130 · Cited by 494
Self-citationAggregation of Cartilage Proteoglycans
Heinegård, D. K., & Hascall, V. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42509-x · Cited by 490
Ruoslahti, E. (1996) · Glycobiology · doi:10.1093/glycob/6.5.489 · Cited by 467
Doege, K. J., Sasaki, M., Kimura, T., & Yamada, Y. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)35257-2 · Cited by 447
Research works printed but not linked: 2
- Yamaguchi, 1996, Perspect. Dev. Neurobiol., 3, 307
- Isogai, 1996, Cancer Res., 56, 3902
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Galtrey, C. M., & Fawcett, J. W. (2007) · Brain Research Reviews · doi:10.1016/j.brainresrev.2006.09.006 · Cited by 575
The role of tenascin-C in tissue injury and tumorigenesis
Midwood, K. S., & Orend, G. (2009) · Journal of Cell Communication and Signaling · doi:10.1007/s12079-009-0075-1 · Cited by 453
“Tenascin-C also interacts with ECM-resident proteoglycans, including members of the lectican family; versican, neurocan, aggrecan and brevican (Day et al. 2004).”
Tenascin-C induced signaling in cancer
Orend, G., & Chiquet-Ehrismann, R. (2006) · Cancer Letters · doi:10.1016/j.canlet.2006.02.017 · Cited by 384
Tissue mechanics regulate brain development, homeostasis and disease
Barnes, J. M., Przybyla, L., & Weaver, V. M. (2017) · Journal of Cell Science · doi:10.1242/jcs.191742 · Cited by 344
“3A) stiffens the tumor tissue relative to normal brain by limiting the flexibility of the ECM (Mouw et al., 2014; Day et al., 2004; Kim and Kumar, 2014).”
BackgroundFell‐Muir Lecture: Proteoglycans and more – from molecules to biology
Heinegård, D. K. (2009) · International Journal of Experimental Pathology · doi:10.1111/j.1365-2613.2009.00695.x · Cited by 326
“These include the fibrillins, the fibulins as well as tenascins (Day et al. 2004).”
BackgroundCrosstalk between glia, extracellular matrix and neurons
Song, I., & Dityatev, A. E. (2017) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2017.03.003 · Cited by 270
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Struglics, A., Larsson, S., Pratta, M. A., Kumar, S., Lark, M. W., & Lohmander, S. L. (2005) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2005.07.018 · Cited by 204
Aggrecan, aging and assembly in articular cartilage
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Extracellular matrix components associated with remodeling processes in brain
Rauch, U. (2004) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4043-x · Cited by 199
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Wen, T. H., Binder, D. K., Ethell, I. M., & Razak, K. A. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00270 · Cited by 170
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BackgroundStattin, E., Wiklund, F. E., Lindblom, K., Önnerfjord, P., Jonsson, B., Tegner, Y., Sasaki, T., Struglics, A., Lohmander, S. L., Dahl, N., et al. (2010) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2009.12.018 · Cited by 161
Self-citationBurnside, E. R., & Bradbury, E. J. (2013) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12114 · Cited by 161
Perineuronal nets in brain physiology and disease
Testa, D., Prochiantz, A., & Nardo, A. A. D. (2018) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2018.09.011 · Cited by 153
Tompson, S. W. J., Merriman, B., Funari, V. A., Fresquet, M., Lachman, R. S., Rimoin, D. L., Nelson, S. F., Briggs, M. D., Cohn, D. H., & Krakow, D. (2008) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2008.12.001 · Cited by 146
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Crespo, D., Asher, R. A., Lin, R., Rhodes, K. E., & Fawcett, J. W. (2007) · Experimental Neurology · doi:10.1016/j.expneurol.2007.05.001 · Cited by 138
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Aspberg, A. (2012) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155412464376 · Cited by 130
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Lundell, A., Olin, A. I., Mörgelin, M., al-Karadaghi, S., Aspberg, A., & Logan, D. T. (2004) · Structure · doi:10.1016/j.str.2004.05.021 · Cited by 127
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Dours-Zimmermann, M. T., Maurer, K., Rauch, U., Stoffel, W., Fassler, R., & Zimmermann, D. R. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.4158-08.2009 · Cited by 123
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BackgroundChondroitin sulphate proteoglycans: Key modulators of spinal cord and brain plasticity
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Choocheep, K., Hatano, S., Takagi, H., Watanabe, H., Kimata, K., Kongtawelert, P., & Watanabe, H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.096479 · Cited by 115
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Rich, R. L., & Myszka, D. G. (2005) · Journal of Molecular Recognition · doi:10.1002/jmr.753 · Cited by 117
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Schwann cell migration is integrin-dependent and inhibited by astrocyte-produced aggrecan
Afshari, F. T., Kwok, J. C., White, L., & Fawcett, J. W. (2010) · Glia · doi:10.1002/glia.20970 · Cited by 103
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BackgroundRole of tenascins in the ECM of gliomas
Brösicke, N., & Faissner, A. (2015) · Cell Adhesion & Migration · doi:10.1080/19336918.2014.1000071 · Cited by 105
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BackgroundEstany, S., Vicens‐Zygmunt, V., Llatjós, R., Montes, A., Penin, R. M., Escobar, I., Xaubet, A., Santos, S., Manresa, F., Dorca, J., et al. (2014) · BMC Pulmonary Medicine · doi:10.1186/1471-2466-14-120 · Cited by 103
“Versican overexpression has been poorly studied in interstitial lung diseases, however its effects on motility, invasion and metastasis have been widely reported in cancer [9,21-23].”
BackgroundExtracellular matrix alterations in brains lacking four of its components
Rauch, U., Zhou, X.-H., & Roos, G. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.01.026 · Cited by 88
Brain matrix: structure, turnover and necessity
Rauch, U. (2007) · Biochemical Society Transactions · doi:10.1042/bst0350656 · Cited by 88
Proteoglycans and Diseases of Soft Tissues
Halper, J. T. (2013) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-7893-1_4 · Cited by 87
Wilson, R., Diseberg, A., Gordon, L., Zivkovic, S., Tatarczuch, L., Mackie, E. J., Gorman, J. J., & Bateman, J. F. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m000014-mcp201 · Cited by 85
Versican proteolysis mediates myocardial regression during outflow tract development
Kern, C. B., Norris, R. A., Thompson, R. P., Argraves, W. S., Fairey, S. E., Reyes, L., Hoffman, S., Markwald, R. R., & Mjaatvedt, C. H. (2007) · Developmental Dynamics · doi:10.1002/dvdy.21059 · Cited by 78
“…may relate to the persistence of signaling or lack thereof resulting from bivalent interactions by means of the HA-binding G1 domain and the G3 domain, which contains binding sites for numerous ECM proteins, including fibulin-1 and tenascin-C (Zhang et al., 1998; Day et al., 2004; Wu et al., 2005).”
BackgroundXiang, Y., Dong, H., Wan, Y., Li, J., Yee, A., Yang, B. B., & Lu, W.-Y. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512980200 · Cited by 74
Metabolism of proteoglycans in tendon
Rees, S., Dent, C. M., & Caterson, B. (2009) · Scandinavian Journal of Medicine and Science in Sports · doi:10.1111/j.1600-0838.2009.00938.x · Cited by 73
“For example, the G3 domain (which contains a C-type lectin moiety) has been shown to bind fibulins 1 and 2 (Aspberg et al., 1999; Olin et al., 2001) and tenascinC (Day et al., 2004).”
BackgroundAggrecan in Cardiovascular Development and Disease
Koch, C. D., Lee, C. M., & Apte, S. (2020) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155420952902 · Cited by 76
N-terminal domains of CCN family 2/connective tissue growth factor bind to aggrecan
Aoyama, E., Hattori, T., Hoshijima, M., Araki, D., Nishida, T., Kubota, S., & Takigawa, M. (2009) · Biochemical Journal · doi:10.1042/bj20081991 · Cited by 66
Kjer-Hansen, P., & Weatheritt, R. J. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01155-9 · Cited by 67
“This can substantially change the function of the protein isoforms impacting subcellular localization 18–21 , interaction strength 22 and enzymatic activity 23–26 .”
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Matsumoto, K., Kamiya, N., Suwan, K., Atsumi, F., Shimizu, K., Shinomura, T., Yamada, Y., Kimata, K., & Watanabe, H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m510330200 · Cited by 66
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Hardingham, T. (2006) · Elsevier eBooks · doi:10.1016/b9-78-012088-5/62650-0066 · Cited by 63
Self-citationStamenković, V., Stamenković, S., Jaworski, T., Gawlak, M., Jovanović, M., Jakovčevski, I., Wilczynski, G. M., Kaczmarek, L., Schachner, M., Radenović, L., et al. (2016) · Brain Structure and Function · doi:10.1007/s00429-016-1224-y · Cited by 64
“In the cerebellum, PNNs are abundantly localized around neurons of the DCN, and their molecular composition, as well as the time course of their formation have been studied intensely (Carulli et al. 2006, 2007; Deepa et al. 2006).”
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Brellier, F., Ruggiero, S., Zwolanek, D., Martina, E., Heß, D., Brown-Luedi, M., Hartmann, U., Koch, M., Merlo, A., Lino, M. M., et al. (2011) · Matrix Biology · doi:10.1016/j.matbio.2011.02.001 · Cited by 58
Tenascin-C induces inflammatory mediators and matrix degradation in osteoarthritic cartilage
Patel, L., Sun, W., Glasson, S. S., Morris, E. A., Flannery, C. R., & Chockalingam, P. S. (2011) · BMC Musculoskeletal Disorders · doi:10.1186/1471-2474-12-164 · Cited by 54
“The correlation between TNC and aggrecan loss could result from two different roles of TN-C: 1) TLR4 dependent TN-C induction of matrix degradation whereby TN-C regulates the expression metalloproteases and 2) Loss of TN-C along with degraded fragments of aggrecan resulting from aggrecanase activity in diseased cartil…”
BackgroundRoll, L., & Faissner, A. (2018) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2018.09.012 · Cited by 54
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BackgroundWilson, C. G., Nishimuta, J. F., & Levenston, M. E. (2009) · Tissue Engineering Part A · doi:10.1089/ten.tea.2008.0106 · Cited by 53
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Chockalingam, P. S., Glasson, S. S., & Lohmander, S. L. (2012) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2012.10.016 · Cited by 49
Brösicke, N., van Landeghem, F. K. H., Scheffler, B., & Faissner, A. (2013) · Cell and Tissue Research · doi:10.1007/s00441-013-1704-9 · Cited by 48
Marx, G. S., & Gilon, C. (2012) · ACS Chemical Neuroscience · doi:10.1021/cn300097b · Cited by 48
Chondroitin sulfate proteoglycans in neural development and plasticity
Maeda, N. (2010) · Frontiers in Bioscience · doi:10.2741/3637 · Cited by 44
Impact of the complement cascade on posttraumatic cartilage inflammation and degradation.
John, T., Pf, S., Morgan, S. J., & Schulze-Tanzil, G. G. (2007) · PubMed · doi:10.14670/hh-22.781 · Cited by 43
“Other cartilage matrix proteoglycans contain lectin motifs or complement binding protein like domains which may be accessable during cartilage injury for complement activation via the lectin pathway (Chen et al., 2002; Day et al., 2004).”
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Xu, M., Stattin, E.-L., Shaw, G., Heinegård, D. K., Sullivan, G. J., Wilmut, I., Colman, A., Önnerfjord, P., Khabut, A., Aspberg, A., et al. (2016) · Stem Cells Translational Medicine · doi:10.5966/sctm.2015-0384 · Cited by 42
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Brellier, F., & Chiquet‐Ehrismann, R. (2011) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2011.01360.x · Cited by 44
“For instance, through their binding to tenascin-C, fibronectin [78], perlecan [79], lectican [80], heparin [81], contactin [82, 83] and SMOC1 [84] have been shown to modify its effects.”
Hayes, A. J., Shu, C. C., Lord, M. S., Little, C. B., Whitelock, J. M., & Melrose, J. (2016) · European Cells and Materials · doi:10.22203/ecm.v032a03 · Cited by 40
Identification of proteoglycan from salmon nasal cartilage
Kakizaki, I., Tatara, Y., Majima, M., Kato, Y., & Endo, M. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.10.025 · Cited by 40
Potential biomarkers of the mature intervertebral disc identified at the single cell level
Li, K., Kapper, D., Youngs, B., Kocsis, V., Mondal, S., Kraus, P., & Lufkin, T. (2018) · Journal of Anatomy · doi:10.1111/joa.12904 · Cited by 38
Ishiyama, A., Mowry, S. E., López, I. A., & Ishiyama, G. P. (2009) · Hearing Research · doi:10.1016/j.heares.2009.03.014 · Cited by 37
“, 2007), proteoglycans (Day et al., 2004) and other ECM components.”
BackgroundBale, S., Verma, P., Varga, J., & Bhattacharyya, S. (2023) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2023.04.030 · Cited by 38
Tenascin-C fragments are endogenous inducers of cartilage matrix degradation
Sofat, N., Robertson, S. D., Hermansson, M., Jones, J. S., Mitchell, P., & Wait, R. (2011) · Rheumatology International · doi:10.1007/s00296-011-2067-8 · Cited by 36
Zacharias, U., & Rauch, U. (2006) · Journal of Cell Science · doi:10.1242/jcs.03094 · Cited by 35
“…tenascins and lecticans is mediated by protein-protein-interaction involving the fibronectin type III domains (FNIII domains) 4-5 of TN-R or tenascin-C and the C-type lectin domain of lecticans (Aspberg et al., 1997; Rauch et al., 1997; Milev et al., 1998; Day et al., 2004; Lundell et al., 2004).”
BackgroundKeller, K. E., Sun, Y. Y., Vranka, J. A., Hayashi, L., & Acott, T. S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0048523 · Cited by 35
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Fürst, C. M., Mörgelin, M., Vadstrup, K., Heinegård, D. K., Aspberg, A., & Blom, A. M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0061407 · Cited by 35
“The aggrecan G3 domain exists in different splice variants in man, with optional epidermal growth factor-like domains (EGF) and complement control protein (CCP) domain, which might finetune interactions between CLD and its ligands [17].”
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“Transfection of the construct into 293-EBNA cells (Invitrogen), selection with hygromycin, and purification of the secreted protein from culture medium by Ni(2) chelation affinity chromatography was as previously described (41).”
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“Whereas previous work has shown that the FNIII domains of TN-C are susceptible to proteolytic cleavage [45] and interact with ligands including integrins [43], they are also subject to heparin binding [46] and binding to other ECM molecules including fibronectin [47].”
BackgroundWilson, C. G., Vanderploeg, E. J., Zuo, F., Sandy, J. D., & Levenston, M. E. (2009) · Arthritis Research & Therapy · doi:10.1186/ar2862 · Cited by 33
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BackgroundLabrousse-Arias, D., Martı́nez-Ruiz, A., & Calzada, M. J. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7275 · Cited by 30
Yang, L., Zhang, C., Wang, W., Wang, J., Xiao, Y., Lü, W., Ma, X., Chen, L., Ni, J., Wang, D., et al. (2018) · BMC Medical Genetics · doi:10.1186/s12881-018-0730-6 · Cited by 30
Rekad, Z., Izzi, V., Lamba, R., Ciais, D., & Obberghen‐Schilling, E. V. (2022) · Matrix Biology · doi:10.1016/j.matbio.2022.05.003 · Cited by 30
Jakovljević, A., Tucić, M., Blažíková, M., Korenić, A., Missirlis, Y. F., Stamenković, V., & Anđjus, P. R. (2021) · Cells · doi:10.3390/cells10061345 · Cited by 32
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Fu, Z., Zhu, G., Luo, C., Chen, Z., Dou, Z., Chen, Y., Chen, Z., Su, S., & Liu, F. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.971462 · Cited by 29
“Additionally, TNC can bind to other ECM proteins, such as periostin (92), perlecan (93), fibrillin-2 (94), aggrecan (95), and SPARC-related modular calcium-binding protein 1 (SMOC1) (96).”
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Tang, F., Brune, J. E., Chang, M. Y., Reeves, S. R., Altemeier, W. A., & Frevert, C. W. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00162.2022 · Cited by 25
Song, X., Li, X., Ge, Y., Song, J., Wei, Q., He, M., Wei, M., Zhang, Y., Chen, T., & Lin, Z. (2023) · International Immunopharmacology · doi:10.1016/j.intimp.2023.110718 · Cited by 24
Moffatt, P., Lee, E. R., St‐Jacques, B., Matsumoto, K., Yamaguchi, Y., & Roughley, P. J. (2011) · Developmental Dynamics · doi:10.1002/dvdy.22529 · Cited by 24
“…Col2-driven mice is not stably localized within the extracellular matrix by interaction with hyaluronan, but is localized by interaction of its G3 region with another matrix component (Day et al., 2004) or is undergoing continuous loss by diffusion and replacement by newly synthesized molecules.”
BackgroundDistribution and role of tenascin-C in human osteoarthritic cartilage
Nakoshi, Y., Hasegawa, M., Akeda, K., Iino, T., Sudo, A., Yoshida, T., & Uchida, A. (2010) · Journal of Orthopaedic Science · doi:10.1007/s00776-010-1513-x · Cited by 24
Sinha, A., Kawakami, J., Cole, K. S., Ladutska, A., Nguyen, M. Y., Zalmai, M. S., Holder, B. L., Broerman, V. M., Matthews, R. T., & Bouyain, S. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104952 · Cited by 24
“The assay design was first validated by testing previously characterized interactions between RPTPζ and contactin-1 (CNTN1) (26, 27) and between TNC, TNR, and ACAN (28) as positive controls in two distinct “orientations”: Fc versus FcYTS and FcYTS versus Fc.”
MethodInfluentialTenascin-C restricts reactive astrogliosis in the ischemic brain
Dzyubenko, E., Manrique‐Castano, D., Pillath‐Eilers, M., Vasileiadou, P., Reinhard, J., Faissner, A., & Hermann, D. M. (2022) · Matrix Biology · doi:10.1016/j.matbio.2022.04.003 · Cited by 21
The Biology of Extracellular Matrix Proteins in Hypertrophic Scarring
Eremenko, E. E., Ding, J., Kwan, P. O., & Tredget, E. E. (2021) · Advances in Wound Care · doi:10.1089/wound.2020.1257 · Cited by 23
Fell‐Muir Lecture: Cartilage 2010 – The Known Unknowns
Hardingham, T. (2010) · International Journal of Experimental Pathology · doi:10.1111/j.1365-2613.2010.00719.x · Cited by 21
“The aggrecan G2 domain was shown to have no function in the formation of aggregates (Fosang & Hardingham 1989), but the G3 domain which includes a C-type lectin fold was shown to bind to several matrix molecules, including tenascins and fibulins (Day et al. 2004).”
BackgroundSelf-citationFrom expression pattern to genetic association in asthma and asthma-related phenotypes
Vaillancourt, V. T., Bordeleau, M., Laviolette, M., & Laprise, C. (2012) · BMC Research Notes · doi:10.1186/1756-0500-5-630 · Cited by 21
“The AGC1 gene, located in the chromosomal region 15q26, is coding for the aggrecan, a major component of the extracellular matrix of the cartilage that binds with tenascins [22].”
BackgroundEffects of covalently attached chondroitin sulfate on aggrecan cleavage by ADAMTS-4 and MMP-13
Miwa, H. E., Gerken, T. A., & Hering, T. M. (2006) · Matrix Biology · doi:10.1016/j.matbio.2006.07.004 · Cited by 21
Stattin, E., Lindblom, K., Struglics, A., Önnerfjord, P., Goldblatt, J., Dixit, A., Sarkar, A., Randell, T. L., Suri, M., Raggio, C., et al. (2022) · Scientific Reports · doi:10.1038/s41598-022-09211-y · Cited by 21
Self-citationRelevance of synovial fluid chondroitin sulphate as a biomarker to monitor polo pony joints.
Baccarin, R. Y. A., Rasera, L., Machado, T. S. L., & Michelacci, Y. M. C. D. S. (2014) · LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas) · Cited by 21
Fukuhara, Y., Cho, S. Y., Miyazaki, O., Hattori, A., Seo, J.-H., Mashima, R., Kosuga, M., Fukami, M., Jin, D., Okuyama, T., et al. (2018) · Clinical Dysmorphology · doi:10.1097/mcd.0000000000000241 · Cited by 17
“The CLD domain has a high affinity for extracellular matrix molecules, including tenascin-R, tenascin-C, fibulin-1, fibulin2, and fibrillin-1, and they interact with each other in a calcium-dependent manner (Aspberg et al., 1997; Rauch et al., 1997; Olin et al., 2001; Isogai et al., 2002; Day et al., 2004; Aspberg, 20…”
BackgroundProteoglycans of the Intervertebral Disc
Melrose, J., & Roughley, P. J. (2013) · Springer eBooks · doi:10.1007/978-3-7091-1535-0_4 · Cited by 19
FBLN1 promotes chondrocyte proliferation by increasing phosphorylation of Smad2
Xu, G., Geng, X., Yang, F., & Zhang, Y. (2021) · Journal of Orthopaedic Science · doi:10.1016/j.jos.2020.12.006 · Cited by 15
V3: an enigmatic isoform of the proteoglycan versican
Wight, T. N., Day, A. J., Kang, I., Harten, I. A., Kaber, G., Briggs, D. C., Braun, K. R., Lemire, J. M., Kinsella, M. G., Hinek, A., et al. (2023) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00059.2023 · Cited by 15
Enriched environment alters the behavioral profile of tenascin-C deficient mice
Stamenković, V., Milenkovic, I., Galjak, N., Todorović, V., & Anđjus, P. R. (2017) · Behavioural Brain Research · doi:10.1016/j.bbr.2017.05.047 · Cited by 13
Calcium-dependent self-association of the C-type lectin domain of versican
Ney, A., Booms, P., Epple, G., Mörgelin, M., Guo, G., Kettelgerdes, G., Gessner, R. V., & Robinson, P. N. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.07.007 · Cited by 12
Brain Interstitial Fluid Drainage Alterations in Glioma-Bearing Rats
Guan, X., Wang, W., Wang, A., Teng, Z., & Han, H. (2018) · Aging and Disease · doi:10.14336/ad.2017.0415 · Cited by 9
“Early studies reported that some of the matrix components excessively expressed with tumor growth and caused the tortuosity of the brain ECS were increased inside the tumor [9, 10].”
BackgroundAnalysis of Aggrecan Catabolism by Immunoblotting and Immunohistochemistry
Roughley, P. J., & Mort, J. S. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-498-8_15 · Cited by 9
Versican contributes to ligament formation of knee joints
Higuchi, T., Suzuki, D., Watanabe, T., Fanhchaksai, K., Ota, K., Yokoo, K., Furukawa, H., & Watanabe, H. (2021) · PLoS ONE · doi:10.1371/journal.pone.0250366 · Cited by 8
“The Cterminal G3 domain binds different ECM molecules such as fibrillin-1 [5], fibulin-1 and -2 [6, 7], tenascins [6, 8], and heparan sulfate proteoglycans [9].”
BackgroundProteoglycans and Diseases of Soft Tissues
Hwang, C. T., & Halper, J. T. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-80614-9_5 · Cited by 8
Bekku, Y., & Oohashi, T. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9636-7_8 · Cited by 8
Identification of Proteoglycan‐Binding Proteins
Muramatsu, T., Muramatsu, H., & Kojima, T. (2006) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(06)16017-6 · Cited by 9
Collagen and Other Proteins of the Nucleus Pulposus, Annulus Fibrosus, and Cartilage End Plates
Mwale, F. (2013) · Springer eBooks · doi:10.1007/978-3-7091-1535-0_5 · Cited by 7
Jakovljević, A., Stamenković, V., Poleksić, J., Hamad, M. I. K., Reiss, G., Jakovčevski, I., & Anđjus, P. R. (2024) · Biomolecules · doi:10.3390/biom14040508 · Cited by 7
“TnC has been shown to interact with the major components of PNNs, aggrecan [63], neurocan, and phosphacan [64,65].”
BackgroundAPBP-1, a DNA/RNA-binding Protein, Interacts with the Chick Aggrecan Regulatory Region
Pirok, E. W., Domowicz, M. S., Henry, J. G., Wang, Y., Santore, M. T., Mueller, M. M., & Schwartz, N. B. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505380200 · Cited by 6
Toscano, P., Meglio, L. D., Lonardo, F., Meglio, L. D., Mazzarelli, L. L., Sica, C., & Meglio, A. D. (2021) · BMC Pregnancy and Childbirth · doi:10.1186/s12884-021-03952-w · Cited by 5
Zhang, D., Liu, Z., Liu, Q., Lan, H., Peng, J., Liu, X., & Liu, W. (2021) · Inflammation · doi:10.1007/s10753-021-01540-w · Cited by 5
“TNC has a hexameric structure and many extracellular binding partners, including matrix components [28], soluble factors [29, 30], and pathogens as well as interactions with cell surface receptors such as TLR4 [21, 31].”
Background
Metadata
- Authors
- Day, J. M., Olin, A. I., Murdoch, A. D., Canfield, A., Sasaki, T., Timpl, R., Hardingham, T. E., & Aspberg, A.
- Affiliations
- Wellcome Centre for Cell-Matrix Research (GB)
- Lund University (SE)
- Max Planck Institute of Biochemistry (DE)
- Corresponding author
- Aspberg, Anders
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2004-03
- Volume
- 279
- Issue
- 13
- Pages
- 12511-12518
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2157467821
- Cited by
- 127
- References
- 47
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 5 · 2023: 6 · 2022: 8 · 2021: 7 · 2020: 1 · 2019: 5 · 2018: 7 · 2017: 5 · 2016: 5 · 2015: 2 · 2014: 2 · 2013: 10 · 2012: 9
- FWCI
- 2.83
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Research Explorer (The University of Manchester) (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- Lund University Publications (Lund University) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Health Sciences › Medicine › Rheumatology › Osteoarthritis Treatment and Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Keywords
- aggrecan, alternative splicing, tenascin-C, tenascin-R, C-type lectin, EGF-like repeats, fibulin-1, fibulin-2, extracellular matrix assembly, chondrocytes, hyaluronan binding, fibronectin type III repeats
- MeSH terms
- Amino Acid Sequence, Base Sequence, Binding Sites, Binding, Competitive, Dose-Response Relationship, Drug, Electrophoresis, Polyacrylamide Gel, Epidermal Growth Factor, Extracellular Matrix, Fibronectins, Humans, Kinetics, Ligands, Molecular Sequence Data, Protein Binding, Proteoglycans, Recombinant Proteins, RNA, Messenger, Time Factors, Extracellular Matrix Proteins, Alternative Splicing, Protein Structure, Tertiary, Tenascin, Chondrocytes, Reverse Transcriptase Polymerase Chain Reaction, Surface Plasmon Resonance, Amino Acid Motifs, Lectins, Lectins, C-Type, Aggrecans
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