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Tenascin-X deficiency mimics Ehlers-Danlos syndrome in mice through alteration of collagen deposition
Abstract
Tenascin-X is a large extracellular matrix protein of unknown function. Tenascin-X deficiency in humans is associated with Ehlers-Danlos syndrome, a generalized connective tissue disorder resulting from altered metabolism of the fibrillar collagens. Because TNXB is the first Ehlers-Danlos syndrome gene that does not encode a fibrillar collagen or collagen-modifying enzyme, we suggested that tenascin-X might regulate collagen synthesis or deposition. To test this hypothesis, we inactivated Tnxb in mice. Tnxb-/- mice showed progressive skin hyperextensibility, similar to individuals with Ehlers-Danlos syndrome. Biomechanical testing confirmed increased deformability and reduced tensile strength of their skin. The skin of Tnxb-/- mice was histologically normal, but its collagen content was significantly reduced. At the ultrastructural level, collagen fibrils of Tnxb-/- mice were of normal size and shape, but the density of fibrils in their skin was reduced, commensurate with the reduction in collagen content. Studies of cultured dermal fibroblasts showed that although synthesis of collagen I by Tnxb-/- and wildtype cells was similar, Tnxb-/- fibroblasts failed to deposit collagen I into cell-associated matrix. This study confirms a causative role for TNXB in human Ehlers-Danlos syndrome and suggests that tenascin-X is an essential regulator of collagen deposition by dermal fibroblasts.
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“TNXB encodes tenascin-X, which is highly expressed in connective tissues. It is essential in the maintenance of the integrity of the extracellular matrix by regulating the collagen fi bril deposition, in which defects lead to EDS, a hereditary connective tissue disorder. 21”
From High-Throughput Screening for CYP21A1P-TNXA/TNXB Chimeric Genes Responsible for Ehlers Danlos Syndrome in Patients with Congenital Adrenal Hyperplasia. (2019) · cites this paper as [21]
Citations
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Joint hypermobility syndromes: The pathophysiologic role of tenascin‐X gene defects
Zweers, M. C., Hakim, A. J., Grahame, R., & Schalkwijk, J. (2004) · Arthritis & Rheumatism · doi:10.1002/art.20488 · Cited by 90
Chang, J., Zhong, R., Tian, J., Li, J., Zhai, K., Ke, J., Lou, J., Chen, W., Zhu, B., Shen, N., et al. (2018) · Nature Genetics · doi:10.1038/s41588-018-0045-8 · Cited by 89
Tenascin-X Mediates Flow-Induced Suppression of EndMT and Atherosclerosis
Liang, G., Wang, S., Shao, J., Jin, Y., Xu, L., Yang, Y., Günther, S., Wang, L., & Offermanns, S. (2022) · Circulation Research · doi:10.1161/circresaha.121.320694 · Cited by 113
Merke, D. P., Chen, W., Morissette, R., Xu, Z., Van Ryzin, C., Sachdev, V., Hannoush, H., Shanbhag, S. M., Acevedo, A. T., Nishitani, M., et al. (2013) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2012-3148 · Cited by 82
Juneja, S., & Veillette, C. (2013) · Arthritis · doi:10.1155/2013/154812 · Cited by 82
Ishikawa, Y., Vranka, J. A., Boudko, S. P., Pokidysheva, E. N., Mizuno, K., Zientek, K. D., Keene, D. R., Rashmir‐Raven, A. M., Nagata, K., Winand, N. J., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.333336 · Cited by 79
Egbert, M., Ruetze, M., Sattler, M., Wenck, H., Gallinat, S., Lucius, R., & Weise, J. M. (2014) · Journal of Dermatological Science · doi:10.1016/j.jdermsci.2013.08.010 · Cited by 77
“These include thrombospondins [31,32], SPARC [33], hevin [34], tenascin-X [35], CCN1 [36,37], CCN2 [38,39], and”
BackgroundRole of matricellular proteins in cardiac tissue remodeling after myocardial infarction
Matsui, Y. (2010) · World Journal of Biological Chemistry · doi:10.4331/wjbc.v1.i5.69 · Cited by 73
First Mouse Model for Combined Osteogenesis Imperfecta and Ehlers‐Danlos Syndrome
Chen, F., Guo, R.-L., Itoh, S., Moreno, L., Rosenthal, E., Zappitelli, T., Zirngibl, R., Flenniken, A., Cole, W., Grynpas, M., et al. (2014) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.2177 · Cited by 76
Gene expression profiles from hypertrophic scar fibroblasts before and after IL‐6 stimulation
Dasu, M. R. K., Hawkins, H. K., Barrow, R. E., Xue, H., & Herndon, D. N. (2004) · The Journal of Pathology · doi:10.1002/path.1539 · Cited by 71
“Tenascin X associates with heterotypic collagen fibrils and facilitates fibril deposition both in vivo and in vitro [45].”
BackgroundA model of tenascin-X integration within the collagenous network
Lethias, C., Carisey, A., Comte, J., Cluzel, C., & Exposito, J.-Y. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.10.037 · Cited by 74
Early Aldosterone-Regulated Genes in Cardiomyocytes: Clues to Cardiac Remodeling?
Fejes‐Tóth, G., & Náray‐Fejes‐Tóth, A. (2007) · Endocrinology · doi:10.1210/en.2006-1438 · Cited by 85
Bader, H., Keene, D., Charvet, B., Veit, G., Driever, W., Koch, M., & Ruggiero, F. (2009) · Matrix Biology · doi:10.1016/j.matbio.2008.09.580 · Cited by 72
Wenstrup, R., Florer, J., Cole, W., Willing, M., & Birk, D. (2004) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20024 · Cited by 71
“A reduction of type I collagen deposition was also observed in cultured dermal fibroblasts from tenascin X (TNX) deficientmice, which hadnormal type I collagen synthesis but reduced collagen deposition in cell culture [Mao et al., 2002].”
BackgroundMatricellular proteins in the trabecular meshwork.
Rhee, D., Haddadin, R. I., Kang, M., & Oh, D.-J. (2009) · Experimental Eye Research · doi:10.1016/j.exer.2008.11.032 · Cited by 70
Interactions of human tenascin-X domains with dermal extracellular matrix molecules
Egging, D. F., van den Berkmortel, F., Taylor, G. D., Bristow, J., & Schalkwijk, J. (2006) · Archives of Dermatological Research · doi:10.1007/s00403-006-0706-9 · Cited by 66
“In mice, the variation in collagen Wbril diameter appears to be increased [ 15 , 18].”
BackgroundSelf-citationBroadening the Spectrum of Ehlers Danlos Syndrome in Patients With Congenital Adrenal Hyperplasia
Morissette, R., Chen, W., Perritt, A. F., Dreiling, J. L., Arai, A. E., Sachdev, V., Hannoush, H., Mallappa, A., Xu, Z., McDonnell, N. B., et al. (2015) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2015-2232 · Cited by 68
“Normal collagen fibril deposition in connective tissue is essential for the collagenous matrix integrity and defects lead to Ehlers Danlos syndrome (EDS), a hereditary connective tissue disorder (4).”
BackgroundEhlers–Danlos syndrome: A showcase of conditions that lead to understanding matrix biology
Byers, P. H., & Murray, M. L. (2014) · Matrix Biology · doi:10.1016/j.matbio.2013.07.005 · Cited by 68
“…deficiency and EDS due to a contiguous gene deletion that included the gene TNXB. Subsequent studies in mouse knock-outs (Tnxb−/−) suggested that tenascin X likely plays a role in collagen deposition but not synthesis (Mao et al., 2002), which may differ through development (Egging et al., 2006).”
BackgroundTNXB mutations can cause vesicoureteral reflux.
Gbadegesin, R., Brophy, P., Adeyemo, A., Hall, G., Gupta, I., Hains, D., Bartkowiak, B., Rabinovich, C., Chandrasekharappa, S., Homstad, A., et al. (2013) · Journal of the American Society of Nephrology · doi:10.1681/asn.2012121148 · Cited by 66
Malfait, F., & Paepe, A. D. (2013) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-7893-1_9 · Cited by 126
Egging, D. F., van Vlijmen‐Willems, I. M. J. J., van Tongeren, T., Schalkwijk, J., & Peeters, A. C. T. M. (2007) · Connective Tissue Research · doi:10.1080/03008200601166160 · Cited by 63
Tenascin-X, Congenital Adrenal Hyperplasia, and the CAH-X Syndrome
Miller, W. L., & Merke, D. P. (2018) · Hormone Research in Paediatrics · doi:10.1159/000481911 · Cited by 61
Molecular and developmental mechanisms of congenital heart valve disease
Lincoln, J., & Yutzey, K. E. (2011) · Birth Defects Research Part A Clinical and Molecular Teratology · doi:10.1002/bdra.20799 · Cited by 60
“Tenascin-X2/2 mice also exhibit hyperextensibility of the skin, characteristic of EDS, but are viable (Mao et al., 2002).”
BackgroundO'Brien, J., Hansen, K. C., Barkan, D., Green, J., & Schedin, P. (2011) · International Journal of Developmental Biology · doi:10.1387/ijdb.113379jo · Cited by 60
“Tenascin-X, another member of the tenascin glycoprotein family, is involved in directing collagen fibril alignment, and has been previously identified as a constituent of nulliparous rat mammary ECM (Mao et al., 2002; Hansen et al., 2009).”
BackgroundZweers, M. C., Dean, W. B., Kuppevelt, T. H. V., Bristow, J. D., & Schalkwijk, J. (2005) · Clinical Genetics · doi:10.1111/j.1399-0004.2005.00401.x · Cited by 62
“Genetically determined deficiency of TNX is associated with the fragmentation of the elastic fibers and reduction of collagen (11, 12).”
BackgroundSelf-citationKatari, S., Wood-Trageser, M., Jiang, H., Kalynchuk, E., Muzumdar, R., Yatsenko, S., & Rajkovic, A. (2015) · Journal of Clinical Endocrinology and Metabolism · doi:10.1210/jc.2015-1401 · Cited by 55
“10445G T) was not reported previously, and Tnxb mouse knockouts have no reported reproductive phenotype (7).”
BackgroundLévy, P., Ripoche, H., Laurendeau, I., Lazar, V., Ortonne, N., Parfait, B., Leroy, K., Wechsler, J., Salmon, I., Wolkenstein, P., et al. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-06-0182 · Cited by 53
Expression of tenascin-C and its isoforms in the breast
Guttery, D. S., Shaw, J., Lloyd, K., Pringle, J. H., & Walker, R. A. (2010) · Cancer and Metastasis Reviews · doi:10.1007/s10555-010-9249-9 · Cited by 54
“Other members of the TN family include tenascin-R (TNR or restrictin), which is restricted to the developing and adult nervous system [7, 8]; tenascin-W (TNW) [9], which is found in the ECM of bone, muscle and kidney [10] (also found recently in malignant mammary tumours [10] and postulated to be a marker of activated…”
BackgroundTenascins in fibrotic disorders—from bench to bedside
Kasprzycka, M., Hammarström, C. L., & Haraldsen, G. (2015) · Cell Adhesion & Migration · doi:10.4161/19336918.2014.994901 · Cited by 56
“Mice deficient in tenascin X partly reproduced this phenotype.(30) In vitro studies revealed that tenascin X interacts with fibrillar collagen type I, III and V when they are in native conformation.”
BackgroundThe evolution of tenascins and fibronectin
Adams, J. C., Chiquet-Ehrismann, R., & Tucker, R. (2015) · Cell Adhesion & Migration · doi:10.4161/19336918.2014.970030 · Cited by 50
“, loose skin and hypermobile joints).(23) It has been proposed that the diversity of the teleost fishes is due in part to the selective retention of genes following 3 rounds of whole genome duplication events.”
BackgroundDeficiency of tenascin-X causes a decrease in the level of expression of type VI collagen.
Minamitani, T., Ariga, H., & Matsumoto, K.-I. (2004) · Experimental Cell Research · doi:10.1016/j.yexcr.2004.03.002 · Cited by 49
Proteomic Identification of Matrix Metalloproteinase Substrates in the Human Vasculature
Stegemann, C., Didangelos, A., Barallobre‐Barreiro, J., Langley, S. R., Mandal, K., Jahangiri, M., & Mayr, M. (2012) · Circulation Cardiovascular Genetics · doi:10.1161/circgenetics.112.964452 · Cited by 50
“Tenascin-X is an important regulator of collagen deposition by dermal fibroblasts.(38) In contrast, tenascin-C binds to fibronectin and inhibits cell spreading.”
BackgroundThe Roles of Tenascins in Cardiovascular, Inflammatory, and Heritable Connective Tissue Diseases
Matsumoto, K., & Aoki, H. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.609752 · Cited by 58
“The results of a number of studies on abnormalities in mice with targeted deletion in Tnxb (40) and in clEDS patients (26, 41) have suggested structural roles of TNX in tissue integrity (7, 42).”
BackgroundInfluentialTenascin-X increases the stiffness of collagen gels without affecting fibrillogenesis
Margaron, Y., Bostan, L. E., Exposito, J., Malbouyres, M., Trunfio-Sfarghiu, A.-M., Berthier, Y., & Lethias, C. (2010) · Biophysical Chemistry · doi:10.1016/j.bpc.2009.12.011 · Cited by 46
“Mice deficient in TNX partly reproduced this phenotype [3], and fibroblas ts i olated from these mice failed to deposit collagen in cell culture [4].”
BackgroundMatricellular Proteins in the Trabecular Meshwork: Review and Update
Chatterjee, A., Villarreal, G., & Rhee, D. J. (2014) · Journal of Ocular Pharmacology and Therapeutics · doi:10.1089/jop.2014.0013 · Cited by 48
“Mice deficient in tenascin-X, like their human counterparts, exhibit skin hyperextensibility and fragility, with histologically normal-appearing collagen fibrils that are less densely packed.(204) This mouse strain is now recognized as a suitable model for Ehlers–Danlos syndrome.”
BackgroundMatrix metalloproteinase 14 is required for fibrous tissue expansion
Taylor, S. H., Yeung, C., Kalson, N., Lu, Y.-H., Zigrino, P., Starborg, T., Warwood, S., Holmes, D. F., Canty-Laird, E., Mauch, C., et al. (2015) · eLife · doi:10.7554/elife.09345 · Cited by 44
“…with irregular outlines (Danielson et al., 1997), COMP can act as a catalyst for collagen fibril formation (Halasz et al., 2007), PCOLCE enhances the cleavage of procollagen to collagen (Takahara et al., 1994) and mice lacking TNXB have reduced numbers of collagen fibrils (Mao et al., 2002).”
BackgroundThe extracellular matrix glycoprotein tenascin‐X regulates peripheral sensory and motor neurones
Aktar, R., Peiris, M., Fikree, A., Cibert‐Goton, V., Walmsley, M., Tough, I. R., Watanabe, P. D. S., Araújo, E. J. D. A., Mohammed, S. D., Delalande, J., et al. (2018) · The Journal of Physiology · doi:10.1113/jp276300 · Cited by 43
“TNX-deficient mice show musculoskeletal and cutaneous features of hEDS (Mao et al. 2002) while other aspects of physiology remain uninvestigated.”
BackgroundMethodO’Brien, J., Vanderlinden, L. A., Schedin, P. S., & Hansen, K. C. (2012) · Journal of Proteome Research · doi:10.1021/pr3003744 · Cited by 38
Transcription factor Mohawk and the pathogenesis of human anterior cruciate ligament degradation
Nakahara, H., Hasegawa, A., Otabe, K., Ayabe, F., Matsukawa, T., Onizuka, N., Ito, Y., Ozaki, T., Lotz, M., & Asahara, H. (2013) · Arthritis & Rheumatism · doi:10.1002/art.38020 · Cited by 39
“Studies of cultured dermal fibroblasts showed that fibroblasts from Tnxb / mice failed to deposit type I collagen into cell-associated matrix, although type I collagen synthesis by cells from Tnxb / and wild-type mice was similar (34).”
Petersen, J. W., & Douglas, J. Y. (2013) · Medical Hypotheses · doi:10.1016/j.mehy.2013.06.005 · Cited by 45
“Subsequently, researchers conducted studies of both TNXBdeficient mice [23,26] and of human populations diagnosed with EDS-HT who displayed serum levels of TNX 50% below those of healthy patients [6,27].”
BackgroundDermal connective tissue development in mice: an essential role for tenascin-X
Egging, D. F., van Vlijmen, I., STARCHER, B. C., Gijssen, Y., Zweers, M. C., Blankevoort, L., Bristow, J., & Schalkwijk, J. (2005) · Cell and Tissue Research · doi:10.1007/s00441-005-0100-5 · Cited by 33
“Of note, the TNX null allele used in our study is on a different (homogenous C57Black6) background than that used by Mao et al. (2002).”
BackgroundMethodResultInfluentialSelf-citationGhali, N., Sobey, G. J., & Burrows, N. (2019) · BMJ · doi:10.1136/bmj.l4966 · Cited by 62
Gravez, B., Tarjus, A., Jiménez-Canino, R., Moghrabi, S. E., Messaoudi, S., de la Rosa, D. Á., & Jaisser, F. (2013) · PLoS ONE · doi:10.1371/journal.pone.0073737 · Cited by 37
“Tenascin-X is an essential regulator of collagen deposition by fibroblasts [28] and is up-regulated during fibrosis after tissue injury [27].”
Background
Metadata
- Authors
- Mao, J. R., Taylor, G., Dean, W. B., Wagner, D. R., Afzal, V., Lotz, J. C., Rubin, E. M., & Bristow, J.
- Affiliations
- University of California, San Francisco (US)
- Lawrence Berkeley National Laboratory (US)
- Corresponding author
- Bristow, James
- Venue
- Nature Genetics
- Published
- 2002-03-04
- Volume
- 30
- Issue
- 4
- Pages
- 421-425
- ISSN
- 1061-4036 (ISSN-L)
- 1546-1718
- OpenAlex
- W2062321035
- Cited by
- 261
- References
- 0
- Citations by year
- 2026: 6 · 2025: 7 · 2024: 10 · 2023: 7 · 2022: 11 · 2021: 16 · 2020: 12 · 2019: 10 · 2018: 10 · 2017: 7 · 2016: 10 · 2015: 14 · 2014: 7 · 2013: 14 · 2012: 13
- FWCI
- 7.43
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Genetics (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Connective tissue disorders research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Skin and Cellular Biology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Dermatological and Skeletal Disorders
- Keywords
- tenascin-X, TNXB, Ehlers-Danlos syndrome, collagen deposition, type I collagen, dermal fibroblasts, skin hyperextensibility, connective tissue diseases, extracellular matrix, skin biomechanics, knockout mice
- MeSH terms
- Animals, Collagen, Ehlers-Danlos Syndrome, Exons, Fibroblasts, Humans, Male, Microscopy, Electron, Microscopy, Fluorescence, Models, Genetic, Molecular Sequence Data, Mutation, Phenotype, Plasmids, Recombination, Genetic, Skin Physiological Phenomena, Time Factors, Immunoblotting, Mice, Knockout, Tenascin, Mice
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