Synonyms
Historical Background
Tenascins are glycoproteins found in the extracellular matrix of chordates (Chiquet-Ehrismann and Tucker 2011). Near their N-terminus tenascins have heptad repeats that support trimerization, and two trimers can be bound by disulfide bridges spanning N-terminal domains to form a hexabrachion. The N-terminal region is followed by one or more epidermal growth factor (EGF)-like domains that have a distinctive arrangement of cysteine residues (****C***C*****C****C*C********C). These are followed by a string of fibronectin type III (FNIII) domains and a C-terminal fibrinogen-related domain.
The original tenascin is tenascin-C (the “C” stands for cytotactin, a name given to this tenascin by one of its codiscoverers). Tenascin-C is the best studied of the tenascins and is prominently expressed in the embryo at sites of cell migration, epithelial-mesenchymal interactions, and in developing connective tissue. In the adult, tenascin-C is found at the...
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Adams JC, Chiquet-Ehrismann R, Tucker RP. The evolution of tenascins and fibronectin. Cell Adhes Migr. 2015;9(1–2):22–33. https://doi.org/10.4161/19336918.2014.970030.
Aloj L, D’Ambrosio L, Aurilio M, Morisco A, Frigeri F, et al. Radioimmunotherapy with Tenarad, a 131I-labelled antibody fragment targeting the extra-domain A1 of tenascin-C, in patients with refractory Hodgkin’s lymphoma. Eur J Nucl Med Mol Imaging. 2014;41(5):867–77.
Brellier F, Martina E, Chiquet M, Ferralli J, van der Heyden M, et al. The adhesion modulating properties of tenascin-W. Int J Biol Sci. 2012a;8(2):187–94.
Brellier F, Martina E, Degen M, Heuzé-Vourc’h N, Petit A, et al. Tenascin-W is a better cancer biomarker than tenascin-C for most human solid tumors. BMC Clin Pathol. 2012b;12:14.
Chiovaro F, Martina E, Bottos A, Scherberich A, Hynes NE, Chiquet-Ehrismann R. Transcriptional regulation of tenascin-W by TGF-beta signaling in the bone metastatic niche of breast cancer cells. Int J Cancer. 2015;137(8):1842–54. https://doi.org/10.1002/ijc.29565.
Chiquet-Ehrismann R, Tucker RP. Tenascins and the importance of adhesion modulation. Cold Spring Harb Perspect Biol. 2011;3:pii: a004960. https://doi.org/10.1101/cshperspect.a004960.
Chiquet-Ehrismann R, Kalla P, Pearson CA, Beck K, Chiquet M. Tenascin interferes with fibronectin action. Cell. 1988;53(3):383–90.
Chiquet-Ehrismann R, Orend G, Chiquet M, Tucker RP, Midwood KS. Tenascins in stem cell niches. Matrix Biol. 2014;37:112–23. https://doi.org/10.1016/j.matbio.2014.01.007.
Degen M, Brellier F, Kain R, Ruiz C, Terracciano L, et al. Tenascin-W is a novel marker for activated tumor stroma in low-grade human breast cancer and influences cell behavior. Cancer Res. 2007;67(19):9169–79.
Degen M, Brellier F, Schenk S, Driscoll R, Zaman K, et al. Tenascin-W, a new marker of cancer stroma, is elevated in sera of colon and breast cancer patients. Int J Cancer. 2008;122(11):2454–61. https://doi.org/10.1002/ijc.23417.
Huang W, Chiquet-Ehrismann R, Moyano JV, Garcia-Pardo A, Orend G. Interference of tenascin-C with syndecan-4 binding to fibronectin blocks cell adhesion and stimulates tumor cell proliferation. Cancer Res. 2001;61(23):8586–94.
Kimura H, Akiyama H, Nakamura T, de Crombrugghe B. Tenascin-W inhibits proliferation and differentiation of preosteoblasts during endochondral bone formation. Biochem Biophys Res Commun. 2007;356(4):935–41.
Lotz MM, Burdsal CA, Erickson HP, McClay DR. Cell adhesion to fibronectin and tenascin: quantitative measurements of initial binding and subsequent strengthening response. J Cell Biol. 1989;109(4 Pt 1):1795–805.
Lowy CM, Oskarsson T. Tenascin C in metastasis: a view from the invasive front. Cell Adhes Migr. 2015;9(1–2):112–24. https://doi.org/10.1080/19336918.2015.1008331.
Martina E, Degen M, Rüegg C, Merlo A, Lino MM, Chiquet-Ehrismann R, Brellier F. Tenascin-W is a specific marker of glioma-associated blood vessels and stimulates angiogenesis in vitro. FASEB J. 2010;24(3):778–87. https://doi.org/10.1096/fj.09-140491.
Meloty-Kapella CV, Degen M, Chiquet-Ehrismann R, Tucker RP. Avian tenascin-W: expression in smooth muscle and bone, and effects on calvarial cell spreading and adhesion in vitro. Dev Dyn. 2006;235(6):1532–42.
Meloty-Kapella CV, Degen M, Chiquet-Ehrismann R, Tucker RP. Effects of tenascin-W on osteoblasts in vitro. Cell Tissue Res. 2008;334(3):445–55. https://doi.org/10.1007/s00441-008-0715-4.
Midwood KS, Valenick LV, Hsia HC, Schwarzbauer JE. Coregulation of fibronectin signaling and matrix contraction by tenascin-C and syndecan-4. Mol Biol Cell. 2004;15(12):5670–7.
Murphy-Ullrich JE, Lightner VA, Aukhil I, Yan YZ, Erickson HP, Höök M. Focal adhesion integrity is downregulated by the alternatively spliced domain of human tenascin. J Cell Biol. 1991;115(4):1127–36.
Neidhardt J, Fehr S, Kutsche M, Löhler J, Schachner M. Tenascin-N: characterization of a novel member of the tenascin family that mediates neurite repulsion from hippocampal explants. Mol Cell Neurosci. 2003;23(2):193–209.
Orend G, Chiquet-Ehrismann R. Tenascin-C induced signaling in cancer. Cancer Lett. 2006;244(2):143–63.
Oskarsson T, Acharyya S, Zhang XH, Vanharanta S, Tavazoie SF, et al. Breast cancer cells produce tenascin C as a metastatic niche component to colonize the lungs. Nat Med. 2011;17(7):867–74.
Scherberich A, Tucker RP, Samandari E, Brown-Luedi M, Martin D, Chiquet-Ehrismann R. Murine tenascin-W: a novel mammalian tenascin expressed in kidney and at sites of bone and smooth muscle development. J Cell Sci. 2004;117(Pt 4):571–81.
Scherberich A, Tucker RP, Degen M, Brown-Luedi M, Andres AC, Chiquet-Ehrismann R. Tenascin-W is found in malignant mammary tumors, promotes alpha8 integrin-dependent motility and requires p38MAPK activity for BMP-2 and TNF-alpha induced expression in vitro. Oncogene. 2005;24(9):1525–32.
Tucker RP, Drabikowski K, Hess JF, Ferralli J, Chiquet-Ehrismann R, Adams JC. Phylogenetic analysis of the tenascin gene family: evidence of origin early in the chordate lineage. BMC Evol Biol. 2006;6:60. https://doi.org/10.1186/1471-2148-6-60.
Tucker RP, Ferralli J, Schittny JC, Chiquet-Ehrismann R. Tenascin-C and tenascin-W in whisker follicle stem cell niches: possible roles in regulating stem cell proliferation and migration. J Cell Sci. 2013;126(Pt 22):5111–5. https://doi.org/10.1242/jcs.134650.
Tucker RP, Chiquet-Ehrismann R. Tenascin-C: its functions as an integrin ligand. Int J Biochem Cell Biol. 2015;65:165–8. https://doi.org/10.1016/j.biocel.2015.06.003.
Weber P, Montag D, Schachner M, Bernhardt RR. Zebrafish tenascin-W: a new member of the tenascin family. J Neurobiol. 1998;35(1):1–16.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2018 Springer International Publishing AG
About this entry
Cite this entry
Degen, M., Tucker, R.P. (2018). Tenascin-W (Tnn, TNN). In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, Cham. https://doi.org/10.1007/978-3-319-67199-4_101623
Download citation
DOI: https://doi.org/10.1007/978-3-319-67199-4_101623
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-319-67198-7
Online ISBN: 978-3-319-67199-4
eBook Packages: Biomedical and Life SciencesReference Module Biomedical and Life Sciences