Encyclopedia of Signaling Molecules

2018 Edition
| Editors: Sangdun Choi

Tenascin-C (TNC, Tnc)

Reference work entry
DOI: https://doi.org/10.1007/978-3-319-67199-4_101622


Historical Background

Tenascins are extracellular matrix glycoproteins with subunits composed of epidermal growth factor (EGF)-like repeats, fibronectin type III (FNIII) domains, and a C-terminal fibrinogen-related domain (Chiquet-Ehrismann and Tucker 2011). Tenascins trimerize via heptad repeats found near their N-terminus, and, in at least some cases, two tenascin trimers can form a hexabrachion. In most vertebrates there are four paralogous tenascins: tenascin-C, tenascin-R, tenascin-W, and tenascin-X. The best studied and first to be discovered is tenascin-C, which was independently identified as an antigen or extract in tumors, tendons, muscles, bones, and developing brain. The name tenascin was adopted for this protein by Chiquet-Ehrismann and colleagues from the Latin verbs tenere (to hold) and nasci (to be born) reflecting its prominent expression in tendons and embryos, respectively (Chiquet-Ehrismann et al. 1986). The “C” of tenascin-C corresponds to cytotactin, which was the name given this protein by Grumet and colleagues (Grumet et al. 1985).

A number of alternatively spliced tenascin-C variants have been identified. In birds and mammals, there are eight constant FNIII repeats, but one or more variable FNIII repeats can be spliced between the fifth and sixth constant repeats. The first detailed study of these splice variants in chick described four variable FNIII repeats that were called FNIIIA, FNIIIB, FNIIIC, and FNIIID (Tucker et al. 1994). Later, additional FNIII repeats were found between FNIIIB and FNIIIC; these were named FNIIIAD2 and FNIIIAD1 for “ADditional” repeats (Derr et al. 1997). Similar naming schemes are used to describe the homologous repeats in mouse and human (Fig. 1a).
Tenascin-C (TNC, Tnc), Fig. 1

The domain architecture of tenascin-C from chicken, mouse, and human (a). Different combinations of variable FNIII domains can be found between the fifth and sixth constant FNIII domains. For the sake of simplicity, the forms illustrated here show all of the potential variable domains even though such large forms of the protein have not been described. Rotary shadowing reveals tenascin-C is a hexabrachion (b). (Image reproduced with permission from Chiquet-Ehrismann et al. (1988)). Cells in culture do not spread on tenascin-C. Neural crest cells migrating from explanted neural tubes will migrate on both tenascin-C (c) and fibronectin (d)-coated tissue culture plastic, but the cells remain rounded on tenascin-C while they spread on fibronectin. (Images reproduced from Mackie et al. (1988)). Tenascin-C added to the medium of chicken embryo fibroblasts will block adhesion and spreading on fibronectin-coated substrata (e) (Figure adapted from data presented in Chiquet-Ehrismann et al. (1988))

In 1975, Yamada and colleagues described the agglutination of fixed sheep erythrocytes by fibronectin extracted with urea from chicken embryo fibroblasts (Yamada et al. 1975). However, when fibronectin purified in this way was examined in the electron microscope, it was clear that the preparations were contaminated with a large, previously undescribed six-armed protein (Erickson and Inglesias 1984). The contaminating hexabrachion (Fig. 1b) is now known to be tenascin-C and much, if not all, of the hemagglutinating activity initially attributed to fibronectin was due to the presence of tenascin-C, which is able to agglutinate fixed erythrocytes at concentrations as low as 1.5 μg/ml (Chiquet-Ehrismann et al. 1986). With hindsight it is not surprising that tenascin-C was an undetected contaminant of the fibronectin preparations: tenascin-C and fibronectin are both expressed by chicken embryo fibroblasts, they bind to each other (Chiquet-Ehrismann et al. 1988), and they have almost identical subunit molecular weights, so they migrate together under reducing conditions on polyacrylamide gels.

Tenascin-C was the first extracellular matrix protein to have anti-adhesive or adhesion modulatory properties. When cells are cultured on adhesive glycoproteins like fibronectin or laminin, they typically attach and spread, but when cultured on tenascin-C-coated dishes, cells typically fail to spread and instead remain rounded or form only small lamellipodia (Fig. 1b, c) (Chiquet-Ehrismann et al. 1988). Remarkably, tenascin-C added to the medium over cells cultured on fibronectin-coated substrata inhibits both attachment and spreading in a dose-dependent fashion (Fig. 1d) (Chiquet-Ehrismann et al. 1988). Determining the molecular basis underlying this adhesion modulation became an important research objective during the following decade (see below). Cells plated on tenascin-C-coated substrata were not only less spread; they were often more motile (Mackie et al. 1988). Early studies also showed that exogenous tenascin-C can promote chondrogenesis in vitro and increase the proliferation of Swiss 3T3 and NIH 3T3 cells (Chiquet-Ehrismann and Tucker 2011).

Patterns of Expression

In embryos, tenascin-C was first observed in the tendons and perichondria of developing limbs in the chicken, as well as in smooth muscle, forming lungs, and feather papillae (Chiquet and Fambrough 1984). It was later shown to be highly expressed in the developing central nervous system (Grumet et al. 1985), developing teeth and glands (Chiquet-Ehrismann et al. 1986) and around migrating neural crest cells (Fig. 2a–c) (Mackie et al. 1988). Tenascin-C is also expressed at sites of both intramembranous and endochondral bone formation (Fig. 2d) (Mackie and Tucker 1992). In situ hybridization and variable domain-specific antibodies show that different embryonic tissues express different alternatively spliced variants of tenascin-C (Mackie and Tucker 1992; Tucker et al. 1994). In adult tissues tenascin-C expression is more limited. It persists in certain dense connective tissues like endomysium and tendons (Chiquet and Fambrough 1984) and is also present in some stem cell niches (Fig. 2e) (Chiquet-Ehrismann et al. 2014). Tenascin-C is also present in the adult at sites of trauma, inflammation, and fibrosis (Fig. 2f) (Udalova et al. 2011) and is prominently expressed in the stroma of most solid tumors (see below).
Tenascin-C (TNC, Tnc), Fig. 2

Tenascin-C is present in the extracellular matrix around many motile cells, including neural crest cells (a). In the embryonic day 3 (E3) chicken, immunohistochemistry shows tenascin-C in the space between the dermomyotome (DM) and neural tube (NT) where neural crest cells are found (arrows). Tenascin-C is also present in developing teeth (b). Here a pre-eruption maxillary molar from a postnatal day 4 (P4) mouse is shown following immunohistochemistry with an anti-tenascin-C (M, papillary mesenchyme; O, odontoblast layer; CT, overlying connective tissue). Tenascin-C is also found in many parts of the developing central nervous system (c), including the dentate gyrus (DG) and CA1 region of the murine hippocampus at P6. Anti-tenascin-C immunohistochemistry of a section through the middle phalanx of a mouse toe (d) shows the expression of tenascin-C in developing bone (B) and periosteum (arrow), as well as in tendons (T) and adjacent to the bulge of hair follicles (arrowhead). Tenascin-C expression is greatly reduced in adult tissues, but it persists in some stem cell niches. For example, it is found in the trabecular region (TR) between the bulge (B) and fibrous capsule (C) of adult mouse whiskers (e). Tenascin-C is also expressed following tissue injury (f). In healing skin incisions, tenascin-C is found in the granulation tissue (GT) underlying the epidermis (E) adjacent to the wound (*)

Adhesion Modulation, Integrin Signaling, and Growth Factor Interactions

The key observations that eventually led to understanding the molecular mechanisms underlying tenascin-C’s modulation of cell adhesion to fibronectin were made by Huang and colleagues (Huang et al. 2001). They showed that cells expressing different levels of the fibronectin receptor α5β1 integrin were equally inhibited by tenascin-C from spreading on fibronectin, indicating that tenascin-C was unlikely to be acting as a competitor of the fibronectin receptor. They went on to show that the 13th FNIII domain of fibronectin (FNIII13) binds to immobilized tenascin-C, that FNIII13 co-immunoprecipitates with tenascin-C, and that exogenous FNIII13 inhibits tenascin-C binding to fibronectin. As FNIII13 was reported by others to be the site where the transmembrane receptor syndecan-4 binds to fibronectin and that syndecan-4 helps promote cell spreading on fibronectin, Huang and colleagues next demonstrated that cells overexpressing syndecan-4 (but not cells overexpressing syndecan-1 or syndecan-2) are able to spread on fibronectin even in the presence of tenascin-C. Others went on to show that cells from syndecan-4 knockout mice cultured on fibronectin remain spread in the presence of tenascin-C and that tenascin-C does induce rounding in these cells following transfection with a syndecan-4 expression vector (Midwood et al. 2004). These authors also showed that tenascin-C interfering with fibronectin/syndecan-4 interactions leads to an inhibition of RhoA activation as well as the inhibition of focal adhesion kinase, ultimately leading to the loss of stress fibers and focal adhesions (Fig. 3a). Interestingly, the cells that are inhibited from spreading on fibronectin by tenascin-C blocking syndecan-4/fibronectin interactions proliferate at a higher rate than cells cultured on fibronectin alone (Huang et al. 2001). This may contribute to tumor growth, as fibronectin and tenascin-C are typically co-expressed in tumor stroma (see below).
Tenascin-C (TNC, Tnc), Fig. 3

Tenascin-C is an adhesion modulatory protein. One mode of tenascin-C action is to prevent fibronectin/syndecan-4 interactions (a). This alters fibronectin-mediated signaling by integrins, leading to reduced stress fibers, focal adhesions, and matrix contraction. Tenascin-C is also able to signal directly as an integrin ligand (b). Tenascin-C expression can be upregulated by mechanical strain through SRF-independent, SAP-dependent MKL-1 signaling (c)

In addition to influencing cell behavior indirectly by blocking fibronectin/syndecan-4 interactions, tenascin-C can act directly on cell behavior as an integrin ligand. Tenascin-C from most, but not all, species has an RGD motif in FNIII3 that is found in the same exposed loop as the integrin-binding RGD motif of fibronectin’s FNIII10 (Tucker and Chiquet-Ehrismann 2015). There is experimental evidence that α8β1, αVβ6, and αVβ3 integrins may recognize this RGD motif. A second, more highly conserved integrin-binding tripeptide motif, IDG, is found in a loop between the B and C beta sheets of the same FNIII3 of tenascin-C. This IDG motif is recognized by α9β1 integrin. In addition, the binding of tenascin-C to α7β1 integrin was mapped to the one the variable FNIII domains. Tenascin-C can promote cell proliferation by activating α9β1 and αVβ3 integrins, and activation of α9β1 and α7β1 integrins can influence cell differentiation. These latter two integrins also appear to play roles in promoting cell motility. The effects of integrin-mediated tenascin-C signaling on cell behavior are summarized in Fig. 3b.

Tenascin-C can bind to a number of growth factors via its FNIII5, including members of the FGF, PDGF, and TGFβ family (De Laporte et al. 2013). Tenascin-C also co-immunoprecipitates with the signaling molecule Wnt3a (Hendaoui et al. 2014). When tenascin-C and Wnt3a are added to the medium of cells containing a reporter construct, there is reduced β-catenin-mediated Wnt3a signaling. However, when Wnt3a is added to tenascin-C coating the surface of tissue culture plastic, Wnt3a signaling is enhanced (Hendaoui et al. 2014). These observations indicate that binding of growth and signaling factors by tenascin-C can both inhibit and promote the properties of these factors, depending on whether or not the tenascin-C is soluble or bound to a substratum.

Regulation of Expression

During embryogenesis, tenascin-C is frequently distributed in segmental patterns. Prrx1 (paired related homeobox 1; formerly called Prx1 or Mhox) is a transcription factor important for limb and craniofacial morphogenesis, with a similar embryonic expression pattern as tenascin-C. Prrx1 transactivates the mouse tenascin-C gene by recognizing a conserved homeodomain binding sequence in its promoter. Two more homeobox transcription factors, Pou3F2 and Otx2, regulate tenascin-C gene expression by direct binding to its promoter. Pou3F2 stimulates whereas Otx2 suppresses transcriptional activity. In contrast, Evx1 (even-skipped homeobox 1) acts in synergy with Jun/Fos transcription factors and indirectly activates the tenascin-C gene; the latter factors target an AP1 site in the promoter. Finally, Sox4 is overexpressed in many human tumors together with tenascin-C and stimulates its expression. The regulation of tenascin-C expression was recently reviewed (Chiovaro et al. 2015).

Tenascin-C is strongly expressed de novo in inflammation, wound healing, and cancer (Chiquet-Ehrismann and Chiquet 2003). Inflammatory cytokines have been shown to induce the protein, but it has not been studied yet how they control tenascin-C transcription on the promoter level. Transforming growth factor-β (TGF-β), which is important for tissue regeneration, signals via Smad transcription factors, and two Smad2/3 binding sites were shown to be responsible for activation of the tenascin-C promoter by TGF-β in human fibroblasts. During wound healing, platelet-derived growth factor regulates tenascin-C expression via the PI3K/Akt signaling pathway, which induces binding of SP1 and Ets transcription factors to the respective consensus sequences in its gene promoter. In addition to soluble growth factors, cell-bound ligands Delta and Jagged induce tenascin-C by binding and activating their transmembrane receptor Notch. The cleaved intracellular domain of Notch translocates to the nucleus and stimulates transcription of the tenascin-C gene. Constitutive Notch2 signaling is presumably responsible for the large accumulation of tenascin-C in glioblastomas. Finally, tenascin-C expression is known to be strongly suppressed by glucocorticoids, but the mechanism has not been elucidated on the gene promoter level. These studies have recently been reviewed (Chiquet-Ehrismann and Tucker 2011).

As expected from its occurrence in weight-bearing tissues such as ligaments and tendons, tenascin-C expression is clearly regulated by tensile stress. For example, tenascin-C was shown to accumulate in arterial walls of hypertensive rats and to be induced de novo in skeletal muscle endomysium in response to eccentric overload (for review, see Chiquet et al. 2009). In vitro, the mechanotransduction pathway that leads from cyclic stretching of embryonic fibroblasts to the induction of the tenascin-C gene has been fully elucidated. In these cells, cyclic strain applied to the elastic culture substrate is transduced into activation of small GTPase RhoA and the downstream Rho-dependent kinase, ROCK. Gene knockout experiments showed that mechanical activation of this pathway depends on pericellular fibronectin, cellular a5b1 integrin, and integrin-linked kinase, which is required for the formation of fibrillar adhesions (Chiquet et al. 2009). Strain-activated RhoA/ROCK induces the formation of actin stress fibers in fibroblasts. The resulting depletion of cytoplasmic G-actin is monitored by the actin sensor and transcriptional regulator megakaryocytic leukemia-1 (MKL-1), which translocates to the nucleus. In response to cyclic strain, nuclear MKL-1 initiates tenascin-C gene transcription both indirectly as a co-factor of SRF (serum response factor) and directly by binding to the proximal gene promoter region (Fig. 3c) (Asparuhova et al. 2011). In other cell types, tenascin-C was shown to be induced by alternative mechanotransduction pathways. In cardiomyocytes, for example, cyclic strain leads to release of reactive oxygen species and activation of NFkB (nuclear factor kappa B), which stimulates transcription of the tenascin-C gene by binding to a consensus sequence in its promoter. In arterial smooth muscle cells, stretch primarily activates the Jun kinase pathway. This induces the synthesis of transcription factor NFAT5, which consequently binds to and activates the tenascin-C gene promoter (reviewed in Chiovaro et al. 2015).

Rheumatoid Arthritis and Inflammation

Tenascin-C is elevated in joints during rheumatoid arthritis (RA) and is necessary for inflammation in a mouse model of RA, and tenascin-C can activate Toll-like receptor 4 (TLR4) in macrophages (Midwood et al. 2009; Goh et al. 2010). TLR4 recognizes lipopolysaccharides (LPS) on the surface of Gram-negative bacteria, which leads to the upregulation of proinflammatory cytokines to fight infection. When sepsis is induced in mice by the injection of LPS, the mice experience weight loss, reduced motility, and diarrhea. However, tenascin-C knockout mice fail to develop these symptoms (Piccinini and Midwood, 2012). The levels of TNF-α, IL-6, CXCL1, and IL-10 are elevated in bone marrow-derived macrophages from wild-type mice following exposure to LPS, but they remain unchanged in cells from tenascin-C knockout animals (Piccinini and Midwood, 2012). These and other observations support the hypothesis that tenascin-C is an early response gene that mediates signaling by TLR4 during inflammation both during infection and RA.

Cancer Biology

Tenascin-C is found in the stroma of most solid tumors (Orend and Chiquet-Ehrismann 2006, Chiquet-Ehrismann and Tucker 2011). In glioblastomas and melanomas, the source of tenascin-C are the tumors cells themselves, but in carcinomas tumor-associated fibroblasts are producing tenascin-C. In high-grade tumors tenascin-C with variable FNIII domains predominates. Experimental evidence supports roles for tenascin-C promoting both angiogenesis and metastasis (Chiquet-Ehrismann and Tucker 2011, Lowy and Oskarsson 2015). miR335 can inhibit metastasis in a mouse model via the downregulation of Sox4 and tenascin-C, and tenascin-C is a signature gene mediating lung metastasis of breast cancer. Clinical studies using iodine-131 or yttrium-90 labeled anti-tenascin-C for intracavitary radioimmunotherapy showed significant increases in postsurgery longevity in patients with astrocytoma or glioblastoma (Reulen et al. 2015).


Tenascin-C is found in the extracellular matrix of vertebrate embryos, and in vitro it typically promotes cell proliferation and migration. Tenascin-C acts both directly as an integrin ligand and by interfering with fibronectin/syndecan-4 interactions, thus altering fibronectin-mediated cell signaling. Tenascin-C reappears during inflammation, wound healing, and cancer, and its expression is upregulated by tensile stress as well as by TGF-β, Notch, and PI3K/Akt signaling pathways. Future challenges include refining the use of anti-tenascin-C as a tumor marker and a target for radioimmunotherapy.

See Also


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Copyright information

© Springer International Publishing AG 2018

Authors and Affiliations

  1. 1.Department of Cell Biology and Human AnatomyUniversity of CaliforniaDavisUSA
  2. 2.Department of Orthodontics and Dentofacial OrthopedicsUniversity of BernBernSwitzerland