Tenascins

Chiquet‐Ehrismann, Ruth

doi:10.1002/0471203076.emm0606

Cited by 4 publications

(4 citation statements)

References 30 publications

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“…When compared two by two, the degree of similarity is strongly increased, showing that FBG-like domains share more than 50% of sequence identity and at least 65% of similarity, except for FBG-X and FBG-W, which appeared to be the most divergent ones. Consequently, FBG-C seems to be closer to FBG-R and FBG-W, and FBG-X seems to be the most distant domain of the Tenascin family (still with >47% identity with its counterparts), as previously suggested by Chiquet-Ehrismann ( 43 ). Nevertheless, this high degree of homology between FBG-like domains strengthens the idea that latent TGF-β activation might be a common property to all members of the Tenascin family.…”

Section: Resultssupporting

confidence: 68%

Latent TGF-β Activation Is a Hallmark of the Tenascin Family

et al. 2021

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Transforming growth factor-β (TGF-β) isoforms are secreted as inactive complexes formed through non-covalent interactions between bioactive TGF-β entities and their N-terminal pro-domains called latency-associated peptides (LAP). Extracellular activation of latent TGF-β within this complex is a crucial step in the regulation of TGF-β activity for tissue homeostasis and immune cell function. We previously showed that the matrix glycoprotein Tenascin-X (TN-X) interacted with the small latent TGF-β complex and triggered the activation of the latent cytokine into a bioactive TGF-β. This activation most likely occurs through a conformational change within the latent TGF-β complex and requires the C-terminal fibrinogen-like (FBG) domain of the glycoprotein. As the FBG-like domain is highly conserved among the Tenascin family members, we hypothesized that Tenascin-C (TN-C), Tenascin-R (TN-R) and Tenascin-W (TN-W) might share with TN-X the ability to regulate TGF-β bioavailability through their C-terminal domain. Here, we demonstrate that purified recombinant full-length Tenascins associate with the small latent TGF-β complex through their FBG-like domains. This association promotes activation of the latent cytokine and subsequent TGF-β cell responses in mammary epithelial cells, such as cytostasis and epithelial-to-mesenchymal transition (EMT). Considering the pleiotropic role of TGF-β in numerous physiological and pathological contexts, our data indicate a novel common function for the Tenascin family in the regulation of tissue homeostasis under healthy and pathological conditions.

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Section: Resultssupporting

confidence: 68%

Latent TGF-β Activation Is a Hallmark of the Tenascin Family

et al. 2021

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“…The expression in the bone and muscle is also regulated by mechanical loading (Webb et al, 1997;Fluck et al, 2000). In fact, in the promoter region of the TN-C genome, an element sensitive to mechanical stress has been found (Chiquet-Ehrismann et al, 1994). Therefore, the TN-C protein in the diseased disks may also be directly upregulated by mechanical stress.…”

Section: Discussionmentioning

confidence: 99%

Effect of hypoxia and interleukin‐1β on expression of tenascin‐C in temporomandibular joint

et al. 2007

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“…This characteristic is shared with the other members of the tenascin family. Indeed, tenascin-R is expressed only in the nervous system, tenascin-X is prominently expressed in muscle and skin, whereas tenascin-C is present in more developing tissues, including the nervous system (Chiquet-Ehrismann, 2002). The pattern of tenascin-W expression during development suggests that it is likely to be involved in specific events during embryogenesis, like palate formation, osteogenesis and smooth muscle development.…”

Section: Discussionmentioning

confidence: 99%

Murine tenascin-W: a novel mammalian tenascin expressed in kidney and at sites of bone and smooth muscle development

Scherberich

Tucker

Samandari

et al. 2004

Journal of Cell Science

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We cloned and characterized a novel member of the tenascin family of extracellular matrix proteins - the murine orthologue of zebrafish tenascin-W. Full-length recombinant tenascin-W was expressed and purified from mammalian cell cultures. Rotary shadowing followed by electron microscopy showed that tenascin-W forms hexabrachions. We studied its expression during development and in the adult by immunohistochemistry, in situ hybridization and immunoblotting. Tenascin-W is expressed during palate formation, osteogenesis and smooth muscle development. In the adult, tenascin-W is found in the kidney, cardiac semilunar valves, corneal limbus and periosteum. Tenascin-W and tenascin-C expression overlap in many of these areas. Bone-morphogenic-protein-2 treated C2C12 cells secrete tenascin-W and are able to adhere to and to extend actin-rich processes on a tenascin-W substratum. In vitro, cells bind to tenascin-W in an RGD-dependent manner. This adhesion is increased by transfection of α8 integrin, which localizes with tenascin-W in the periosteum and kidney.

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Tenascins

Cited by 4 publications

References 30 publications

Latent TGF-β Activation Is a Hallmark of the Tenascin Family

Latent TGF-β Activation Is a Hallmark of the Tenascin Family

Effect of hypoxia and interleukin‐1β on expression of tenascin‐C in temporomandibular joint

Murine tenascin-W: a novel mammalian tenascin expressed in kidney and at sites of bone and smooth muscle development

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