Tenascin-C: From Discovery to Structure-Function Relationships

Chiquet, Matthias (2020). Tenascin-C: From Discovery to Structure-Function Relationships. Frontiers in immunology, 11(611789), p. 611789. Frontiers Research Foundation 10.3389/fimmu.2020.611789

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Forty years ago, the tremendous complexity of extracellular matrix (ECM) was still largely an uncharted area, mainly because many of its components could only be solubilized by denaturing agents. Known were just five types of collagens, elastin, a couple of proteoglycans, and a few ECM glycoproteins, among them fibronectin, thrombospondin-1, and laminin-111 (1). The best studied was fibronectin (2), which became notorious for promoting specific cell adhesion to collagens. In parallel, the search for yet undetected large ECM glycoproteins continued. In 1981-82, Carter (3) observed several novel glycoproteins in human fibroblast ECM extracts. Among them, "GP250" was
shown to be distinct from fibronectin but resisted isolation. However, between 1983-85 several research groups independently discovered and characterized a similar ECM glycoprotein that later became known as tenascin-C (see below). Its subunits were comparable in size to fibronectin but instead of dimers formed large (>106 kDa) disulfide-linked oligomers. In the following paragraphs,
the history and context of the individual discoveries of tenascin-C is briefly recounted. I then describe how a combination of methods available at the time lead to a detailed structural model of tenascin-C. This was the basis for trying to assign functions to different parts of the molecule. For reasons outlined below, this turned out to be more difficult than for fibronectin.

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