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The **Tenascin-C extra-domain A1** refers to a specific alternatively spliced fibronectin type III (FNIII) domain (A1) within the larger Tenascin-C glycoprotein. Tenascin-C is a large, hexameric extracellular matrix protein involved in tissue remodeling, cell adhesion, migration, and immune regulation. The A1 domain is present in certain splice variants of Tenascin-C, commonly upregulated in malignant, inflammatory, or regenerative contexts but absent from most healthy adult tissues[1][3]. Expression of A1-containing isoforms has been observed in gliomas and other tumors, implicating this domain in oncogenesis and tumor progression as well as in neurodevelopment. The interaction of Tenascin-C (including its A1 domain) with cell surface receptors (e.g., integrins, EGF receptor, Toll-like receptor-4) and with the extracellular matrix mediates key functional effects on cell behavior, making it a potential target for biomarker and therapeutic strategies in oncology and regenerative medicine[4][1][3].
Antibody-based approaches generally function by blocking TNC interactions responsible for immunomodulation, cell adhesion, or migration. Therapeutic targeting may disrupt cancer-stroma interactions or modulate immune cell recruitment and activation.
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