Intracellular localization of tenascin in squamous cell carcinoma of oral cavity: an immunohistochemical study. 1996

M Mori, and Y Muramatsu, and K Yamada, and P Shrestha, and Y Takai
Department of Oral and Maxillofacial Surgery, Asahi University School of Dentistry, Gifu, Japan.

Tenascin is a multifunctional extracellular matrix glycoprotein generally expressed in epithelial tumors at sites of epithelial tumor-mesenchymal tissue interface. Studies so far have indicated that mesenchymal cells are a major source of tenascin in tumor tissues. The present study evaluated biopsies and surgically resected specimens of oral squamous cell carcinoma from 20 patients for the expression of tenascin using immunohistochemical methods. The normal mucosa included in all surgically resected specimens showed a delicate band in the submucosal connective tissue, with infrequent breaks in continuity in the immediate vicinity of the basement membrane. The hyperplastic/hyperkeratinized or dysplastic mucosa either showed a continuous band or enhanced expression of TN in the submucosal connective tissue. Evaluation of serial sections for immunoreactivity of tenascin in 7 cases of carcinoma showed intracellular localization of tenascin; particularly at the invading fronts of carcinomas of the buccal mucosa and tongue. The results of the present study may imply that despite the possible induction of tenascinllfrom mesenchymal cells by carcinoma cells, carcinoma cells, if they produce tenascin, do so at the invasive fronts.

UI MeSH Term Description Entries
D009061 Mouth Mucosa Lining of the ORAL CAVITY, including mucosa on the GUMS; the PALATE; the LIP; the CHEEK; floor of the mouth; and other structures. The mucosa is generally a nonkeratinized stratified squamous EPITHELIUM covering muscle, bone, or glands but can show varying degree of keratinization at specific locations. Buccal Mucosa,Oral Mucosa,Mucosa, Mouth,Mucosa, Oral
D009062 Mouth Neoplasms Tumors or cancer of the MOUTH. Cancer of Mouth,Mouth Cancer,Oral Cancer,Oral Neoplasms,Cancer of the Mouth,Neoplasms, Mouth,Neoplasms, Oral,Cancer, Mouth,Cancer, Oral,Cancers, Mouth,Cancers, Oral,Mouth Cancers,Mouth Neoplasm,Neoplasm, Mouth,Neoplasm, Oral,Oral Cancers,Oral Neoplasm
D009363 Neoplasm Proteins Proteins whose abnormal expression (gain or loss) are associated with the development, growth, or progression of NEOPLASMS. Some neoplasm proteins are tumor antigens (ANTIGENS, NEOPLASM), i.e. they induce an immune reaction to their tumor. Many neoplasm proteins have been characterized and are used as tumor markers (BIOMARKERS, TUMOR) when they are detectable in cells and body fluids as monitors for the presence or growth of tumors. Abnormal expression of ONCOGENE PROTEINS is involved in neoplastic transformation, whereas the loss of expression of TUMOR SUPPRESSOR PROTEINS is involved with the loss of growth control and progression of the neoplasm. Proteins, Neoplasm
D002294 Carcinoma, Squamous Cell A carcinoma derived from stratified SQUAMOUS EPITHELIAL CELLS. It may also occur in sites where glandular or columnar epithelium is normally present. (From Stedman, 25th ed) Carcinoma, Epidermoid,Carcinoma, Planocellular,Carcinoma, Squamous,Squamous Cell Carcinoma,Carcinomas, Epidermoid,Carcinomas, Planocellular,Carcinomas, Squamous,Carcinomas, Squamous Cell,Epidermoid Carcinoma,Epidermoid Carcinomas,Planocellular Carcinoma,Planocellular Carcinomas,Squamous Carcinoma,Squamous Carcinomas,Squamous Cell Carcinomas
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D014062 Tongue Neoplasms Tumors or cancer of the TONGUE. Cancer of Tongue,Tongue Cancer,Cancer of the Tongue,Neoplasms, Tongue,Cancer, Tongue,Cancers, Tongue,Neoplasm, Tongue,Tongue Cancers,Tongue Neoplasm
D019063 Tenascin Hexameric extracellular matrix glycoprotein transiently expressed in many developing organs and often re-expressed in tumors. It is present in the central and peripheral nervous systems as well as in smooth muscle and tendons. (From Kreis & Vale, Guidebook to the Extracellular Matrix and Adhesion Proteins, 1993, p93) Cytotactin,Hexabrachion,Tenascin-C,J1-200-220,Tenascin C

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