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Specific expression of tenascin in human colonic neoplasms.

Tenascin, a novel six-armed extracellular matrix glycoprotein, was immunohistochemically examined in the human normal adult colon, and colonic neoplasms such as tubular adenomas, primary and metastatic adenocarcinomas. In contrast to previous reports, tenascin was hardly detectable in the normal adu...

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Detalles Bibliográficos
Autores principales: Sakai, T., Kawakatsu, H., Hirota, N., Yokoyama, T., Sakakura, T., Saito, M.
Formato: Texto
Lenguaje:English
Publicado: Nature Publishing Group 1993
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1968444/
https://www.ncbi.nlm.nih.gov/pubmed/7684238
Descripción
Sumario:Tenascin, a novel six-armed extracellular matrix glycoprotein, was immunohistochemically examined in the human normal adult colon, and colonic neoplasms such as tubular adenomas, primary and metastatic adenocarcinomas. In contrast to previous reports, tenascin was hardly detectable in the normal adult colons, being predominantly localised in the fibrous stroma surrounding the glandular epithelia of the neoplastic lesions. The neoplastic cells themselves were totally negative for tenascin expression. Both the tubular adenoma tissues and the superficial layer of well-differentiated adenocarcinomas in general were intensely reactive to tenascin antibody, and the staining intensity increased as the adenoma became more atypical in cases of tubular adenomas. By pretreatment of the paraffin-embedded tissue sections with pepsin, the distribution of tenascin was often intensified considerably and distinct localisation was more clearly demonstrated in the colonic tumour tissues. Tenascin was also biochemically purified from human invasive colonic carcinomas, and this cancerous tissue tenascin was compared with that extracted from a human umbilical cord fibroblast cell line in terms of molecular heterogeneity. Two major isoforms of the purified tenascin from colonic cancer tissues were found to have relative molecular masses of 250 kD and 190 kD, which were almost identical to those of human foetal fibroblast tenascin glycoproteins. In addition, several lower molecular weight isoforms were frequently detectable in the cancerous tissues, which might represent immuno-reactive tenascin isoforms proteolytically digested in human colonic carcinomas in vivo. IMAGES: