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- Title
The use of thrombomodulin to study epithelial cell differentiation in neoplastic and non-neoplastic oral lesions.
- Authors
Tabata, Masashi; Yonezawa, Suguru; Sugihara, Kazumasa; Yamashita, Sukehide; Maruyama, Ikuro; Tabata, M; Yonezawa, S; Sugihara, K; Yamashita, S; Maruyama, I
- Abstract
The quantification of argyrophilic nucleolar organizer regions (AgNOR) was performed in 34 cases of adenoid cystic carcinoma (ACC) to determine (1) whether AgNOR count correlates with its different histologic grades pertinent to prognosis, and (2) whether AgNOR counts can offer any additional prognostic advantage over histologic grading. According to SZANTO et al.'s histologic grading criteria (4), 12 cases were Grade 1, 7 cases Grade 2, and 15 were Grade 3. Patients were divided into 20 favorable cases (without metastases) and 14 unfavorable cases (with metastases). Although most Grade 3 tumors had high AgNOR counts (&ges;4) and Grade 1 tumors with low (<4) AgNOR counts outnumbered those with high AgNOR counts, considerable overlap of AgNOR values in different grades was observed. However, all unfavorable cases had high AgNOR counts regardless of their histologic grades, suggesting that the metabolic alterations associated with the malignancy level of ACC may partly be portrayed by the AgNOR count, irrespective of the histologic appearance. Cumulative survival rates of Grade 1 tumors and of tumors with low AgNOR counts were better than those of Grade 3 tumors and those with high AgNOR counts. Within the limited number of cases in this series the AgNOR count exhibits a potential for identifying some aggressive ACCs that cannot be detected by histology alone.adenoid cystic carcinoma, AgNOR, histologic grading, prognosis. Thrombomodulin (TM) is a glycoprotein originally isolated from rabbit lung vasculature and characterized as a natural endothelial anticoagulant. Thrombin binds to TM noncovalently with high affinity. Thrombin - TM complexes can activate protein C efficiently. Activated protein C inactivates factors Va and VIIIa and regulates the blood coagulation cascade. Thus TM converts thrombin from a procoagulant protease to an anticoagulant. TM is found on endothelial cells in veins, arteries and capillaries. Our previous study has shown that TM is also expressed on the cell surface of squamous epithelium. In the present study, we aimed to disclose differences in TM expression among normal, dysplastic, and malignant squamous epithelium in human oral mucosa by counting TM-positive cells in each lesion. TM was uniformly expressed in the spinous layer of normal human oral squamous epithelium. The number of TM-positive cells was not significantly different between normal epithelium, lichen planus and mild dysplasia. In contrast, in moderate and severe dysplasia and well-differentiated squamous cell carcinoma (SCC), there were significantly fewer positive cells compared with normal epithelium. In SCCs, the periphery and the central keratinized area of tumor islands were often negative. The proportion of TM-positive cells in poorly differentiated SCC was significantly lower than in well-differentiated SCC. These results indicate that TM may have diagnostic value in the histological examination of oral premalignant and malignant lesions.
- Subjects
THROMBOMODULIN; EPITHELIAL cells; BLOOD coagulation; ADENOID cystic carcinoma; TUMORS; EPITHELIUM; CELL differentiation; CELL receptors; COMPARATIVE studies; ENDOTHELIUM; GENES; RESEARCH methodology; MEDICAL cooperation; ORAL diseases; MOUTH tumors; ORAL mucosa; PRECANCEROUS conditions; RESEARCH; SQUAMOUS cell carcinoma; EVALUATION research; ORAL lichen planus; CELL physiology
- Publication
Journal of Oral Pathology & Medicine, 1995, Vol 24, Issue 10, p443
- ISSN
0904-2512
- Publication type
journal article
- DOI
10.1111/j.1600-0714.1995.tb01131.x