IMPORTANCE OF CELLULAR LOCALIZATION OF MOESIN AND CD44 VARIANTS IN PATIENTS WITH ORAL SQUAMOUS CELL CARCINOMA
Hiroichi Kobayashi, Takeshi Koike, Atsushi Nakatsuka, Hiroshi Kurita, Kenji Kurashina
Moesin, a member of ERM (ezrin/radixin/moesin) family, links cell surface glycoproteins such as CD44 and CD43 by its globular N-terminal domain. Recent study indicates that membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration. The purpose of this report is to assess whether localization of moesin is similar with localization of CD44 variants in oral squamous cell carcinoma (OSCC) cells if moesin and CD44 variants may shift from cell surface to cytoplasm by MT1-MMP. The expression of moesin and CD44 was evaluated immunohistochemically in paraffin-embedded tissues of 59 specimens of OSCC. Expression pattern of moesin and CD44 variants were divided two groups: membranopus pattern cytoplasmic pattern. Expression pattern of moesin, CD44s, CD44v6 and CD44v7/8 were found to be correlated with histological differentiation, mode of invasion and lymph node metastasis. Expression pattern of moesin was shown to be adversely correlated with expression pattern of CD44s, CD44v6 and CD44v7/8.
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Immunohistochemical evaluation of moesin in malignant salivary neoplasms
Takeshi Koike, Hiroichi Kobayashi,, Sakai Hironori, Jun'nosuke Narikawa, Takahiro Kamata, Atsushi Nakatsuka, Hiroshi Kurita, Kenji Kurashina
Moesin, a member of ERM (ezrin/radixin/moesin) family of proteins, is a cytosollic molecule that crosslinks the plasma membrane to actin filaments. We previously reported clinical significance of cellular distribution of moesin in patients with oral squamous cell carcinoma. Little is knouwn about expression of moesin in malignant salivary neoplasms. Here, moesin expression was investigated by immunohistochemistry in 6 cases of normal salivary gland, 10 cases of adenoid cystic carcinoma (ACC), 8 cases of mucoepidermoid carcinoma (MEC), 3 cases of polymorphous low-grade adenocarcinoma (PLGA), 1 salivary duct carcinoma (SDC), 1 papillary cystadenocarcinoma (PCA), 1 malignant myoepithelioma (MME), 1 epithelial-myoepithelial carcinoma (EMC) and 1 mucinous adenocarcinoma (MAC). In normal salivary gland, moesin was seen in myoepithelial cells around serous secretory acini and mucous secretory acini. Moesin was observed in lateral membrane of serous secretory acini and basal layer cells of the duct. In ACC and PLGA, myoepithelial-like cells showed positive immunoreactivity for moesin, S-100 protein, alpha-SMA, calponin and vimentin, whereas luminal cells showed expression of cytokeratin 7 and cytokeratin 14. In ACC, PLGA and MEC expression pattern of moesin was similar to that of S-100 protein, alpha-SMA, calponin and vimentin. In conclusion, our results suggest that moesin expression may be useful as a new marker for myoepithelial cells of salivary gland neoplasm
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