Malignant myoepithelioma is a rare neoplasm of salivary gland which may either arise de novo or develop in a pre-existing pleomorphic adenoma. The malignant myoepithelioma occurs in 0.45% of major salivary gland tumors. Malignant myoepitheliomas arising in the pleomorphic adenoma number less than 20 in English literature and 1 in Korea. We describe a case of malignant myoepithelioma arising in a recurrent pleomorphic adenoma of the left parotid gland of a 61-year-old man. The tumor was ill-defined and composed of polygonal or plasmacytoid myoepithelial cells.
Infiltration to surrounding tissue, hemorrhage, necrosis, increased mitotic activity and vascular tumor emboli indicated its malignant nature. There were several satellite nodules with histologic features of typical pleomorphic adenoma. Immunohistochemically, tumor cells were reactive for S-100 protein, AE1/AE3, vimentin, smooth muscle actin and glial fibrillary acid protein.
Malignant myoepithelioma (myoepithelial carcinoma), is a very rare malignant epithelial neoplasm accounting for less than 1% of all salivary gland tumors and has an intermediate malignant potential. We report a case of malignant myoepithelioma arising in the left parotid gland in a 54-year-old man, which was difficult to differentiate from pleomorphic adenoma and other malignant salivary gland neoplasms. Fine needle aspiration cytology of the parotid gland showed cellular smear, composed of overlapped sheets and clusters or individually scattered tumor cells without any acinic or ductal structures. The tumor cells were rather uniform, with distinct cell borders and moderate amount of cytoplasm. The eccentrically located nuclei were oval to round and pleomorphic and showed prominent nucleoli. A few clear cells were noted in the cellular aggregates.
Metachromatic matrix was seen between individual tumor cells in a lacelike fashion, resembling pleomorphic adenoma.
According to the immunohistochemical staining, we recognized that the component cells are myoepithelial in nature, showing reactivity for the S-100 protein, vimentin, and actin.