[Myoepithelial differentiation markers in salivary gland neoplasia].
Salivary gland tumors frequently present myoepithelial cell differentiation that is not always easily identified on routinely stained sections. Recently novel markers of myoepithelium have been studied, such as calponin (CALP), caldesmon (CALD), and smooth muscle myosin heavy chain. These markers, together with smooth muscle actin may be useful tools for identifying myoepithelial cells. We immunohistochemically studied a series of 23 benign and malignant salivary gland tumors using antibodies to these four markers. The tumors were classified as follows: pleomorphic adenoma (n = 8), basal cell adenoma (n = 3), myoepithelioma with plasmacytoid cells (n = 2), epithelial-myoepithelial cell carcinoma (n = 6) and adenoid cystic carcinoma (n = 4). All tumors were positive for at least one of the four markers. CALP and smooth muscle actin were the markers more frequently expressed. Positivity was mostly located in the myoepithelial cells that constitute the external layer of the glandular or tubular neoplastic structures. In poorly differentiated epithelial myoepithelial carcinomas, composed of solid sheets of neoplastic cells and sometimes of clear cells, immunohistochemical staining for myoepithelial markers evidenced rudimentary glandular structures. CALP and smooth muscle actin were positive in the two cases of myoepithelioma with plasmacytoid cells. In conclusion, the combined staining with four markers helps to disclose myoepithelial cell differentiation and can be a useful tool for the correct histopathological diagnosis of salivary gland tumors. Among the four markers studied, CALP and smooth muscle actin were the most useful to identify myoepithelial cell differentiation.
Scarpellini
F
F
Dipartimento di Oncologia, Università di Bologna, Ospedale Bellaria, Via Altura 3, I-40139 Bologna, Italia.
Marucci
G
G
Foschini
M P
MP
D000199:Actins / Q000032:analysis; D018262:Adenocarcinoma, Clear Cell / Q000737:chemistry / Q000473:pathology; D000236:Adenoma / Q000737:chemistry / Q000473:pathology; D008949:Adenoma, Pleomorphic / Q000737:chemistry / Q000473:pathology; D000328:Adult; D000368:Aged; D000369:Aged, 80 and over; D000943:Antigens, Differentiation / Q000032:analysis*; D000951:Antigens, Neoplasm / Q000032:analysis*; D002135:Calcium-Binding Proteins / Q000032:analysis; D002148:Calmodulin-Binding Proteins / Q000032:analysis; D002277:Carcinoma / Q000737:chemistry / Q000473:pathology; D003528:Carcinoma, Adenoid Cystic / Q000737:chemistry / Q000473:pathology; D002454:Cell Differentiation; D004847:Epithelial Cells / Q000737:chemistry; D005260:Female; D006801:Humans; D008297:Male; D008840:Microfilament Proteins; D008875:Middle Aged; D009130:Muscle, Smooth / Q000473:pathology; D009208:Myoepithelioma / Q000737:chemistry / Q000473:pathology; D018995:Myosin Heavy Chains / Q000032:analysis; D009363:Neoplasm Proteins / Q000032:analysis; D014411:Neoplastic Stem Cells / Q000737:chemistry; D020033:Protein Isoforms / Q000032:analysis; D012468:Salivary Gland Neoplasms / Q000737:chemistry / Q000473:pathology*; D000096985:Calponins
D000199:Actins; D000943:Antigens, Differentiation; D000951:Antigens, Neoplasm; D002135:Calcium-Binding Proteins; D002148:Calmodulin-Binding Proteins; D008840:Microfilament Proteins; D018995:Myosin Heavy Chains; D009363:Neoplasm Proteins; D020033:Protein Isoforms; D000096985:Calponins
Marcatori di differenziazione mioepiteliale nelle neoplasie delle ghiandole salivari.