Myoepithelial tumors of salivary glands: a clinicopathologic, immunohistochemical, ultrastructural, and flow-cytometric study. 1996

L Alós, and A Cardesa, and J A Bombí, and C Mallofré, and A Cuchi, and J Traserra
Department of Pathology, Hospital Clínic i Provincial, University of Barcelona Medical School, Spain.

Myoepitheliomas of the salivary glands remain a controversial entity. To contribute to the knowledge of this entity, 16 myoepithelial tumors of the salivary glands were studied: 12 benign myoepitheliomas (BME) and 4 malignant myoepitheliomas (MME). The clinical and the histologic findings of each case were studied Immunohistochemistry and flow-cytometry analysis were performed from the paraffin-embedded material in 15 cases. An electron-microscopy study was performed in 8 cases. The myoepithelial tumors affected patients of both sexes equally. The mean age of the patients with BME was 54 years, and the mean age of patients with MME was 62 years. Eight cases of BME originated in the parotid gland and 4 cases originated in the minor salivary glands. All the MME developed from a benign preexistent tumor: two developed from a pleomorphic adenoma in the parotid gland, and the other two MME developed in the minor salivary gland from a BME. The myoepithelial tumors were composed of epithelioid, plasmacytoid, spindle, or clear cell types, and they showed a solid or a myxoid pattern of growth. Immunohistochemical studies revealed marked and diffuse positivity to cytokeratins, vimentin, and S-100 protein in all cases. Glial fibrillary acidic protein was positive in 8 cases (53%), and muscle-specific actin and smooth-muscle actin were positive in only 3 cases (20%); they were all cases of BME. Desmin was negative in all tumors. Ultrastructural studies showed the presence of basal membrane, tight junctions, intermediate filaments, and microvilli as well as actin-like filaments lacking focal densities in all cases. But actin-like filaments with focal densities were not identified. Flow cytometry determined that all BME were diploid with a mean proliferative index of 7.73%. Two of the MME were diploid and the other two MME were aneuploid. The mean proliferative index of MME was 11.93%. In conclusion, BME and MME originated in major and minor salivary glands can display different histologic patterns and cellular features. Some immunohistochemical and ultrastructural characteristics have been found in all these neoplasms, which supports the idea that myoepitheliomas are composed by neoplastic modified myoepithelial cells, not fully differentiated. These techniques can be useful for the diagnosis of these tumors.

UI MeSH Term Description Entries
D007150 Immunohistochemistry Histochemical localization of immunoreactive substances using labeled antibodies as reagents. Immunocytochemistry,Immunogold Techniques,Immunogold-Silver Techniques,Immunohistocytochemistry,Immunolabeling Techniques,Immunogold Technics,Immunogold-Silver Technics,Immunolabeling Technics,Immunogold Silver Technics,Immunogold Silver Techniques,Immunogold Technic,Immunogold Technique,Immunogold-Silver Technic,Immunogold-Silver Technique,Immunolabeling Technic,Immunolabeling Technique,Technic, Immunogold,Technic, Immunogold-Silver,Technic, Immunolabeling,Technics, Immunogold,Technics, Immunogold-Silver,Technics, Immunolabeling,Technique, Immunogold,Technique, Immunogold-Silver,Technique, Immunolabeling,Techniques, Immunogold,Techniques, Immunogold-Silver,Techniques, Immunolabeling
D007633 Keratins A class of fibrous proteins or scleroproteins that represents the principal constituent of EPIDERMIS; HAIR; NAILS; horny tissues, and the organic matrix of tooth ENAMEL. Two major conformational groups have been characterized, alpha-keratin, whose peptide backbone forms a coiled-coil alpha helical structure consisting of TYPE I KERATIN and a TYPE II KERATIN, and beta-keratin, whose backbone forms a zigzag or pleated sheet structure. alpha-Keratins have been classified into at least 20 subtypes. In addition multiple isoforms of subtypes have been found which may be due to GENE DUPLICATION. Cytokeratin,Keratin Associated Protein,Keratin,Keratin-Associated Proteins,alpha-Keratin,Associated Protein, Keratin,Keratin Associated Proteins,Protein, Keratin Associated,alpha Keratin
D008297 Male Males
D008441 Maxillary Neoplasms Cancer or tumors of the MAXILLA or upper jaw. Maxillary Neoplasm,Neoplasm, Maxillary,Neoplasms, Maxillary
D008854 Microscopy, Electron Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen. Electron Microscopy
D008875 Middle Aged An adult aged 45 - 64 years. Middle Age
D009208 Myoepithelioma A usually benign tumor made up predominantly of myoepithelial cells. Myoepithelial Tumor,Myoepithelial Tumors,Myoepitheliomas,Tumor, Myoepithelial,Tumors, Myoepithelial
D009418 S100 Proteins A family of highly acidic calcium-binding proteins found in large concentration in the brain and believed to be glial in origin. They are also found in other organs in the body. They have in common the EF-hand motif (EF HAND MOTIFS) found on a number of calcium binding proteins. The name of this family derives from the property of being soluble in a 100% saturated ammonium sulfate solution. Antigen S 100,Nerve Tissue Protein S 100,S100 Protein,S-100 Protein,S100 Protein Family,Protein, S100,S 100 Protein
D010307 Parotid Neoplasms Tumors or cancer of the PAROTID GLAND. Cancer of Parotid,Parotid Cancer,Cancer of the Parotid,Neoplasms, Parotid,Cancer, Parotid,Cancers, Parotid,Neoplasm, Parotid,Parotid Cancers,Parotid Neoplasm
D011003 Ploidies The degree of replication of the chromosome set in the karyotype. Ploidy

Related Publications

L Alós, and A Cardesa, and J A Bombí, and C Mallofré, and A Cuchi, and J Traserra
April 1995, American journal of clinical pathology,
L Alós, and A Cardesa, and J A Bombí, and C Mallofré, and A Cuchi, and J Traserra
December 2018, Zhonghua bing li xue za zhi = Chinese journal of pathology,
L Alós, and A Cardesa, and J A Bombí, and C Mallofré, and A Cuchi, and J Traserra
January 1997, Anticancer research,
L Alós, and A Cardesa, and J A Bombí, and C Mallofré, and A Cuchi, and J Traserra
October 1999, Head & neck,
L Alós, and A Cardesa, and J A Bombí, and C Mallofré, and A Cuchi, and J Traserra
April 1999, Virchows Archiv : an international journal of pathology,
L Alós, and A Cardesa, and J A Bombí, and C Mallofré, and A Cuchi, and J Traserra
February 1990, Ophthalmology,
L Alós, and A Cardesa, and J A Bombí, and C Mallofré, and A Cuchi, and J Traserra
September 1992, The American journal of surgical pathology,
L Alós, and A Cardesa, and J A Bombí, and C Mallofré, and A Cuchi, and J Traserra
September 1994, European journal of cancer. Part B, Oral oncology,
L Alós, and A Cardesa, and J A Bombí, and C Mallofré, and A Cuchi, and J Traserra
July 1989, Human pathology,
L Alós, and A Cardesa, and J A Bombí, and C Mallofré, and A Cuchi, and J Traserra
December 2009, Oral oncology,
Copied contents to your clipboard!