Mitochondria-rich normal, metaplastic, and neoplastic cells show overexpression of the epitope H recognized by the monoclonal antibody H.
The epitope H contains an O-linked N-acetylglucosamine (O-GlcNAc) residue in a specific conformation and/or environment recognized by monoclonal antibody H (mAbH). We have previously shown that the epitope H is present in more than one polypeptide and in various types of normal and pathological cells. In the present study, we focused on mitochondria-rich normal, metaplastic, and neoplastic cells, prompted by our recent immuno-electron microscopy findings that mAbH clearly stains the mitochondria of breast epithelial cells in infiltrating ductal breast carcinomas and fibroadenomas. The indirect immunoperoxidase method was applied using the mAbH to investigate the distribution of the epitope H in mitochondria-rich normal cells and in metaplastic and neoplastic oncocytic cells. Immunohistochemical staining for the mAbH was observed in oxyphil cells of parathyroid glands, in striated duct cells of parotid glands, in urinary tubules of kidneys, in parietal cells of gastric body mucosa, in oxyphil cells of Hashimoto's thyroiditis, in epithelial cells of Warthin's tumors of the parotid gland, in neoplastic cells of oxyphil adenomas and carcinomas (Hürthle's tumors) of the thyroid gland, and in neoplastic cells of oncocytomas of the kidneys. The present study shows that the epitope H is strongly expressed in mitochondria-rich normal cells, as well as in metaplastic and neoplastic oncocytic cells, which are known to have cytoplasms packed with mitochondria. Since mAbH recognizes an O-GlcNAc residue, our findings indicate that O-GlcNAc-glycosylated polypeptides are present at mitochondria where the components of the respiratory chain and energy transduction are localized. These findings may be of interest for gaining insight into the histophysiology of mitochondria-rich normal cells and into the pathogenesis of oncocytic lesions, since O-GlcNAc glycosylation may modify proteins involved in oncogenesis such as tumor suppressor proteins and oncoproteins, as well as proteins with important biological functions such as cytoskeletal proteins, transcription factors, heat-shock proteins, and chromatin proteins.
Department of Anatomy-Histology-Embryology, Medical Faculty, University of Thessaly, 22 Papakyriazi Street, Larissa 41222, Greece. arvanitis@med.uth.gr
Dimitrios L
DL
Arvanitis
Leonidas D
LD
Arvanitis
Ioannis G
IG
Panourias
Panagiotis
P
Kitsoulis
Panagiotis
P
Kanavaros
D000117:Acetylglucosamine / Q000276:immunology / Q000378:metabolism*; D000911:Antibodies, Monoclonal; D000951:Antigens, Neoplasm / Q000276:immunology / Q000378:metabolism; D014408:Biomarkers, Tumor / Q000276:immunology / Q000378:metabolism; D000939:Epitopes / Q000276:immunology / Q000378:metabolism; D019084:Fluorescent Antibody Technique, Indirect; D006801:Humans; D007124:Immunoenzyme Techniques; D008679:Metaplasia / Q000276:immunology / Q000378:metabolism / Q000473:pathology; D008928:Mitochondria; D009369:Neoplasms / Q000276:immunology / Q000378:metabolism* / Q000473:pathology; D024862:Oxyphil Cells / Q000378:metabolism* / Q000473:pathology
D000911:Antibodies, Monoclonal; D000951:Antigens, Neoplasm; D014408:Biomarkers, Tumor; D000939:Epitopes; D000117:Acetylglucosamine