Immunohistochemical evaluation of transglutaminase c in tumours of salivary glands

Transglutaminase C (TGase C), a family of Ca²⁺-dependent enzymes and an essential component in the cross-linking of peptide bonds, has been found to be a marker of epithelial differentiation with a possible role in cellular apoptosis, extracellular matrix stabilisation and Ca²⁺ binding, thereby having a potential role in tumour growth, differentiation and invasive behaviour. The expression of TGase C was evaluated in normal human salivary glands and their neoplastic lesions which included pleomorphic adenoma (n = 30), Warthin's tumour (n = 5), adenoid cystic carcinoma (n = 10), acinic cell carcinoma (n = 5), mucoepidermoid carcinoma (n = 5) and control tissue specimens of normal oral mucosa and squamous cell carcinoma, using polyclonal antibody, the specificity of which was determined by Western blotting, generated by immunising rabbits with purified transglutaminase. The TGase C was observed in the epithelial cells in the control tissue specimens examined. Pleiomorphic adenoma revealed reaction products in luminal tumour cells, the non-luminal or modified myoepithelial cells and their plasmacytoid variants, squamous metaplastic cells and chondroid cells. Adenoid cystic carcinomas had tumour cells in the luminal cells of tubular and cribriform structures and the acinic cell carcinoma had from low to moderate immunoreactivity in the tumour cell component and a diffuse immunoreactivity in the stroma for TGase C. Mucoepidermoid carcinoma showed no reaction products in the mucous-producing cells, while intermediate and epidermoid cells had immunoreactivity in the cell cytoplasm. As the presence of TGase C in salivary gland tumours was confined to those tumour cells which form the predominant histomorphology in each tumour subtype, it may be suggested that these enzymes may have a potential role in the regulation of cellular function in neoplastic salivary tissues affecting tumour growth, differentiation and neoplastic behaviour.