alpha-chymotrypsin and Adenoma--Pleomorphic

Presence of lysozyme, lactoferrin, alpha 1-antitrypsin, alpha 1-antichymotrypsin and ferritin was examined by the immunoperoxidase method in 15 consecutive parotid gland tumors as well as in normal parotid gland tissue. Lysozyme and lactoferrin were detected in intercalated duct cells of normal tissue and in the epithelial component of pleomorphic adenomas. alpha 1-antitrypsin, alpha 1-antichymotrypsin and ferritin were found in both epithelial and mesenchymal components of pleomorphic adenomas but not in normal parotid tissue. In the epithelial component of adenolymphoma only alpha 1-antichymotrypsin and lactoferrin were observed. The results would support a tentative histogenetic link between the intercalated duct cell and the epithelial component of the pleomorphic adenoma.

Topics: Adenocarcinoma; Adenolymphoma; Adenoma, Pleomorphic; alpha 1-Antichymotrypsin; alpha 1-Antitrypsin; Chymotrypsin; Ferritins; Histocytochemistry; Humans; Immunoenzyme Techniques; Lactoferrin; Lactoglobulins; Muramidase; Parotid Neoplasms

Immunohistochemical identification of alpha 1-antitrypsin (alpha 1-AT) and alpha 1-antichymotrypsin (alpha 1-ACh) in pleomorphic adenomas of salivary glands is reported in order to compare their distribution profiles with those of lysozyme and lactoferrin, already described elsewhere. Normal salivary glands indicated positive alpha 1-AT staining in ductal segments and had no alpha 1-ACh in any glandular cell. Pleomorphic adenomas displayed moderate positivity to alpha 1-AT staining in duct-like, tubular and glandular epithelia which was particularly intense in luminal cells. The limited number of tumour cells which showed duct-like structures with a single cellular layer arrangement, displayed the highest staining to alpha 1-ACh. Strongly alpha 1-AT positive tumour cells located on the inner side of luminal cavities were also markedly positive to alpha 1-ACh. Spindle shaped tumour cells existed outside tubular and ductal structures and were negative to alpha 1-AT and alpha 1-ACh. Distribution of alpha 1-AT in salivary glands was similar to that of lysozyme as is usual in ductal segments or their transformed cells, and occurrence of alpha 1-ACh localization rather resembled that of lactoferrin, with occurrence in acinar compartments and changed epithelia within acini. The biological role of a specific immunohistochemical distribution of alpha 1-AT and alpha 1-ACh in pleomorphic adenomas may be associated with a self regulating mechanism which inhibits degradation by tissue proteinases.

Topics: Adenoma, Pleomorphic; alpha 1-Antichymotrypsin; alpha 1-Antitrypsin; Chymotrypsin; Histocytochemistry; Humans; Immunochemistry; Lymphadenitis; Salivary Gland Neoplasms; Salivary Glands; Submandibular Gland