Tomihisa Ninomiya

Myoepitheliomas and Myoepithelial Adenomas of Salivary Gland Origin: Immunohistochemical Evaluation of Filament Proteins, S-100 α and β, Glial Fibrillary Acidic Proteins, Neuron-specific Enolase, and Lactoferrin

Immunohistochemical identification of keratin proteins (TK, KL1 and PKK1), vimentin, myosin, S-100 protein (using polyclonal antiserum) and S-100 alpha and beta subunits, glial fibrillary acidic protein (GFAP), neuron-specific enolase (NSE), lactoferrin, and lysozyme was made in myoepitheliomas, myoepithelial adenomas, and clear cell adenomas of salivary gland origin. Myoepithelioma cells were divided into two types: plasmacytoid cells, which showed great heterogeneity in terms of keratins and S-100 alpha and beta proteins and a lack of GFAP, NSE, lactoferrin, and lysozyme in most the cells, and fibrous and dendritic tumor cells, which displayed variable staining for keratin and S-100 alpha and beta proteins. Myoepithelial adenomas were composed of small-, intermediate-, and large-sized spindle cells that showed irregular positive reactions for keratins and S-100 alpha and beta. Immunohistochemical deposition of S-100 protein was restricted strongly to the dendritic cells present in hyalinous and myxomatous areas. Clear cell adenomas revealed uniformly slight staining of keratins and S-100 proteins, and negative staining or rarely positivity for GFAP, NSE, lactoferrin, and lysozyme. When the immunohistochemical deposition of these proteins was compared between normal glands and myoepithelial tumors, heterogeneity of expression of keratins, S-100 proteins, GFAP, and NSE was notable in the tumors. Progenitor cells of several kinds of myoepithelioma were suggested to be intercalated reserve cells, which are thought to be the same cell that gives rise to pleomorphic adenoma of salivary glands.

Immunohistochemical localization of the α and β subunits of S-100 protein in pleomorphic adenoma of the salivary glands

SummaryThe immunohistochemical expression of the α andβ subunits of S-100 protein in reactive, modified and transformed of myoepithelial cells, salivary pleomorphic was investigated using monoclonal antibodies. With S-100 α, normal salivary glands showed strong staining in serous acinar cells and moderate to slight staining in ductal segments, and with S-100β staining was slight or negative in acinar cells, but strong in nerve fibres. In pleomorphic salivary adenomas, the immunohistochemical distribution of S-100 α andβ proteins indicated great variation in the tumour cells. Some neoplastic cells gave similar staining for both S-100 α andβ, others were strongly positive for S-100 α and stained only slightly for S-100 /gb, or vice versa. Yet other cells were positive for S-100 α and negative for S-100β, or vice versa. Pleomorphic salivary adenomas were classified both by histopathological criteria and by their staining pattern for S-100 α andβ proteins. Great heterogeneity in S-100 α andβ protein expression was found in individual tumour cells of both ductal and myoepithelial origin, and no regular pattern was identified.The cellular origin of salivary pleomorphic adenomas is discussed in terms of S-100 α andβ protein immunohistochemistry. Pleomorphic adenoma cells may be transformed from reserve cells into tumour cells displaying biologic properties of myoepithelial cells, ductal cells, or a mixture of both.

Identification of vascular system in experimental carcinoma for cryosurgery—Histochemical observations of lectin UEA-1 and alkaline phosphatase activity in vascular endothelium

Histopathologic and histochemical changes in experimental carcinomas following cryotreatment were observed to detect alkaline phosphatase (ALP) activity and UEA-1 lectin binding. Experimental carcinomas were induced in the hamster cheek pouch by topical application of 0.5% DMBA acetone solution twice a week. The cryoprobe at -60 degrees C was directly attached to the tumor surface for 90 sec. Histochemically, the tumor tissue following cryotreatment was completely destroyed in the surface area by the direct freezing and such cryonecrotic tumor tissue lacks stainability. Soon after cryotreatment and before cryonecrosis takes place, it has been observed that there is an intense dilatation of capillary vessels. Histochemically, high ALP activity was limited to capillary endothelium and to inflammatory cells. Lectin UEA-1 staining was usually found in both normal and neoplastic epithelial cells which were confined to capillary vessels. At 1 to 3 hr after cryotreatment, lectin UEA-1 binding was also positive in dilated endothelial cells of the frozen tissue as well as viable remaining neoplastic epithelia by freezing. ALP activity and UEA-1 binding disappeared in capillaries of cryonecrotic area in tumor tissues. Those findings suggest that biologic membrane changes in capillary endothelium of tumor stroma occur following cryotreatment.

Branchial cleft cysts. Histologic and immunohistochemical aspects.

8 cases of branchial cleft cysts and 1 case of branchiogenic carcinoma were examined immunohistochemically for detectable keratin, immunoglobulins (IgG, IgA, IgM), carcinoembryonic antigen (CEA), factor VIII related antigen (Factor VIII RGA), and lysozyme. Lectin binding patterns were also determined. Histologically, cystic lining epithelia were classified into stratified squamous epithelium without keratinization, columnar epithelium with or without cilia, or a mixture of both. Almost all of the cases indicated accompanying lymphoid structures with germinal centers. Keratin expression in epithelial cells was slightly positive, and lectin binding affinities in them were similar to those of oral squamous epithelium. CEA was found on the surface border of columnar epithelial cells, but cystic epithelia in most of the cases were devoid of lysozyme. Endothelial cells of capillary vessels showed positive binding by UEA-1 lectin and the presence of factor VIII RAG. In the lymphoid structures, there were scattered strongly positive lysozyme-staining cells as well as a few lymphocytes bearing IgG, IgA, or IgM.

Histologic and histochemical changes in experimental carcinomas following cryosurgery

Histologic and histochemical changes in experimental SCCs following cryosurgery were reported. Effects of cryosurgery on SCCs of hamster cheek pouch were classified into 3 zones; the superficial zone was the cryodestructive layer on which the cryoprobe had been attached directly to the SCC; the zone beneath this layer was the indirect cryodestructive layer; the 3rd zone was unaffected tissue in which the critical low temperature was never reached. In the superficial cryodestructive layer, tumor cells were destroyed completely and bleeding was found in the stroma. In the zone beneath it, neoplastic cells also showed morphologic and enzymatic changes indicating incomplete cellular destruction; dilatation of capillary vessels was also found. LDH isozyme pattern displayed a high level of LDH 5 in the non-treated SCC, and following cryosurgery, the high level of LDH 5 decreased and revealed an approximately normal LDH 5 pattern.

Effects of cryosurgery in experimental carcinoma on lectin binding and keratin distribution

Histochemical alterations of lectin binding and keratin distribution in experimental carcinomas of the hamster cheek pouch were obtained following cryotreatment. Cryotreated carcinoma cells showed a characteristic reduction in lectin binding and keratin staining shortly following cryosurgery. Tumor tissue, on the 2nd and 3rd days after cryotreatment, displayed destruction and necrosis with almost a complete loss of lectin binding and keratin staining. The remaining neoplastic cells located in the deeper layer showed positive reaction for both lectin binding and keratin, which is indicative of tumor recurrence. Histochemical staining of lectin binding and keratin proteins were useful markers in cryotreated tumor cells to identify either destruction and necrosis or vital activity of neoplastic growth.

Immunoreactive prolactin in lesions and tumours of salivary glands

The prolactin binding in obstructive lesions and tumours of salivary glands was described by use of the immunohistochemical PAP technique. Normal salivary glands had prolactin binding cells in the striated ducts only. Chronic obstructive lesions of submandibular glands showed negative immunoreaction for prolactin binding in ductal cells, but positive staining of the luminal surface of ductal segments. In pleomorphic adenomas, occasional neoplastic cells located along the luminal borders of tubular, ductal, or of duct-like epithelial structures were strongly reactive with anti-prolactin and 26.5% of cases pleomorphic adenoma were positive for anti-prolactin. Adenoid cystic carcinoma exhibited positive prolactin binding on the luminal surface of some of tumour foci, but not in the rest of the tumour. Warthins tumour was devoid of detectable prolactin binding.