Shin Fukui

Heterogeneity of keratin distribution in the oral mucosa and skin of mammals as determined using monoclonal antibodies

SummaryThe immunohistochemical localization of keratins in the oral epithelia of several mammals was investigated using the monoclonal antibodies to keratins, PKK1 (41–56 kilodaltons) and KL1 (55–57 kilodaltons). The staining patterns obtained in different locations of the oral mucosa and of the skin epidermis were compared. In the papillae on the dorsal surface of the tongue, some areas exhibited marked PKK1 staining, while other area were PKK1 negative. In general, rodent oral epithelia were negative for PKK1 in the basal layer, while comparatively strong PKK1 staining was observed in cells of the upper spinous layer. In the epidermis, positive PKK1 reactions were confined to the basal layer, while KL1 staining was occasionally seen in the basal layer of oral epithelia. In cats, dogs, and monkeys, different PKK1 and KL1 binding patterns were observed in oral epithelia. Also, the distribution in oral epithelia differed from that seen in the epidermis of these animals. In the epidermis, the distribution of PKK1 and KL1 was regular, with PKK1 usually being confined to the basal layer, while KL1 binding was found in the spinous and granular cell layers, and was dependent on the degree of keratinization. In the animals studies, keratin expression as detected by PKK1 and KL1-was different in the skin epidermis and oral epithelia, and the localization of these keratins differed in the various types of oral mucosa.

Expression of keratins during experimentally induced carcinogenesis in hamster cheek pouch visualized polyclonal and monoclonal antibodies

SummaryWe obtained immnohistochemical profiles of several keratin proteins during experimentally induced carcinogenesis in hamster cheek-pouch mucosa using a polyclonal antibody (TK; detecting keratins with molecular masses of 41 65 kilodalton) and two monoclonal antibodies (KL1, 55- to 57-kilodalton keratins; PKK1; 40-, 45- and 52.5-kilodalton keratins). The squamous epithelium of normal pouch mucosa exhibited positive TK staining in all layers. KL1 staining in the spinous layer and PKK1 staining in the basal layer, thus indicating a regional or zonal distribution pattern. Epithelia undergoing basal hyperplasia showed irregular localization of PKK1 binding, while hyperkeratinized lesions exhibited the binding pattern found in normal epithelium. In case of epithelial dysplasia, there was reduced KL1 staining in spinous cells and decreased PKK1 staining in the basal and parabasal layers. Papillomas exhibited a rather zonal distribution of keratin staining. All squamous-cell carcinomas, irrespective of their degree of keratinization and infiltration pattern, showed slight or no PKK1 staining. Such lesions were only positive for KL1-detectable keratins in keratinizing tumour cells and exhibited an irregular distribution of TK binding. The expression of keratin proteins during carcinogenesis in hamster cheekpouch mucosa may parallel that of keratins in human squamous-cell carcinomas originating in the oral mucosa.

Differential distribution of immunohistochemically detected keratin proteins in mammalian oral epithelia.

Keratin proteins were immunohistochemically demonstrated in different parts of the oral epithelium. Keratin staining in the squamous-cell epithelium was restricted to the spinous and granular cell layers, with a comparatively low reaction in the basal layer cells and none in the superficial cornified layer. In comparing the keratin staining levels, those in the buccal and sublingual epithelia were rather higher than those in the hard palatal epithelia. Staining intensities for keratin proteins were not the same in either different locations of the oral epithelium or in the same location in different animals.

Immunohistochemical expression of keratin proteins in urinary bladder carcinoma.

Transitional carcinomas of the urinary bladder were examined immunohistochemically for keratin proteins with the use of polyclonal antiserum (TK, 41-65 kDa) and 3 monoclonal antibodies (KL 1, 55-57 kDa; PKK 1, nos. 19, 18, 8; and K 8.12, nos. 16, 13). Umbrella cells gave particularly strong staining for TK, KL 1 and PKK 1, whereas they were negative for K 8.12. Basal- and intermediate-layer cells in urothelial epithelium were moderately positive for all keratins. Brunns nests cells showed comparatively slight or moderate keratin staining, and K 8.12 staining of Brunns nests was higher than in urothelial epithelial cells. Transitional carcinoma (grades I and II) indicated uniform keratin distribution, and staining was strong with TK, while that of KL 1, PKK 1 and K 8.12 varied, and grade III tumors showed the lowest intensity of staining. K 8.12 staining in papillary transitional carcinomas was strongly positive in basal located tumor cells, as compared with apical tumor cells. Squamous cell carcinoma was varying positive to keratin reactions dependent on the degree of keratinization. Heterogenity of keratin distribution in papillary transitional carcinomas was given between basal tumor cells and well differentiated tumor cells including umbrella-like cells.

False positive reaction for carcinoembryonic antigen in Paget cells: immunohistochemical observation

SummaryPaget cells from cases of mammary and extramammary Paget’s disease were examined for carcinoembryonic antigen (CEA) and CEA-related antigens by the immunoperoxidase method. Paget cells showed a conspicuous positive reaction with antiserum to CEA, but were negative when nonspecific cross-reacting-antigen (NCA)-absorbed antiserum to CEA, or a monoclonal antibody to CEA was used as the detecting agents. Paget cells may contain large amounts of NCA antigen or CEA-related substances.