Yohko Noda

Distribution of keratin proteins in neoplastic and tumorlike lesions of squamous epithelium

Seventy-six cases of tumorlike and neoplastic lesions from epidermis and oral epithelium were analyzed by a histochemical technique for the demonstration of keratin. Formalin-fixed paraffin sections were reacted with rabbit antihuman keratin antiserum (dilution of 1:40). The types of distribution of keratin in cells of lesions were classified into five categories: (1) regional, as found in normal squamous epithelia and benign hyperkeratinized lesions, and papilloma, and keratinized squamous cell carcinoma; (2) total, as seen in intensely keratinized lesions, such as verruca vulgaris and highly keratinized squamous cell carcinoma; (3) negative, as displayed by basal cell carcinoma; (4) scattered, as in the most poorly differentiated squamous cell carcinomas; and (5) mixed cellular, as found in both poorly and moderately differentiated squamous cell carcinomas.

Immunohistochemical Identification of Epithelial Membrane Antigen in Sweat Gland Tumours by the Use of a Monoclonal Antibody

A total of 78 cases of adnexal tumors of the skin were examined with the use of monoclonal antibody against epithelial membrane antigen (EMA). The EMA reaction was confined to luminal surfaces and lateral borders of sweat glands, both eccrine and apocrine, being usually absent in ductal segments. Neoplastic lesions of all the adenomatous tumours and mixed tumours of sweat glands showed specifically positive EMA staining of luminal surfaces and lateral borders of tubular, duct-like, and cystic structures. However, solid foci of those tumours were negative for EMA. Tumours of ductal origin, e.g. syringomas and poromas, exhibited positive EMA staining in their plasma membrane, although normal intact keratinocytes did not stain for EMA. Immunohistochemical distribution of EMA in skin adnexal tumours was classified into two types: one in which the luminal surfaces and lateral outer borders were positive, similar to that of the normal secretory coil, and the other in which the plasma membrane of neoplastic cells of ductal origin was positive.

Immunohistochemical localization by monoclonal antibodies of S-100 α and β proteins in mixed tumours and adenomas of the skin

SummaryA study using monoclonal antibodies was made to evaluate the immunohistochemical localization of S-100 protein subunits a and β in a total of 41 mixed tumours and adenomas of sweat gland origin. Normal eccrine glands showed positive staining for S-100 α in the secretory portion and in epithelial cells located in the transitional area from the coiled duct to the intraepidermal duct, as well as granular deposition of S-100 β at the luminal surface of the secretory coil and duct. The myoepithelial cells were negative for S-100 α and β. In mixed tumours, the tumour cells were round or oval in shape and displayed markedly positive staining for S-100α and slightly positive or negative staining for S-100β. S-100 α staining in clear cell tumours was typically more intense than in any other sweat gland tumour. It is possible that clear cell tumours may arise from the transitional area of sweat glands. Spindle cell tumours displayed on abundance of S-100 α subunits but little S-100β. Occasional spindle cells located in the outer layer of tubular structures within tumours gave positive S-100α staining. This result was different from that seen in pleomorphic salivary adenomas. Cells having undergone chondroidal changes revealed a positive S-100 reaction.

Immunohistochemical study of carbonic anhydrase in mixed tumours from major salivary glands and skin

Immunohistochemical distribution of carbonic anhydrase isoenzyme I and II was studied in mixed tumours of major salivary glands and skin. The normal salivary glands displayed strong carbonic anhydrase activity in both ductal epithelium and serous acinar cells and the serous demilune cells in the submandibular glands, including the eccrine ducts. Pleomorphic adenoma salivary gland origin exhibited positive staining in the innerlayer of epithelial cells of tubular, duct-like and glandular structures. No enzymatic staining was noted in the outer layer of tumour cells in these structures. Spindle tumour cells or the fibroblast-like cells with long cytoplasmic processes identified in the adjacent hyalin and myxomatous stroma were rarely positive, while chondroidal and osteo-chondroidal cells were highly reactive. Mixed tumours of eccrine gland origin showed the most reactive staining cells scattered throughout neoplastic epithelium in all tissues examined. Immunohistochemical stainability was usually higher for carbonic anhydrase II than I for both normal and tumour tissues. The biological roles of the distribution profiles of carbonic anhydrase are discussed.

Lectin binding patterns in salivary glands treated with amylase.

Lectin binding patterns of ConA (Glc, Man), PNA and SBA (Gal, GalNAc), RCA-I (Gal) DBA (GalNAc), WGA (GlcNAc), and UEA-I (Fuc) in the major salivary glands of mice, rats, hamsters, and guinea pigs were reported using paraffin sections subjected to alpha-amylase treatment at 1, 3, and 6 h digestions. Lectin staining following treatment with amylase was generally enhanced in acinar, duct, and GCT cells. However, increasingly different reactions were obtained depending upon the lectins used, the various salivary glands from different specimens treated, and the different properties of the serous, mucous, and sero-mucous cells in the histologic sections. The lectins that demonstrated rather markedly increased staining were ConA, PNA, SBA, WGA, and UEA-I, whereas RCA-I and DBA increased little in comparison, or actually decreased. It appears from these findings that complex carbohydrates within murine salivary glands contained large amount of glucose, mannose, galactose, and N-acetyl galactosamine residues. The basement membranes of glandular cells in salivary glands demonstrated markedly positive ConA staining following alpha-amylase digestion.

Immunohistochemical localization of carbonic anhydrase I and II in submandibular salivary glands of the mouse, rat, hamster and guinea pig

Tissues were fixed in Bouin and Carnoy solutions, and the peroxidase, anti-peroxidase (PAP) method was used. Serous acinar cells of the guinea pig were positive for carbonic anhydrase (CA), but acinar cells of rodents were negative. Granular convoluted tubule (GCT) cells of the mouse, rat and hamster had varying degrees of staining for CA isoenzyme I and II. Striated and excretory ducts from all four species were usually positive for CA. Scattered cells containing a high concentration of CA I and CA II were present in striated ducts and GCT of the hamster, GCT of the rat and striated and excretory ducts of the guinea pig.

Different bindings to lectin in human submandibular gland after enzymatic digestion

Lectin binding affinities were described in human submandibular gland (SMG) in the paraffin sections following alpha-amylase, sialidase, and trypsin digestions. Lectins in the present study were used Con A (Glc, Man binding lectins), PNA, and SBA(Gal, GalNAc), RCA-1(Gal), DBA(GalNAc), WGA(GlcNAc), and UEA-1(Fuc). Lectin stainings in serous and mucous acinar cells and ductal epithelia were reported to compare enzyme treated and nontreated sections. Amylase treatment showed increasing Con A staining in connective tissue fibers and no marked changes in SMG to lectin bindings. Sialidase digestion was characteristically intense in PNA and SBA bindings in SMG cells, and also enhanced staining to UEA-1 in serous and duct cells and to WGA in mucous and duct cells were noted. Trypsin digestion indicated a slight increase to Con A binding, and was relatively strong to UEA-1 in serous and duct cells and a little strong to WGA. The results suggested that SMG serous cells contain higher amounts of Gal, GalNAc, and Fuc residues; and mucous cells were also abundant in Gal, GalNAc, and GlcNAc residues.

Distribution difference of lectin binding in salivary gland treated with sialidase and trypsin

Histochemical evaluation of complex carbohydrates in the salivary glands from rodents following sialidase and trypsin treatment were reported by the use of lectins binding technique which specifically link to corresponding sugar residues in macromolecules. Lectin staining in salivary gland generally increased following 1 h sialidase treatment, particularly in guinea-pig specimens. Lectin staining followed by treatment of trypsin (30 min) showed in increase in staining which is characteristic of UEA-I lectin. In long duration treated sections, by either sialidase or trypsin, lectin staining usually decreased in salivary glands. In the present study, complex carbohydrates of salivary glands may be hydrolyzed and degraded by sialidase and trypsin treatments, and lectin binding affinity is then also enhanced due to exposed sugar residues in complex carbohydrates.

Immunohistochemical study of carbonic anhydrase in mixed tumours and adenomas of sweat and sebaceous glands

Immunohistochemical distribution of carbonic anhydrase II (CA) in mixed tumours and adenomas of sweat gland origin and in sebaceous adenomas was demonstrated by the PAP method. Normal sweat glands, both eccrine and apocrine, clear cells of the secretory coils, and ductal epithelial cells all showed conspicuous staining for CA, and sebaceous glands were also positive. Mixed tumours of the skin indicated strongly positive staining for CA in the luminal cells of tubular and duct‐like or cystic structures, while most of the other tumour cells were negative. In solid or massive foci, CA positive cells were found scattered among the cellular mass. Sebaceous adenomas were usually moderately positive for CA throughout the tumour.