lactoferrin and Salivary-Gland-Neoplasms

Topics: Actins; Adult; alpha 1-Antitrypsin; Female; Humans; Immunohistochemistry; Lactoferrin; Muramidase; Phosphopyruvate Hydratase; Pregnancy; S100 Proteins; Salivary Gland Neoplasms; Salivary Glands; Submandibular Gland

10 pleomorphic adenomas of the human parotid gland were transplanted on several groups of nude mice. For comparative reasons, 10 other pleomorphic adenomas, a neurinoma and a chordoma and transplants of squamous cell carcinomas and of normal salivary gland tissue were also analysed. In the primary tumours and in the transplants, the presence of keratin, carcinoembryonic antigen, tissue polypeptide antigen, lactoferrin, lysozyme, immunoglobulins, secretory component, amylase, fibronectin and of several lectin-receptors (PNA, WGA, HPA, Ulex europaeus) was sought. The immunohistological observations show that many of the features of a pleomorphic adenoma are constant under the conditions of transplantation. In the transplanted tumour, the same heterogeneity as in the primary tumours can be observed. Autoradiographic studies show little labelling with 3-H thymidine, which is in good accordance with the biological behaviour of the tumour. The distribution of fibronectin shows an interesting association with myoepithelial-like cells. Our results support the hypothesis that the histogenetic origin of the pleomorphic adenoma is a cell pool of the terminal ductal segment. A differentiation towards ductal cells (with production of secretory substances) and towards myoepithelial cells (associated with large amounts of basal membrane like substances) is observed.

Topics: Adenoma, Pleomorphic; Animals; Autoradiography; Carcinoembryonic Antigen; Carcinoma, Squamous Cell; Cell Division; Fibronectins; Histocytochemistry; Humans; Immunochemistry; Immunoglobulin A; Immunoglobulin A, Secretory; Immunoglobulin G; Immunoglobulin M; Keratins; Lactoferrin; Lectins; Mice; Mice, Nude; Muramidase; Neoplasm Transplantation; Salivary Gland Neoplasms; Tetradecanoylphorbol Acetate; Transplantation, Heterologous

It has been hypothesised that secretory carcinoma of the salivary gland (SCsg) might have a lactational-like differentiation. Therefore, we aimed to assess the immunoexpression of breast hormonal receptors and milk-related proteins in cases of SCsg and other salivary gland tumours with prominent secretory activity.. Immunohistochemistry against prolactin and growth hormone receptors, lactoferrin, human milk fat globule 1, MUC 1 and MUC4 was performed in twelve cases of SCsg and 47 other salivary gland tumours.. Most cases of SCsg were negative for prolactin and growth hormone receptors. All cases of SCsg showed enhanced membranous-cytoplasmic staining for human milk fat globule 1, a pattern seen in other tumour groups. Only SCsg showed widespread strong staining for lactoferrin, concomitantly in the cell compartment and secretion. The other positive tumour types exhibited restricted staining. MUC1 and MUC4 showed no distinct pattern of expression.. Although SCsg failed to demonstrate a complete lactational-like differentiation, lactoferrin showed a distinctive expression pattern in SCsg compared to other tumour types, which makes it a good marker to help in its differential diagnosis.

Topics: Biomarkers, Tumor; Carcinoma; Cell Differentiation; Humans; Lactoferrin; Prolactin; Receptors, Somatotropin; Salivary Gland Neoplasms; Salivary Glands

To study the histological and immunohistochemical characteristics of oncocytic carcinoma of salivary gland.. 7 cases of oncocytic carcinoma of salivary gland were investigated by HE, PAS, PTAH staining and immunohistochemistry.. Among the cases, 4 were male and 3 were female. The average age was 49 years old. 3 cases occurred in the parotid, 1 cases in submandibular, 1 cases in sublingual and 2 cases in minor salivary gland of palate. Investigated histologically, the tumour cells are characterized by oncocyte. The evidence of cellular atypia, obviously increased mitoses and infiltrative growth pattern are indicative of malignancy. Immunohistochemically, alpha 1-ACT, alpha 1-AT, LF, TF and CEA were all strongly positive in the normal salivary cells and adenolymphoma, while in oncocytic carcinoma, alpha 1-ACT and alpha 1-AT were moderate positive and LF, TF and CEA were light positive.. 7 cases were characterized by oncocyte and showing infiltrative growth, alpha 1-ACT, alpha 1-AT, LF, TF, CEA were positive in oncocyte.

Topics: Adenocarcinoma; Adult; alpha 1-Antichymotrypsin; alpha 1-Antitrypsin; Carcinoembryonic Antigen; Female; Humans; Lactoferrin; Male; Middle Aged; Salivary Gland Neoplasms; Transferrin

A case of intraductal papilloma occurring in the anterior lingual salivary gland (Blandin-Nuhn's gland) of a 58-year-old woman is presented. This location has not been reported previously. The results of histologic and immunohistochemical studies point to an epithelial origin of excretory salivary gland ducts and also demonstrate the secretory potential of the tumor cells.

Topics: Antigens, Neoplasm; Female; Humans; Immunohistochemistry; Keratins; Lactoferrin; Membrane Glycoproteins; Middle Aged; Mucin-1; Papilloma; S100 Proteins; Salivary Gland Neoplasms; Salivary Glands, Minor; Tongue Neoplasms

Eight cases of acinic cell carcinoma of the salivary glands were histologically reclassified and their immunohistochemical expression and distribution for various tissue antigens were examined. The epithelial elements were divided into tubuloglandular components, microcystic patterns and solid nests. The authors' results indicated the following: 1) The duct luminal cells of tubuloglandular components have distinct epithelial features with cytokeratin (KL 1), alpha 1-antichymotrypsin (alpha 1-ACT), transferrin, lactoferrin, IgA, and carcinoembryonic antigen (CEA) positivity. 2) The cyst-lining cells of microcystic pattern expressed immunophenotypes similar to those of the duct luminal cells. 3) The acinic cells in solid nests had positive results for KL 1, alpha 1-antitrypsin (alpha 1-AT), transferrin, lactoferrin and vasoactive intestinal polypeptide (VIP). 4) The clear cells in solid areas had positive results for KL 1, alpha 1-AT, transferrin and VIP. Both the clear cells and the neoplastic acinic cells showed a rather similar pattern of immunoreactivity. Therefore, the clear cells may transform from the neoplastic acinic cells. 5) Secretory products in tubuloglandular and microcystic patterns had positive results for alpha 1-ACT, lactoferrin, IgA and CEA. 6) The basement membrane-like material between the neoplastic islands has distinct positivity for alpha 1-AT. The result suggests that alpha 1-AT is a useful marker of basement membrane-like material.

Topics: Adult; Aged; alpha 1-Antichymotrypsin; alpha 1-Antitrypsin; Biomarkers, Tumor; Carcinoma; Cytoplasm; Female; Ferritins; Humans; Immunoenzyme Techniques; Intermediate Filaments; Lactoferrin; Male; Middle Aged; Proteins; Reference Values; Salivary Gland Neoplasms; Transferrin

An immunoperoxidase staining technique was used for detecting three major iron-binding proteins (transferrin, ferritin and lactoferrin) in 54 adenoid cystic carcinomas (ACCs) of major and minor salivary glands. Twenty-three normal salivary glands were investigated for comparison. Transferrin staining was detected mainly in the intercalated duct and serous acinar cells, and was found inconsistently in the myoepithelial cells surrounding normal ductules. Ferritin was always absent in the normal epithelial component of salivary gland. The presence of lactoferrin was demonstrated in the serous acinar cells and intercalated duct cells of normal salivary tissues. Five histological patterns were found in ACC, and for the cellular components of each, it was possible to establish a special immunohistochemical profile. Transferrin positivity was detected in the small angular cells of 25 cases (48%), in the duct luminal cells of 19 cases (37%) and in the hyalinized stroma of 4 cases (8%). Ferritin staining was positive in the small angular cells of 23 cases (44%) and in the duct luminal cells of 15 cases (29%). Lactoferrin was detected in only duct luminal cells of 38 ACCs (73%). The comparative immunohistochemical analysis between transferrin and ferritin showed a similar distribution in this carcinoma. On the basis of the immunohistochemical data, lactoferrin might be used as a marker of glandular differentiation.

Topics: Biomarkers, Tumor; Carcinoma, Adenoid Cystic; Ferritins; Humans; Immunoenzyme Techniques; Lactoferrin; Neoplasm Proteins; Salivary Gland Neoplasms; Transferrin

The immunohistochemical expression of lysozyme (Ly), lactoferrin (La), alpha 1-antitrypsin (alpha 1-AT), and alpha 1-antichymotrypsin (alpha 1-Ach) was described, and their distributions were compared to each other in 28 cases of adenoid cystic carcinoma (ACC) of the salivary glands. ACC materials were obtained from the parotid gland (7), the submandibular gland (4), the sublingual gland (8), and minor oral salivary glands (9). Histopathologically, ACC was classified into cribriform (14), tubular (3), and basaloid or solid patterns (11). Positive staining for Ly was found in 1 case of solid ACC in the sublingual gland; La was found in 4 cases (2 cribriform, 1 tubular, 1 basaloid) in the sublinguals (3) and parotid glands (1); alpha 1-AT was found in 6 cases and alpha 1-Ach in 17 cases. The immunohistochemical localization of Ly and La was usually confined to luminal tumor cells of tubulo-ductal structures, irrespective of the pathologic types. Positive staining for alpha 1-AT and alpha 1-Ach appeared in tumor cells of cribriform, tubular and solid ACC. Tumor cells with positive La staining coincided with a positive reaction to alpha 1-AT and alpha 1-Ach, and tumor cells with alpha 1-AT positive deposition were also positive for alpha 1-Ach. The contents of pseudocysts in the cribriform pattern showed a positive reaction to La, alpha 1-AT, and alpha 1-Ach. Of the 28 cases of ACC, positive expressions for Ly, La, alpha 1-AT and alpha 1-Ach were found with a high frequency of alpha 1-Ach staining (17 in 28 cases were positive). In sublingual ACC (8), 7 cases were positive for immunohistochemical reactions. Co-expression or simultaneous expression for Ly, La, alpha 1-AT, and alpha 1-Ach in ACC suggest that tumor cells are protected from proteolysis or degradation.

Topics: alpha 1-Antichymotrypsin; alpha 1-Antitrypsin; Carcinoma, Adenoid Cystic; Humans; Immunohistochemistry; Lactoferrin; Muramidase; Salivary Gland Neoplasms

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.

Topics: Adenoma; Cytoskeletal Proteins; Glial Fibrillary Acidic Protein; Humans; Immunohistochemistry; Lactoferrin; Lactoglobulins; Lysosomes; Myoepithelioma; Myosins; Phosphopyruvate Hydratase; S100 Proteins; Salivary Gland Neoplasms; Vimentin

A total of 27 cases of salivary gland adenocarcinomas were studied from clinicopathological view point. Adenocarcinomas of the salivary gland were microscopically subclassified into 3 groups according to Luna's classification: Salivary duct carcinomas histologically resembled the ductal carcinoma of the breast, displayed nuclear atypia and had poorer prognosis than the other subclasses of salivary gland adenocarcinomas. Terminal duct carcinomas lacked in nuclear atypia and displayed a variety of growth patterns, including papillary, cribriform, tubular, and solid. Some terminal duct carcinomas showed prominent mucin-production. Epithelial-myoepithelial carcinomas had clear cytoplasms and exuberant glycogen. In addition to the clinicopathological study, nuclear areas of the tumor cells were measured in each of the 27 salivary gland adenocarcinomas, and mean nuclear area (MMA) and standard deviation (SD) were calculated. The group with more than 50 microns 2 of MNA had poorer prognosis than the group with 50 microns 2 or less of MNA, and the group with more than 13 microns 2 of SD had poorer prognosis than the group with 13 microns 2 or less of SD. Finally, immunohistochemical study was performed against various markers including keratin, epithelial membrane antigen, lactoferrin, S-100 protein, CEA, etc., using the Avidin-biotin-peroxidase complex method. Lactoferrin was present in most of the salivary duct carcinomas, on the other hand, S-100 protein was detected in all of the five cases of the terminal duct carcinoma investigated. But immunohistochemical study is not especially useful in distinguishing subclasses of salivary gland adenocarcinomas or investigating the origin of tumor cells.

Topics: Adenocarcinoma; Adolescent; Adult; Aged; Aged, 80 and over; Carcinoma, Intraductal, Noninfiltrating; Cell Nucleus; Female; Humans; Immunoenzyme Techniques; Lactoferrin; Male; Middle Aged; Prognosis; S100 Proteins; Salivary Gland Neoplasms

Immunohistochemical identification of lysozyme and lactoferrin was made in salivary pleomorphic adenomas (147 cases) and the staining patterns were evaluated with respect to the histological features and histogenesis. In normal salivary glands, the intercalated duct cells gave positive staining for lysozyme in major glands, and serous acinar cells, demilune cells, and interlobular duct cells were positive in minor glands. Lactoferrin staining was irregularly positive in serous cells and ductal epithelium. In pleomorphic adenomas, the reaction for lysozyme was positive in 14% (21/147) of the cases, and was confined to luminal cells of tubulo-ductal structures. Lactoferrin in pleomorphic adenomas was distributed in luminal tumor cells (51%; 75/147), in outer tumor cells (3%; 4/147), and in both luminal and outer tumor cells (5%; 7/147) in tubulo-ductal structures; it was also detected in plasmacytoid myoepithelial cells (5%, 8/147). However, modified myoepithelial cells and other types of neoplastic myoepithelial participants were negative for lactoferrin staining. The occurrence of both lysozyme and lactoferrin in salivary pleomorphic adenomas suggests their participation in the local defense mechanism in the tumor.

Topics: Adenoma; Humans; Immunohistochemistry; Lactoferrin; Lactoglobulins; Muramidase; Salivary Gland Neoplasms

Immunohistochemical expression of 8 cases of mucoepidermoid carcinomas (G-I, 3 cases; G-II, 2 cases; and G-III, 3 cases) revealed marked heterogeneity of the proteins examined. Immunohistochemically detectable keratins (TK, KL1, and PKK1) were distributed in epidermoid cells, but were absent in mucous secreting cells. Strongly positive deposits of keratin proteins were detected in squamoid tumor cells in the G-I tumors. The tumor cells displayed positive staining for S-100 alpha, but did not stain with polyclonal S-100 antiserum or with monoclonal S-100 beta. The cells showing highest reactivity for S-100 protein were scattered in neoplastic foci and were probably Langerhans cells. Lactoferrin and lysozyme reactions were generally negative in tumor foci; but a positive reaction for lactoferrin was found in luminal tumor cells although rarely, and lysozyme staining was occasionally noted in histiocytes in the stroma. Amylase activity was usually absent in the tumor cells, with the exception of one case in which it was confined to the tumor cells. Mucoepidermoid carcinomas of various grades indicated marked heterogeneity in terms of various immunohistochemically detectable proteins.

Topics: Adolescent; Adult; Aged; Aged, 80 and over; Amylases; Carcinoma; Female; Histocytochemistry; Humans; Immunoenzyme Techniques; Keratins; Lactoferrin; Lactoglobulins; Male; Middle Aged; Muramidase; Periodic Acid-Schiff Reaction; S100 Proteins; Salivary Gland Neoplasms; Staining and Labeling

An immunoperoxidase staining technique was used for detecting alpha one-antichymotrypsin (alpha 1-ACT), alpha one-antitrypsin (alpha 1-AT), lactoferrin and transferrin in routine histological paraffin sections of 30 adenolymphomas, as well as in normal salivary gland tissue. Microscopically, the epithelial, component of adenolymphomas consisted of tall columnar luminal cells and irregularly shaped basal cells. alpha 1-ACT was detected in the luminal layer of epithelium in 27 (90%) of 30 adenolymphomas, while the basal layer was positive in 4 cases (13%). Lactoferrin could be observed in the columnar cells of 21 cases (70%) and was positive in the basal cells of 2 cases (7%). In normal salivary gland tissue, alpha 1-ACT and lactoferrin were observed in the intercalated duct and serous acinar cells. The staining pattern of alpha 1-AT in adenolymphoma was similar to those of alpha 1-ACT and lactoferrin, however, the number of positive cases for alpha 1-AT was fewer than in the alpha 1-ACT and lactoferrin. alpha 1-AT was not found in the normal salivary gland. On the contrary, the localization of transferrin in the epithelial component of adenolymphomas was exclusively different from those of alpha 1-ACT, alpha 1-AT and lactoferrin. Transferrin was found more often in the basal cells than in the tall columnar apical cells. The staining pattern of transferrin in the normal salivary gland was different from alpha 1-ACT and lactoferrin, and transferrin was positive in the cytoplasm of intercalated ducts, serous acinar and myoepithelial cells.(ABSTRACT TRUNCATED AT 250 WORDS)

Topics: Adenolymphoma; alpha 1-Antichymotrypsin; alpha 1-Antitrypsin; Epithelium; Head and Neck Neoplasms; Humans; Immunoenzyme Techniques; Lactoferrin; Lactoglobulins; Salivary Gland Neoplasms; Submandibular Gland Neoplasms; Transferrin

A clonal neoplastic epithelial duct cell (HSGc) of human salivary gland origin has a fine structure similar to the intercalated duct cell and the capacity to express secretory component and lactoferrin. HSGc cells tend to form an occasional glandular arrangement in vitro and in vivo, and transplantation of cells into nude mice resulted in production of adenocarcinoma. By repeated single cell cloning, different types of clones could be isolated from HSGc. Cuboidal clones resemble the parent cell, but fail to form the glandular arrangement or express lactoferrin, suggesting a less differentiated type. Elongated clones have a fine structure similar to myoepithelial cells and carry myoepithelial markers such as S100 protein, actin, and myosin which are not detected in the HSGc and its cuboidal clones. These myoepithelial-like clones are able to express secretory component, lactoferrin, and lysozyme and to produce glycosaminoglycans, suggesting that they are a functionally active form of the neoplastic cell but different from the normal myoepithelial cell. Judging from their growth properties in vitro and in vivo, the myoepithelial-like clones are less malignant than HSGc or its cuboidal clones. Of four elongated clones, two did not produce tumors in athymic mice, while all of the cuboidal clones were tumorigenic. These findings suggest a possible conversion of the neoplastic duct cell to myoepithelial-like variants with low malignancy.

Topics: Actins; Adenocarcinoma; Antigens; Carcinoma; Cell Cycle; Cell Line; Cell Separation; Clone Cells; Epithelium; Fluorescent Antibody Technique; Humans; Keratins; Lactoferrin; Microscopy, Electron; Muramidase; Myosins; S100 Proteins; Salivary Gland Neoplasms; Secretory Component

Antisera of several secretory products of the salivary gland were used to investigate the histogenesis of acinic cell tumors and mixed salivary gland tumors for comparison. Amylase, lactoferrin, secretory piece, and proline-rich protein (PRP) immunoreactivity was detected in the majority of acinic cell tumors; staining was focal, except for PRP, which was diffuse. Lysozyme immunoreactivity was rare. There was discordance for immunoreactivity with several antisera in identifiable tumor lobules of half of the neoplasms. An antikeratin serum outlined microcystic and follicular areas but rarely solid foci. These findings support the contention that acinic cell tumors derive from a tubular type stem cell. Lactoferrin and secretory piece immunoreactivity was not common in mixed tumors and was confined to scattered ductal cells and luminal contents. Rare small foci of amylase and PRP immunoreactivity were found in two mixed tumors only.

Topics: Adenoma, Pleomorphic; Adolescent; Adult; Aged; Amylases; Carcinoma; Female; Humans; Immunochemistry; Keratins; Lactoferrin; Male; Middle Aged; Muramidase; Peptides; Proline-Rich Protein Domains; Salivary Gland Neoplasms; Staining and Labeling

In oral dysplasias and squamous cell carcinomas, relationships exist between the presence of keratin filaments and cell differentiation. The keratinized areas of high differentiated carcinomas are carcinoembryonic antigen (CEA) positive. The labeling of the higher molecular keratins is similar to the distribution of lectin receptors so that lectins represent membrane-oriented markers of differentiation. In dysplasias a gradual loss of blood group substances A and B can be observed. Squamous cell carcinomas possess no substances A or B. H antigen as precursor of A and B is increased in preneoplasias and absent in carcinomas. In oral papillomas, leukoplakias, and carcinomas virogen koilocytotic cell changes, papilloma viruses and viral antibodies can be demonstrated. In salivary gland tumors a distinct pattern of distribution for keratin, vimentin, CEA, tissue polypeptide antigen (TPA), metalloproteins, and enzymes can be observed. The cellular stromal reaction (lymphocytes, Langerhans cells, and so forth) can be defined more exactly by monoclonal antibodies.

Topics: Antigens, Viral; Blood Group Antigens; Carcinoembryonic Antigen; Cell Differentiation; Histocytochemistry; Humans; Intermediate Filament Proteins; Keratins; Lactoferrin; Mouth Neoplasms; Peptides; Receptors, Mitogen; Salivary Gland Neoplasms; Tissue Polypeptide Antigen

The neoplastic epithelial duct cells human salivary gland (HSG) and myoepithelial cells human pleomorphic adenoma (HPA) established from human salivary gland were examined by the immunoperoxidase method for the presence of specific antigens such as carcinoembryonic antigen (CEA), S-100 protein, secretory component (SC), lactoferrin (LF), and myosin. Isolation of the cells and their morphologic features were reported previously. Consequently, the presence of CEA, SC, and LF in the HSG cells was demonstrated. The HPA cells were identified to express the specific antigens reactive to anti-S-100 protein, anti-myosin and anti-CEA sera in addition to the presence of oxytocin receptor. When the two cell lines were co-cultured in monolayer culture or within the sponge matrix, a large number of ductlike or tubular structures were formed in an optimal ratio of 1:2 in HSG and HPA cells, whereas the cultures of HSG cells only grew with occasional formation of ductlike structure. In addition, in HSG and HPA cells in an area with their contact in the mixed cultures, CEA staining was intensified as compared with the culture of HSG or HPA cells only and further S-100 protein was detected in HSG cells, whereas S-100 protein was not detected in the culture of HSG cells only. These findings strongly suggest that the intercalated duct and myoepithelial cells from human salivary gland propagate with their interaction together in the expression of specific antigens such as CEA and S-100 protein or in the morphogenesis of salivary gland epithelial cells.

Topics: Adenoma, Pleomorphic; Carcinoembryonic Antigen; Cell Communication; Cell Line; Epithelium; Humans; Lactoferrin; Myosins; S100 Proteins; Salivary Gland Neoplasms; Secretory Component

Amylase (Am), lactoferrin (Lf), lysozyme (Ly), secretory component (SC), epithelial IgA, and epithelial IgM were traced by paired immunofluorescence staining in ethanol-fixed specimens from 15 pleomorphic adenomas of the parotid gland. Epithelial elements positive for some of the markers were detected in a variable number of the specimens (Am, 0; Lf, 11, Ly, 2; CEA, 6; SC, 11; IgA, 9; and IgM, 6); their expression seemed to depend on a certain degree of glandular differentiation. Variable co-expression of secretory epithelial markers probably reflected different degrees of differentiation, indicating that clonal diversification may explain the histological complexity of pleomorphic adenomas. The most consistent expression (in almost 75% of the specimens) shown by Lf and SC might further reflect histogenetic relationship to intercalated ducts in which these antigens are normally found in largest amounts.

Topics: Adenoma, Pleomorphic; Adult; Aged; Carcinoembryonic Antigen; Female; Fluorescent Antibody Technique; Humans; Immunoglobulin A, Secretory; Immunoglobulin M; Lactoferrin; Male; Middle Aged; Muramidase; Salivary Gland Neoplasms; Secretory Component

The group of tumour markers contain antigens and cell products which can be demonstrated in tumour cells by immunocytochemical methods (immunofluorescence, immunoperoxidase) and can, thus, be analysed for the classification of tumour. In human salivary gland tumours the distribution of cytoplasmatic antigens as components of the cytoskeleton, the occurrence of cell membrane antigens and of enzymatic cell products is demonstrated. Prekeratin, as an intermediate-sized filament protein, is a specific marker of epithelial tumours, whereas vimentin is a marker of mesenchymal cells. A special feature is the occurrence of prekeratin and vimentin in spindle-shaped cells of pleomorphic adenomas. The tumour-associated carcinoembryonic antigen (CEA) is found in glandular tumours and highly differentiated keratinized squamous cell carcinomas. With regard to enzymatic cell products, lactoferrin is present in glandular tumours and amylase in acinic cell tumours, but lysozyme is not detectable. The implementation of tumour markers contributes not only to an improvement in tumour diagnosis, but opens up new aspects in the cyto- and histogenesis of tumours.

Topics: Amylases; Antigens, Neoplasm; Carcinoembryonic Antigen; Cytoskeleton; Humans; Lactoferrin; Microtubules; Muramidase; Peptides; Receptors, Mitogen; Salivary Gland Neoplasms; Tissue Polypeptide Antigen