Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027651 (tumor)
 685,946 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Vimentin was isolated and purified from the pig eye lens by homogenization, ultracentrifugation, extraction in urea buffer and preparative electrophoresis. It was identified with SDS-PAGE and rabbit anti-vimentin was raised against the purified vimentin. The specificity of anti-vimentin was examined with immunohistochemical technique and double immune diffusion. Results showed that the vimentin antibody possessed good specificity for mesenchyme-derived cells. Tumor tissue sections from 151 cases were stained with anti-vimentin, anti-keratin, anti-desmin, anti-S-100 protein, anti-Factor-FVIII released antigen, and anti-lysozyme. Positive staining was obtained in mesenchyme-derived cells, while the epithelial tumor cells did not react with anti-vimentin. It indicated that vimentin antibody is effective for tumor differential diagnosis in surgical pathology.
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PMID:[Vimentin and tumor diagnosis]. 239 Jul 90

A case of hypopharyngeal lipoma is reported and the fundamental role of C.T. in the diagnosis of laryngo-pharyngeal neoplastic pathologies is emphasized. Laryngoscopy made it quite easy to detect the lesion, showing the smooth surface of a large tumor, although it proved difficult to explore the lower portion because of the narrowing of the larynx. Thermography showed a hypothermia area in the right neck region but did not offer any further information. Only C.T. made correct identification of the site and extension of the lesion possible. It was also possible to identify its fat composition, as suggested by the typical density pattern. The tumor presented a homogeneous hypodense structure and its limits were well defined throughout their entire extension. Furthermore, it was possible to rule out any macroscopic infiltration of the adjacent cartilaginous surfaces of the larynx. The latter feature was confirmed by the C.T. images obtained after intravenous administration of an iodine contrast medium and was consistent with the hypothesis of a benign lesion. Thus the lesion could be considered a lipoma; a highly uncommon non-epithelial tumor of the hypopharyngeal region but which occurs more frequently than liposarcoma. Nonetheless, such C.T. tissue characterization requires histological support so as to prevent distinguishing a well differentiated liposarcoma only after recurrence. The greatest likelihood for accurate diagnosis lies in complete utilization of the data derived from the entire diagnostic procedure. The direct laryngoscopy of the lesion is very important as it makes it possible to inspect the surface and first evaluate any anatomo-pathological alterations. Nonetheless, the most extensive information is provided by C.T.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Lipoma of the hypopharynx: role of computerized tomography in the diagnosis protocol]. 239 26

The radiobiological parameters of 33 tumor cell lines were studied in biopsy samples obtained from patients prior to radiotherapy. Epithelial tumor cells derived from head and neck cancer patients were more radioresistant than tumor cell lines derived from patients with sarcoma regardless of method of analysis. The presence of radioresistant tumor cell lines was associated with local failure in some patients. However, the presence of radiosensitive tumor cells did not necessarily predict local control. Our data suggest radiocurability is complex and inherent radiobiological parameters of tumor cells may be only one factor in radiotherapy outcome.
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PMID:Radiobiological characterization of head and neck and sarcoma cells derived from patients prior to radiotherapy. 239 10

An unusual epithelial neoplasm arising in the tongue of a 17 month-old-boy was studied by light and electron microscopy. By routine light microscopic examination, the tumor cells exhibited clear cytoplasm. Histochemical studies revealed the presence of large amounts of periodic acid-Schiff (PAS)-positive, diastase-labile material in the cytoplasm. Ultrastructurally, this material was identified as electron dense particles (20-35 nm diameter) of beta-glycogen. The epithelial nature of the tumor cells was suggested by the presence of intercellular junctions, segments of basal lamina, and well-developed Golgi complexes. Furthermore, the cells were often clustered and formed abnormal lumina with small microvillus projections. Several histologic features, such as lack of capsule, infiltration of muscle and invasion of blood vessel, indicated that this neoplasm was malignant. However, there was no recurrence or distant metastases more than 2.5 years after surgical excision, suggesting a low-grade malignancy. The glycogen-rich clear cell variant of adenocarcinoma is histogenetically derived from minor salivary glands like most of the glandular neoplasms in the oral cavity. Investigation of the literature on adult and childhood minor salivary gland neoplasms revealed that the glycogen-rich, clear-cell variant of adenocarcinoma has not previously been reported in the tongue.
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PMID:Glycogen-rich clear cell carcinoma in the tongue. A cytochemical and ultrastructural study. 242 Apr 37

Antibodies to intermediate filament proteins react in a tissue-specific manner and can be used to characterize tumor cells present in thin-needle aspirates from solid tumors, from palpable lymph nodes and cells present in samples from peritoneal and pleural effusions. From our studies so far the following conclusions can be drawn: Polyclonal antisera to cytokeratins can identify carcinoma metastases in thin-needle aspirates from palpable lymph nodes and distinguish them from malignant lymphomas and nonmalignant lesions such as chronic lymphadenitis, which show only vimentin-positive cells. Monoclonal antibodies to specific cytokeratin polypeptides are able to distinguish between different types of epithelial tumor metastases, i.e. metastases from adenocarcinomas and metastases from squamous cell carcinomas. Cells present in peritoneal and pleural effusions can be partly characterized using intermediate filament antisera. We have found that metastatic adenocarcinoma cells from breast, ovary, endometrium, cervix, colon and stomach, as well as squamous cell carcinomas and malignant mesothelioma stain specifically with antibodies to cytokeratin while mesenchymally derived tumors such as malignant lymphomas, malignant melanomas, and fibrosarcomas, are positive for vimentin only. Metastatic tumor cells of epithelial origin present in aspirates from human serous body cavity fluids may coexpress vimentin next to their original cytokeratin intermediate filaments. Benign mesothelial cells present in body cavity fluids frequently coexpress cytokeratins and vimentin. Tumor cells present in thin-needle aspirates from solid tumors such as pleomorphic adenomas of the parotid gland can be identified as such because of their typical patterns of intermediate filament (co-)expression.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Cytoskeletal proteins as tissue-specific markers in cytopathology. 242 90

We performed studies on the lectin-binding pattern in epithelial tumor cell components of 4 cases of mixed tumor of the skin developing on the face in addition to identification of keratin and carcinoembryonic antigen (CEA), compared with those of normal sweat glands. Normal eccrine glands showed specific labelling with Dolichos biflorus agglutinin (DBA) and soybean agglutinin (SBA), whereas none of the studied lectins reacted specifically with normal apocrine glands. In mixed tumors the dark cells, which form the inner layer of the tubuloalveolar and ductal structure, showed the presence of keratin and CEA, as well as of specific sugar structures that bind to DBA and SBA. On the other hand the light cells that form the outer layer of the tubular structures or the solid epithelial cell nests gave only a faint to moderate staining of keratin, and no staining of CEA or lectins. It is probable that the inner dark cells differentiate toward the cells that have the same sugar structures on the cell surface as those of the normal eccrine gland cells, while the outer light cells appear to be immature or in a less differentiated state.
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PMID:Immunohistochemical studies on epithelial cells in mixed tumor of the skin. 242 16

The malignant intraepithelial proliferations--malignant melanoma level I, bowenoid epithelial dysplasia, and mammary as well as extramammary Paget's disease--may cause differential diagnostic difficulties. We have examined 12 cases of malignant melanoma level I, nine cases of bowenoid epithelial dysplasia, 17 cases of extramammary and five cases of mammary Paget's disease for S100 protein, carcinoembryonic antigen (CEA), cytokeratin, and keratin to evaluate the sensitivity and specificity of these reactions with regard to their differential diagnostic value. Antibodies against S100 reacted specifically with the tumor cells in intraepithelial malignant melanomas; antibodies against CEA reacted specifically with the tumor cells in Paget's disease; and cytokeratin and keratin antibodies reacted with the epithelial tumor cells in Paget's disease as well as in bowenoid epithelial dysplasia. However, only antibodies to CEA and keratin showed 100% sensitivity. We conclude that the investigated antibodies may be of differential diagnostic value in cases of intraepidermal neoplasias, but that a negative reaction does not exclude diagnosis of these diseases.
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PMID:The differential diagnosis of intraepidermal malignant lesions using immunohistochemistry. 242 74

An attempt was made to detect a pancreatic tumor antigen (PTA) in transplantable pancreatic adenocarcinomas induced by N-bis(2-hydroxypropyl)nitrosamine (DHPN) in hamsters. Antibody against antigenic protein was raised by immunizing rabbits with whole homogenate of the tumors transplanted into the back of hamsters. PTA was purified by affinity chromatography and shown to have the physicochemical properties of a glycoprotein with a molecular weight of 800,000, migrating in the beta regions upon agarose gel electrophoresis. Loss of immunological properties was observed after heating at 65 degrees C for 30 min. Enzyme immunoassay revealed that the levels of PTA in the serum and tissue showed a positive correlation with the induction of the presence of tumor, and size of the tumor. It is tentatively suggested that PTA values above 150 ng/ml serum are indicators of tumors, because in normal hamsters the PTA range is from 25 to 130 ng/ml serum. Immunohistochemically, PTA was demonstrated to be localized within the cytoplasm of epithelial tumor cells of well-differentiated tubular adenocarcinomas.
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PMID:Pancreatic tumor antigen in transplantable adenocarcinomas induced by N-bis(2-hydroxypropyl)nitrosamine in hamsters. 244 68

A very rare odontogenic epithelial tumor with the combined characteristics of an adenomatoid odontogenic tumor (AOT) and calcifying epithelial odontogenic tumor (CEOT) was found in a 27 year old female. The histopathology, immunohistochemistry of keratin, lectin-binding patterns and distribution of carbonic anhydrase were determined. The nature of the calcified bodies was also examined biophysically. The tumor consisted of cuboidal and columnar odontogenic epithelial cells in the cystic wall, and AOT and CEOT in the central cavity. Odontogenic epithelial cells forming the cyst wall in the CEOT were positive for TK- and KL1-keratins, while that detected with PKK1 antibody was absent in the tumorous epithelium. Lectin binding of tumor epithelial cells was examined with Concanavalin A (Con A), peanut agglutinin (PNA), soybean agglutinin (SBA), dolichos biflorus agglutinin (DBA), wheat germ agglutinin (WGA), ricinus communis agglutinin (RCA-I), and ulex europeus agglutinin I (UEA-I) lectins, and the tumor epithelium indicated existence of glucose, mannose, Gal, GalNAc, and GlcNAc residues. The lectin binding patterns of the calcified material showed an increased intensity by enzymatic pretreatments. With an electron probe X-ray microanalyser (EPMA), the calcified lesions gave a high peak for calcium ion and for phosphorus ion and a low one for magnesium ion, as obtained from line and surface analysis.
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PMID:Odontogenic tumor with combined characteristics of adenomatoid odontogenic and calcifying epithelial odontogenic tumors. 244 95

Monoclonal antibody 1116NS 19-9 (Mab 19-9) exhibits selective reactivity with human gastrointestinal carcinomas and recognizes a carbohydrate determinant (CA 19-9) defined as a sialylated lacto-N-fucopentaose II. A scheme was devised for the purification of a human gastrointestinal tumor-associated glycoprotein antigen expressing CA 19-9 from colorectal carcinoma cell line SW1116 culture media in high yield. The key steps in the purification were immunoaffinity column chromatography with Mab 19-9 followed by reduction and alkylation of the specifically bound proteins in the presence of 6 M guanidine hydrochloride and a second Mab 19-9 immunoaffinity fractionation. The purified CA 19-9 containing glycoprotein ran as a single band on sodium dodecyl sulfate-polyacrylamide gradient gels with an apparent molecular mass of 210 kilodaltons. In the absence of detergents, this purified glycoprotein apparently reassociated to form aggregates of 600-2000 kilodaltons molecular mass as determined by size-exclusion chromatography. Amino acid analysis of CA 19-9 containing glycoprotein revealed that serine, threonine, and proline together accounted for greater than 35% of the amino acid residues, consistent with a mucin-like structure for the protein. Carbohydrate compositional analysis, however, was in contrast to a typical mucin with a fucose:mannose:galactose:N-acetylgalactosamine: N-acetylglucosamine:N-acetylneuraminic acid molar ratio of 4:1:12:2.5:5:5. The presence of both N-acetylgalactosamine and mannose suggested that both O- and N-linked oligosaccharides may exist on CA 19-9 containing glycoprotein. Protein and carbohydrate analyses indicated that this novel tumor-associated glycoprotein was 85% carbohydrate by weight. This purification procedure may be applicable to the isolation of other epithelial tumor-associated antigens.
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PMID:Purification and composition of a novel gastrointestinal tumor-associated glycoprotein expressing sialylated lacto-N-fucopentaose II (CA 19-9). 244 52


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