Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0001430 (adenoma)
 21,222 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Immunohistochemical examinations of lacrimal gland specimens were carried out with monoclonal antibodies to S-100 protein and glial fibrillary acidic protein (GFAP) in 3 cases of normal tissue, 2 cases of hypertrophy and 3 cases of pleomorphic adenoma of the lacrimal gland. In specimens of normal lacrimal gland tissue, S-100 protein was identified in myoepithelial cells and ductal epithelia, but GFAP was not identified in any part of the gland. In specimens of lacrimal gland hypertrophy, the findings were identical. In pleomorphic adenoma of the lacrimal gland, asteroid cells in the myxoid and/or chondroid areas were strongly stained by antibodies to both S-100 protein and GFAP. In the solid areas of pleomorphic adenoma specimens, S-100 protein-positive fusiform or round cells and GFAP-positive round cells were observed. It was thought that S-100 protein-positive cells could have originated from myoepithelial cells and that GFAP could be a tumor-associated antigen. These findings agreed with recent immunohistochemical findings in pleomorphic adenoma of the salivary gland. It was speculated that pleomorphic adenoma of the lacrimal gland could cause mesenchymal metaplasia of the myoepithelial cells, as happens in pleomorphic adenoma of the salivary gland.
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PMID:Immunohistochemical study of pleomorphic adenoma of lacrimal gland. 166 41

We performed immunohistochemical examinations in 1 hypertrophy and 3 pleomorphic adenomas of the lacrimal glands with monoclonal antibodies to S-100 protein and GFAP (glial fibrillary acidic protein). It was thought that hypertrophy of the lacrimal gland would be cytological equivalent to normal lacrimal gland tissue because of the lack of cytological atypia except when accompanied by lymphoid infiltration. In hypertrophy of lacrimal gland, S-100 protein was identified in myoepithelial cells and parts of the ductal epithelia, but GFAP was not identified in any part. In pleomorphic adenomas of lacrimal glands, asteroid cells of myxoid and/or chondroid areas were strongly stained with both antibodies to S-100 protein and GFAP. In solid areas of pleomorphic adenomas, S-100 protein-positive fusiform or round cells and GFAP-positive round cells were observed. It was thought that S-100 protein-positive cells could have originated from myoepithelial cells and GFAP could be a tumor-associated antigen. The results coincided with recent immunohistochemical findings of pleomorphic adenoma of the salivary gland. It was suspected that pleomorphic adenoma of lacrimal gland could develop from mesenchymal metaplasia of myoepithelial cells as in the case of pleomorphic adenoma of salivary gland.
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PMID:[Immunohistochemical study of pleomorphic adenoma of the lacrimal gland]. 216 72

Pleomorphic adenoma of the salivary glands was studied by the peroxidase-antiperoxidase method and Ouchterlony's double diffusion for the presence of so-called nervous system-specific proteins, S-100 protein, glial fibrillary acidic protein (GFAP), and astroprotein. Positive immunostaining for S-100 protein was observed in tumor cells of epithelial, myxomatous, and chondroid areas. An immunodiffusion test confirmed its presence in the tumor. Normal salivary glands were also stained with anti-S-100 serum, but the reaction was less intense than that of tumor. Specific immunostaining for GFAP and astroprotein was found in a small number of cells of myxomatous and chondroid areas and occasionally in cells in epithelial areas. An immunodiffusion test suggests that the GFAP-related antigen of the pleomorphic adenoma showing a minor heterogeneity of antigenic determinants is almost identical with GFAP. Normal salivary glands did not stain with GFAP or astroprotein antisera, nor did they react with anti-GFAP serum by immunodiffusion. Thus, the S-100 protein and GFAP-related antigen may be actively synthesized in adenoma cells during the course of tumor development. In addition, the GFAP-related antigen is considered to be a tumor-associated antigen of pleomorphic adenoma of the salivary glands.
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PMID:Localization of S-100 protein and glial fibrillary acidic protein-related antigen in pleomorphic adenoma of the salivary glands. 628 62

The measurement of both immune complex-bound and free unbound tumor-associated antigen was evaluated independently on a panel of sera from colon cancer patients by radioimmunoassay (RIA). A monoclonal antibody (mAb 46.3) raised against secreted antigens from human colon cancer cells in vitro was utilized in the RIA. When circulating immune complexes alone were analyzed, the data demonstrated that 5 of 5 (100%) Dukes' A patients and 11 of 16 (69%) Dukes' B patients had elevated levels of immune complexes reactive with mAb 46.3. Analysis of free circulating antigens demonstrated elevated levels of mAb 46.3-reactive antigen present in 5 of 5 (100%) Dukes' A patients and 15 of 16 (95%) Dukes' B patients. However, by analyzing total reactivity, defined by combining results from RIA with free and immune complex-bound antigen, the sensitivity of detection for Dukes' B increased to 16 of 16 (100%). Total antigen levels in sera from patients with benign diseases (ulcerative colitis, Crohn's disease, adenoma) were not significantly different from normal controls. Analysis of both free and bound antigen in RIA is, therefore, a more sensitive indicator than RIA with immune complex alone. For the advanced stages of disease, only 1 of 5 (20%) Dukes' C and 0 of 5 (0%) Dukes' D sera were positive for reactive immune complexes. When the combined RIA was evaluated, 3 of 5 (60%) and 1 of 5 (20%) Dukes' C and D sera, respectively, were positive with mAb 46.3. Taken together, these results show that RIA with mAb 46.3 is a sensitive indicator for the early stages of colon cancer.
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PMID:Improved detection of the early stages of colon cancer by determining both free circulating and immune complex-bound antigens reactive with monoclonal antibody. 803 25

The MN/CA9 protein is a tumor-associated antigen that has been shown to have diagnostic utility in identifying cervical dysplasia and carcinoma. MN/CA9 expression is limited to very few normal tissues. We have now extended those observations to further investigate expression of the MN/CA9 protein in histological sections and fine-needle aspiration biopsy smears of normal kidney, benign renal cell lesions, all categories of renal cell carcinomas (clear/granular/spindle cell, chromophilic cell, chromophobic cell, and collecting duct cell RCCs), metastatic RCCs, and non-renal cell clear cell adenocarcinomas. We have found that high levels of MN/CA9 expression is seen in all primary RCCs, cystic RCCs, and metastatic RCCs, with the exception of two cases of the chromophobe cell type, which were MN/CA9 negative. Identical MN/CA9 immunostaining was also observed in the aspiration cytological smears. In contrast, all benign lesions, including pyelonephritis, renal cysts, adenomas, oncocytomas, and normal kidney, did not express the MN/CA9 protein. Thus, we conclude that MN/CA9 protein expression could serve as a valuable adjunct to the cytological and histological diagnosis of benign renal cysts versus cystic RCC, adenoma versus RCC, and oncocytoma versus granular cell RCC. Diffuse membraneous staining of all RCCs (with the exception of chromophobic cell RCC) suggests that MN/CA9 protein expression might have an important clinical utility in the early detection and treatment of RCC. Absence of MN/CA9 expression in non-renal cell clear cell adenocarcinoma also indicates that MN/CA9 protein expression may be used as a differential diagnostic biomarker of metastatic clear cell RCC.
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PMID:Identification of the MN/CA9 protein as a reliable diagnostic biomarker of clear cell carcinoma of the kidney. 923 Jan 82