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Query: UMLS:C0027651 (tumor)
 685,946 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Differential localization of glycoconjugates was detected on microvilli and microridges of the intact cell surface of frog pronephric tumor cells in tissue culture. Alcian blue and Alcian blue/PAS staining showed a heavy concentration of dye limited to the unique short microvilli and extensive microridges of the tumor cells as previously seen with SEM (Tweedell and Williams 1976). Staining was absent or greatly reduced on microvilli of the normal pronephric cell surface. Previous exposure of each kind of cells to neuraminidase or extraction by mild hydrolysis removed the active staining sites but Alcian blue uptake was unaffected by prior digestion with testicular hyaluronidase. Fluorescein isothiocyanate (FITC) bound wheat germ agglutinin (WGA) produced a similar pattern of fluorescence on the microvilli of the tumor cells and a limited distribution on the normal cells. Digestion with neuraminidase preferentially removed but did not completely eliminate the surface binding of WGA on both the normal and tumor cells. Exposure of tumor cell monolayers to FITC bound limulin, a lectin specific for sialic acid, also produced an intense surface fluorescence on the microvilli and ridges of tumor cells. Prior treatment with neuraminidase prevented the surface fluorescence but not internal binding. Normal pronephric cells gave sparse surface fluorescence but extensive internal binding. Each procedure indicates a preferential localization of complex carbohydrates, including sialic acid, on the unique microvilli of the tumor cells. Concurrent assays for sialic acid recovered from the tumor cells indicated that lectin bound surface sialic acid was removable with neuraminidase.
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PMID:Localization of glycoconjugates on the surfaces of pronephric tumor cells in vitro. 618 38

A fetal antigen (FA) was isolated from spent culture medium of a melanoma (M14) cell line. Allogeneic serum samples from melanoma patients, previously characterized with respect to anti-FA activity, were used as the source of anti-FA antibody. The FA activity was partially purified by membrane ultrafiltration, gel filtration, and chloroform:methanol extraction. The partially purified FA was then used to develop an enzyme-linked immunosorbent assay (ELISA). By indirect ELISA both the IgG and IgM classes of anti-FA antibodies were detected in the sera of cancer patients and normal volunteers. The incidences of anti-FA antibodies in the sera of cancer patients and normal volunteers were not significantly different. As detected by competitive inhibition in ELISA, FA activity was widely distributed among melanoma, sarcoma, and carcinoma tumor tissues and cultured tumor cells, as well as among fetal brain, skin, and muscle tissues. FA activity was destroyed by treatment with beta-galactosidase and hyaluronidase, but it was not destroyed by proteolytic and lipolytic enzymes. The antigen bound to immobilized ricin, peanut, and soybean lectins. FA activity in material purified by ricin-affinity chromatography was associated with molecules in the 60,000- to 70,000-dalton region as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. These results suggest a glycoprotein nature for the FA isolated from the spent culture medium of melanoma (M14) cells; this FA apparently elicits formation of natural antibodies in the cancer patients and normal donors.
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PMID:Immunochemical characterization of fetal antigen isolated from spent medium of a human melanoma cell line. 619 35

Immunization of mice with a plasma membrane-enriched fraction from human malignant melanoma cells and subsequent generation of hybridomas resulted in the isolation of an IgG1 monoclonal antibody, 155.8, that recognizes chondroitin sulfate proteoglycans. By cell binding analysis, 155.8 was shown to react with seven of eight cultured melanoma cell lines, but not with a variety of lymphoblastoid cell lines or cultured tumor cells derived from other solid tumor types. Indirect immunoprecipitation of the 155.8 antigen from intrinsically labeled melanoma cells revealed a glycoprotein of Mr = 250,000 and a sulfated molecule of Mr greater than 400,000. The antigen was identified as a chondroitin sulfate type A/C proteoglycan synthesized by melanoma cells on the basis of its sensitivity to chondroitinase ABC digestion and the identification of sulfated glycosaminoglycans released from the antigen immunoprecipitated by 155.8. The determinants recognized by antibodies 155.8 and 9.2.27, another anti-chondroitin sulfate proteoglycan, immunoprecipitate only a proteoglycan from high density cesium chloride gradient fractions, (1.487 g/liter); however, they immunoprecipitate a free glycoprotein of Mr = 250,000 from low density fractions (1.317 g/liter). This demonstrated that the 155.8 and 9.2.27 determinants, both of which reside on the glycoprotein of Mr = 250,000, are also present in the proteoglycan, suggesting that this glycoprotein is the proteoglycan core protein. Monoclonal antibody 155.8 reacts with a determinant on the core protein distinct from that recognized by 9.2.27. Proteoglycans bearing 155.8 determinants are distributed on the surface of cultured melanoma cells in a punctated fashion that apparently resolves to short, filamentous structures at high magnification. Immunohistochemical analysis demonstrated that 155.8-defined proteoglycans are found in freshly biopsied melanoma tissue, suggesting that these antigens are also synthesized in vivo by melanoma cells.
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PMID:Characterization of monoclonal antibody 155.8 and partial characterization of its proteoglycan antigen on human melanoma cells. 619 23

In 41 salivary gland tumors, the characteristics of the intercellular components and vascular endothelial cells were surveyed by immunohistochemical staining for laminin and factor VIII-related antigen (VIII R:Ag), and by mucopolysaccharidase-digestion for glycosaminoglycan (GAG). In myxomatous areas of pleomorphic adenomas, small vessels (diameter 6.5 +/- 0.11 micron) were frequent and found to be negative or weakly positive by VIIIR:Ag staining although endothelial cells were clearly positive for VIIIR:Ag in capsule surrounding the tumor tissues. Alcian blue stainability was diminished by treatment with both Streptomyces hyaluronidase and chondroitinase. By laminin staining, a vascular pattern was clearly detected, but the majority of tumor cells were not stained. In adenomatous areas, the basement membrane-like linear laminin-staining reaction was observed to be weak and inconsistent around some tumor cell nests. However, in adenoid cystic carcinomas, laminin-positivity was much more intense than in other tumors such as pleomorphic adenoma, mucoepidermoid tumor and adenocarcinoma. In cylindromatous areas, the inner luminal surface in the pseudocysts was markedly positive for laminin, and there was weak positivity around tumor cell nests having a trabecular pattern. By immunoelectron microscopy, a juxtacellular network of replicated basal lamina of tumor cells which lined the inner surface of pseudocysts was positive for laminin. Alcian blue-positivity in the pseudocyst was abolished with heparitinase and chondroitinase, but not with hyaluronidase.
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PMID:Histochemical studies of intercellular components of salivary gland tumors with special reference to glycosaminoglycan, laminin and vascular elements. 620 53

Six cases of synovial sarcoma were examined histochemically in order to clarify the components of mucosubstances in the tumor tissues. The tumors were classified into 1) monophasic type, 2) predominantly monophasic type with focal biphasic differentiation, and 3) biphasic type. The former two groups and sarcomatous areas in the biphasic tumors contained various amounts of hyaluronic acid, chondroitin sulfate, and, in some cases, heparitin sulfate. By contrast, the epithelioid regions in the biphasic-type tumors had periodic acid-Schiff-positive glycoproteins which contained various amounts of sialic acid, in addition to hyaluronic acid and chondroitin sulfate. The significance of the presence of glycoproteins in the mesenchymal tumors is emphasized. It seems likely that the synovial sarcomas contain various kinds of mucosubstances and that sensitivity to hyaluronidase treatment is not necessarily the diagnostic criterion of synovial sarcoma.
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PMID:Histochemical characterization of mucosubstances in synovial sarcoma. 620 16

Co-culture of cancer patients' nonadherent peripheral blood lymphocytes with irradiated autologous fresh tumor cells, termed the mixed lymphocyte-tumor interaction (MLTI) test, resulted in significant stimulation of 3H-Tdr in corporation on day 6 in 19 of 37 autologous combinations. The MLTI test was performed in a microtiter wells (0.2 ml) and a variety of solid tumor cells (sarcomas and carcinomas) were used. Tumor cells were dissociated from the fresh biopsy tissue by nontrypsin enzymatic digestion (deoxyribonuclease, hyaluronidase, and collagenase) and the tumor cells enriched by depletion of macrophages using adherence procedures. Occasionally, further tumor cell purification was achieved by separation of cells on the basis of size on dis-continuous gradients. Positive MLTI resulted in stimulation as high as 20-fold over the backgrounds of PBL and tumor cells cultured alone. Mean positive MLTI was SI of 7.7. The negative MLTI were not a reflection of generalized immunosuppression, because tumor cell preparations that did not stimulate autologous PBL did stimulate allogeneic PBL. In an additional patient, PBL not responding in the autologous MLTI did respond to allogeneic tumors. MLTI using cryopreserved cells reproduced the MLTI results using fresh cells in 11 of 16 tests; the other five tests were all positive in the fresh MLTI and negative when using cryopreserved cells. Despite reports from many other groups it appears that positive MLTI were not tumor-specific. In 14 experiments we were able to simultaneously test the proliferative response to autologous tumor as well as to an autologous normal tissue (lung, liver, colon, and bowel). In eight of these experiments positive responses were obtained with tumor stimulators and in seven of these, positive proliferation was also obtained with normal tissue.
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PMID:The human mixed lymphocyte-tumor cell interaction test. I. Positive autologous lymphocyte proliferative responses can be stimulated by tumor cells as well as by cells from normal tissues. 620 46

Tumors and tumorous conditions of superficial and deep soft tissues may owe their naked-eye appearance and much of their bulk to the accumulation of mucopolysaccharide material or, on rare occasions, to edema. The so-called myxoid tumors may be chondroblastic, fibroblastic, lipoblastic, myoblastic, or neurogenic. Benign and malignant tumors may be encountered. Naked-eye and microscopic appearances are described. Pseudotumors such as bursae, ganglia, cutaneous mucinoses, fasciitis, and myxoid cysts may enter the differential diagnosis. The value of accurate documentation is stressed. Histochemistry can make a limited contribution to diagnosis. The entities described have been examined with regard to alcian blue staining with and without pretreatment with hyaluronidase. Alcian blue staining in the presence of increasing concentrations of magnesium chloride has been investigated and found to be of value in the identification of tumors of chondroblastic origin.
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PMID:The myxoid tumors of somatic soft tissues. 626 45

Histochemical studies were performed on glycosaminoglycan (GAG) components in Wilms tumors of rats and rabbits and fetal kidneys of rats. 1. Wilms tumors. The interstitial components had an intense stainability with Alcian blue, and digestion test with hyaluronidase and chondroitinase was intensely positive. The epithelial tumor cells, showing a tubular pattern, were also stained with Alcian blue. The enzyme-digestion test was positive in the basal portion of the tumor cells, whereas it was negative in the free surface of the cells. 2. Rat kidneys. In fetal rats, the epithelial cells as well as the interstitial components were stained with Alcian blue, and the enzyme-digestion test was intensely positive. However, in adult rats, Alcian blue-stainability in the free surface of the tubular epithelium was not abolished by treatment with hyaluronidase and chondroitinase. The substance in the free surface seemed to be consisted mainly of heparan sulfate. Although the physiological significance of GAG in the cell surface cannot be deduced, it is quite conceivable that GAG, especially heparan sulfate, plays an important role in fluid absorption and transportation.
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PMID:[Histochemical study of glycosaminoglycan in Wilms tumors of rats and rabbits and fetal kidneys of rats]. 629 55

An autopsy case of pseudomesotheliomatous carcinoma of the right lung in a 56-year-old man occupationally exposed to stone dust is presented. From open biopsy specimens in which polyhedral epithelium-like cells appeared arranged in nests, sheets, and trabecula without apparent tubular pattern, a malignant pleural mesothelioma was suspected. At autopsy, the right pleural cavity was obliterated by the tumor mass which covered the collapsed pulmonary parenchyma and was clearly demarcated from it. The gross appearance of the tumor was similar to that of malignant pleural mesothelioma. Histologically, marked interstitial fibrosis of the subpleural parenchyma of both lungs was observed, and the tumor tissue was interspersed in the parenchyma adjacent to the tumor mass. The tumor showed both intracytoplasmic and intercellular positive materials with colloidal iron, alcian blue (pH 2.5), and toluidine blue stains, which entirely disappeared after streptomyces hyaluronidase digestion. A small amount of intracytoplasmic PAS-positive material resistant to diastase digestion was also observed. Immunohistochemical staining for carcinoembryonic antigen, which is said to be negative in malignant pleural mesothelioma, was positive intracellularly. There were no histologic findings indicating asbestos exposure. From these findings, the authors made a diagnosis of poorly differentiated adenocarcinoma, which was characterized by the production of hyaluronic acid.
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PMID:Pseudomesotheliomatous carcinoma of the lung with histochemical and immunohistochemical study. 634 86

Transfection is a technique for inducing transformation of normal fibroblasts (NIH 3T3) with DNA (oncogenes) from human tumors. Our goal was to determine if these transformed cells expressed antigens associated with malignancy. NIH 3T3 cells were transfected with DNA fragments from a human acute lymphocytic leukemia (ALL 1-69), and transformed colonies were selected for growth in soft agar. Transfected cells containing human DNA sequences demonstrated by Southern blot analysis were used to immunize Balb/C mice. Monoclonal antibodies were produced and screened for binding to the parental leukemia (ALL 1-69), transfectant (17(2], and 3T3 cells in an enzyme-linked assay. A monoclonal antibody (IgM kappa) designated 17-9H3 bound to ALL 1-69 and secondary transfectant 17(2) but not to NIH 3T3 plasma membranes. Immunoperoxidase staining confirmed this binding pattern and demonstrated that the antigen was expressed on the cell surface. Expression of the antigen by transfectants directly correlated with the presence of a single 6.1 kilobase human DNA sequence. The antibody binding site of the antigen was inactivated by trypsin, glucosidase, and hyaluronidase. Binding of the 17-9H3 antibody was selective for acute lymphocytic leukemias (5/8) and osteogenic sarcomas (33/36), although other tumor types did demonstrate significant binding by immunoperoxidase staining. The majority of normal tissues did not bind 17-9H3 with the exception of some metabolically active cells (renal tubular epithelium, secretory epithelial cells, and cardiac smooth muscle), germ cells, Leydig cells of the testes, and some lymphoid cells. Monoclonal antibodies to oncogene-associated antigens may be potentially useful for cancer diagnosis and therapy and as probes for oncogene isolation.
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PMID:A novel approach to production of antitumor monoclonal antibodies: antibody to a cell surface glycoprotein associated with transformation by a human oncogene. 637 59


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