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)

Investigations on methods for the utilization of fluorescein-isothiocyanate-labelled Concanavalin A, Lens culinaris lectin and Ricinus communis lectin for immunohistological demonstration as simple sugar moieties are reported. The stainings were carried out on rabbit erythrocytes. Ehrlich ascitee tumor cells and various mammalian tissues. Optimum results were obtained in living cells and native cryostate tissue sections. The influence of different fixing agents and conditions of fixation on the degree of tissue flurorescence were studied. Generally the fluorescense decreased by aldehyde fixation. Similar effect was observed following fixation by heat. Furthermore, changes in the pattern of fluorescence depending on the type of tissue and utilized lectin were observed after aldehyde fixation. The degree of tissue fluorescence was fairly independent of the pH value. The specificity of the particular reactions for saccharide demonstration was shown; glycerol is capable of a differently strong "hapten-like" action.
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PMID:The use of flurorescein investigations with concanavalin A, Lens culinaris lectin and Ricinus communis lectin. 6 Nov 31

Tumor-specific transplantation antigen (TSTA) was solubilized from cell membranes of sarcoma Meth-A with non-ionic detergent Nonidet P40. Soluble TSTA was partially characterized by chromatographic separation and electrophoresis. The antigen responsible for tumor rejection activity had a molecular weight of approximately 70,000 daltons in the presence of detergent and an electrophoretic mobility of alpha-globulin. TSTA was well separated from mouse histocompatibility antigen H-2 by a sequence of procedures, including gel filtration, lectin affinity chromatography, column electrophoresis, and rechromatography on agarose, showed only three major bands on polyacrylamide gel electrophoresis. TSTA was specific for sarcoma Meth-A.
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PMID:Biological and biochemical properties of Nonidet P40-solubilized and partially purified tumor-specific antigens of the transplantation type from plasma membranes of a methylcholanthrene-induced sarcoma. 6 94

Normal human lymphoid cells from peripheral blood, spleen, tonsils and thymus were examined for their ability to mediate three different cytotoxic effector cell functions: antibody-dependent cellular cytotoxicity (ADCC); lectin-induced cellular cytotoxicity (LICC) and natural killer activity (NK), against 51Cr labelled erythroid and tumor target cells. We found a hierarchy of cytotoxic activities in the different lymphoid tissues. Peripheral blood and spleen cells were able to mediate LICC, ADCC and NK activities. Tonsil cells showed a natural segregation of the different cytotoxic functions: NK and ADCC activity against tumor target cells were absent, whereas LICC activity was fully present. With respect to ADCC activity against erythroid targets, tonsil cells showed low, but significant, cytotoxicity. Thymus cells had no detectable ADCC, NK and LICC activities. Correlation in the different lymphoid tissues between cytotoxic activities and cell surface marker studies revealed: (a) that the presence of E-SRBC rosette forming cells was not always associated with the detection of LICC activity, as is the case with the thymus; (b) that, in the absence of detectable Eox-7S rosette forming cells (thymus and tonsils), NK and ADCC activities against tumor cells were always absent, but LICC was observed (tonsils), indicating that the presence of this Fc(7S) receptor bearing cells is strongly associated with the expression of NK and ADCC but not with LICC.
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PMID:Comparison of the cytotoxic activities of different human lymphoid tissues. 9 8

Crude and purified murine lectin preparations are extracted from costal cartilage (TAI). They inhibit the antiviral state induced by interferon. They also agglutinate the Crocker 180/TG tumor cells. After IP inoculation in mice, the purified lectin preparation significantly decreases tumor incidence and increases the animal's life span.
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PMID:[Inhibitory effect of the tissue antagonism of interferon on the development of 180/TG Crocker tumor: recognition of a new murine lectin]. 9 61

Although not obviously immunogenic when developing intraperitoneally or subcutaneously, the P-815 mastocytoma cell induces a significant immune response when injected intradermally into the syngeneic host. In some animals the immune reaction leads to spontaneous tumor regression and survival of the animals, but in most cases the effectively initiated immune-reaction is abrogated by as yet unknown mechanisms. The T cell is identified as the killer cell both in vivo and in vitro during the described period of immune reactivity. By means of two antibodies from two different species, rendered specific for the P-815 tumor cell by in vivo absorption in DBA/2 mice, two distinct antigens have been identified, isolated and partially purified from P-815 cell membranes. One of them is obviously different from H-2 antigens, the other one shows striking similarities with H-2 antigens (molecular weight, lectin binding properties), but does not coprecipitate with H-2 antigens in an indirect precipitation assay, using Staph. aureus Cowan I as the Fc-binding agent.
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PMID:The stimulation of a T cell response in the syngeneic host by the P-815 mastocytoma cell and the isolation of a tumor-associated antigen which has some H-2 antigen characteristics. 11 88

The way in which the lectins concanavalin A (Con A) and Ricinus communis agglutinin (Ricin) alter the K+ content of Ehrlich ascites tumor cells was investigated. Unidrectional and net fluxes were determined in unwashed cells during a time course following lectin addition. Total influx, ouabain sensitive influx, Mg++- and Na+-K+-ATPase activity were all unaffected. Cell ATP content was normal for at least 19 minutes after exposure to Con A. Early after contact with Ricin or Con A efflux was stimulated 2-3-fold, resulting in net K+ loss, but after 20 minutes efflux had returned to normal. Ricin and Con A acted similarly although Ricin was present at only 1/50 the concentration of Con A. When the findings are evaluated together with previous work it is suggested that a particular membrane glycoprotein may be concerned in the efflux alteration observed.
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PMID:Nature of lectin-induced alteration of potassium transfer in Ehrlich ascites tumor cells. 13 11

A previous study demonstrated that cells of transplantable hepatocellular carcinomas were agglutinated by the plant lectin concanavalin A, while normal hepatocytes were not. In the present experiments, 95% or more of cells obtained from primary hepatocellular carcinomas which resulted from exposure of rats to N-2-fluorenylacetamide were agglutinated by this lectin. Exposure to this carcinogen also produces grossly visible foci of morphologically and biochemically altered hepatocytes which have been termed hepatic (hyperplastic; premalignant, neoplastic) nodules. Although these hepatocyte aggregates are generally accepted as precursors of the hepatocellular carcinomas, no agglutination was detected when their cells were exposed to concanavalin A. These results indicate that concanavalin A agglutinability is not acquired as a result of tumor transplantation. Furthermore, they suggest that significant alterations must occur in the cells of hepatic nodules prior to the manifestation of malignant behavior.
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PMID:Concanavalin A agglutination of cells from primary hepatocellular carcinomas and hepatic nodules induced by N-2-fluorenylacetamide. 16 71

Concanavalin A (Con A) was found to inhibit the killing of antibody-sensitized line-1 tumor cells (TA) by guinea pig complement (GPC) but not by human complement (HuC). Other plant lectins (wheat germ, leucoagglutinin, and pokeweed mitogen) were also tested but Con A was the only lectin found to inhibit antibody-GPC-mediated killing. The inhibitory effect of Con A was observed when the GPC was mixed with Con A or when the antibody-sensitized cells were pretreated with Con A (TA-Con A) before the addition of GPC. The effect could be reversed by treatment of such cells with alpha-D-methylglucopyranoside or by incubation at 37 degrees C for approximately 2 hr. Con A appeared to act by preventing the binding of the first component of GPC (GPC1) to antibody-sensitized tumor cells. Differences in the binding of the first component of HuC (HuC1) and GPC1 to TA-Con A suggested that a difference in the binding site for HuC1 and GPC1 might exist. There was no difference in the number of GPC1 molecules fixed to antibody-sensitized sheep erythrocytes (EA) or EA treated with Con A in experiments using the same antibody as used with the tumor cells and the same Con A preparation. It would consequently appear that the inhibitory effect of Con A on the binding of GPC1 to TA is not due solely to an interaction of Con A with the antibody.
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PMID:Effect of concanavalin A on the killing of tumor cells by antibody and complement. 19 97

The detergent Nonidet P40 was used to solubilize tumor-specific transplantation antigens (TSTA) from crude membranes obtained from dissociated cells of simian virus 40-induced sarcoma of BALB/c mice. A good recovery of specific tumor rejection activity was observed. One fraction, fraction V, was obtained following polyacrylamide-agarose filtration of the solubilized material, and this fraction contained most of the activity. An increased specific activity followed gel filtration. Preliminary data from lectin column chromatography of the active fraction V indicated a separation of TSTA activity from H-2 activity.
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PMID:Biologic and biochemical properties of detergent-solubilized tumor-specific transplantation antigen from a simian virus 40-induced neoplasm: brief communication. 19 60

Chickens and quails were immunized in parallel either i.v. or intramuscularly (i.m.) with lectin column-purified antigens from chick embryo cells that were transformed in vitro by avain sarcoma virus (ASV). After five to six injections, immunity of the animals was tested by challenge with ASV into the wing webs. Whereas tumor growth was inhibited after i.v. immunization with respect to incidence rate and time of tumor appearance, tumor growth was enhanced after i.m. injection. Animals that were injected with normal cell antigens served as controls. Spleen cells from only those animals that were immunized i.v. exerted a cytotoxic effect in vitro against ASV-transformed cells, whereas spleen cells from i.m. injected animals, in contrast, suppressed such cytotoxicity. The search for serum blocking or arming factors suggested that sera from i.m. injected animals block cellular cytotoxicity whereas sera from i.v. immunized animals render normal spleen cells cytotoxic (arming effect). The use of viruses from different subgroups and of antigens from gp85-lacking ASV-transformed cells indicates that immune effects were obtained against tumor cell surface antigens that differ from the antigen that is involved in virus neutralization (s-gp85).
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PMID:Influence of different routes of anti-tumor immunization: alternative induction of tumor immunity and tumor enhancement. 22 70


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