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

This study investigates the nature and specificity of cytotoxic T lymphocytes (CTL) in patients with melanoma which are able to kill autologous melanoma cells. Interleukin 2 (IL2)-dependent T cell clones from two melanoma patients and a normal subject were generated in mixed lymphocyte cultures (MLC) or mixed lymphocyte tumor cell cultures (MLTC) and propagated for prolonged periods in tissue culture. Analysis of their phenotype by a wide range of monoclonal antibodies (M.Abs) revealed two main phenotypes which depended on whether they expressed Fc receptors detected by Leu 11 M.Abs or not. Leu 11- T cells (referred to as Type 1) were inhibited by M.Abs to T3, T8, and a common HLA, ABC antigen. Conversely Leu 11+ T cells (referred to as Type 2) were inhibited by M.Ab to Leu 11 but not by M.Ab to T3, T8 and the HLA, ABC antigen. Subtypes among Type 1 cells were recognized which depended on their specificity. The most restricted were CTL [Type 1(a)] clones generated only in MLTC which recognized the autologous melanoma cell plus 1 of 11 other melanoma target cells. Type 1(b) CTL clones recognized a larger proportion (approximately 50%) of the melanoma cells. A third category [Type 1(c)] recognized antigens on melanoma cells shared with that on the EBV-transformed B cells used as stimulators in the MLC. Type 2 CTL clones had broad specificity to melanoma and nonmelanoma cells, characteristic of that described for lymphokine activated killer (LAK) cells. The latter were MHC unrestricted but further studies are required to clarify whether the Type 1 CTL clones are MHC restricted or not. The CTL activity of all clones was inhibited by M.Ab to the sheep red blood cell receptor and to the T10 antigens. It is suggested that recognition of these different types of CTL clones may assist future studies on the immune response against melanoma and the nature of antigens recognized by CTL.
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PMID:Clonal analysis of cytotoxic T lymphocytes (CTL) against autologous melanoma. Classification based on phenotype, specificity and inhibition by monoclonal antibodies to T cell structures. 242 40

A retrospective analysis was undertaken in which 15 female and 15 male breast cancers were matched by age, stage, estrogen receptor status, and histologic type. Our protocol compares male and female breast cancers for reactivity with antibodies against tumor-associated antigens known to be present on female breast cancer cells. Formalin-fixed sections of each primary tumor were reacted in the ABC immunoperoxidase assay against antibodies B72.3 and DF.3 and an antibody to the ras p21 antigen. Reactivity to B72.3 and DF.3 was similar. However, the ras p21 antigen was expressed to a significantly greater extent in female breast cancers (p = .0008). Thus, although there are similarities in antigenic phenotype of male and female breast cancers, some female breast cancers may have a different pathogenesis as demonstrated by increased amounts of a specific oncogene product.
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PMID:A comparison of tumor-related antigens in male and female breast cancer. 242 26

A histopathological and immunohistochemical study has been made on a case of an ovarian cancer that developed into a dermoid cyst with a malignant transformation. The case involved a 64-year-old married woman and her clinical grading was determined as being in Stage Ia (i). The ovarian tumor, weighing 1550 g, consisted of large cystic and small solid parts, and a well-differentiated squamous cell carcinoma (large cell, keratinized type) was observed in the solid part. By using an immunoperoxidase technique (the ABC method), the SCC was found to be positive in many cancer cells and the TPA also was positive in some cancer cells, though both the CEA and AFP were found to be negative.
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PMID:[A case report of ovarian squamous cell carcinoma developing into a dermoid cyst with malignant transformation--immunohistochemical study]. 244 9

In order to clarify the biological characteristics of rat mammary tumors induced by 7,12-dimethylbenz-[a]-anthracene (DMBA), histochemical and immunohistochemical studies were performed. Two types of luminal spaces were observed within the tumor. In one type, the lumen was surrounded by eosinophilic columnar cells which were strongly reactive for soybean agglutinin (SBA) but weakly stained with keratin antibodies. In the luminal spaces, substances positive for PAS, dialyzed iron ferrocyanide or alcian blue and resistant to mucopolysaccharidase were occasionally observed. Ultrastructurally, the luminal surface was characterized by the presence of microvilli and tight junctions. In the other type, the lumen was often found in highly cellular foci and surrounded by pale, polygonal or elongated cells which were weakly stained with keratin antibodies but not SBA. The luminal spaces presented a peculiar structure filled mainly with mucoid substances sensitive to hyaluronidase, chondroitinase ABC and heparitinase, and the inner surface of the spaces was surrounded by basement membrane components: laminin, fibronectin and type IV collagen. The results of the present study therefore showed that DMBA-induced mammary tumor consists, partly, of a structure resembling human adenoid cystic carcinoma.
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PMID:Immunohistochemical studies of DMBA-induced rat mammary tumors. 245 33

The capacity of various blood-borne cells, whether normal or malignant, to extravasate was found to correlate with heparanase-mediated degradation of HS in subendothelial ECM. This degradation was stimulated by proteases or plasminogen and inhibited by native heparin and by various modified nonanticoagulant species of heparin. These heparins also induced a marked reduction in tumor cell metastasis and autoimmune diseases in experimental animals. Heparanase-mediated degradation of HS in ECM also released EC growth factors that are stored in ECM, most likely by high affinity binding to HS. Such growth factors were extracted from subendothelial ECM synthesized in vitro and from basement membranes of the cornea in vivo, and are structurally and functionally related to bFGF;bFGF binds to ECM and is readily released by incubation with either HS, heparin or low MW heparin fragments as well as by various normal and malignant cells and by heparanase-mediated degradation of ECM HS. In contrast, there was little or no release of growth-promoting activity upon incubation of ECM with hyaluronic acid, chondroitin sulfate or chondroitinase ABC. A model is proposed suggesting that regulation of capillary growth and neovascular response may result from displacement of an angiogenic protein (bFGF) from its storage sites within basement membranes.
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PMID:Involvement of heparanase in tumor metastasis and angiogenesis. 246 49

Monoclonal antibodies (MAbs) that are candidates for antibody-directed therapy were evaluated by a flow cytometric method. This method accurately quantitates the intensity of staining and the percentage of cells from freshly derived primary tumors expressing the relevant cell surface antigens. This method was applied to human colorectal, gastric, and ovarian carcinomas. It allowed calculations of the number of drug molecules that potentially could be delivered by each MAb as well as selection of the optimal combinations of antibodies for treatment of each type of cancer. The binding of all the MAbs varied among the tumors, although combinations of antibodies reduced this problem. A combination of MAbs C14 and NCRC-23 recognized 97% of colorectal tumors. A combination of C14, NCRC-23, and 791T/36 recognized 95% of gastric tumors. Combinations of either 791T/36 and C14 or 791T/36 and NCRC-11 recognized 80% of ovarian tumors. The number of cells binding with a single MAb varied within the tumor. The optimal anti-colorectal tumor antibody was NCRC-23 (anti-carcinoembryonic antigen), which recognized a mean of 65% of the large cells within a tumor at a mean antigen density of 4.9 X 10(5) sites/cell. The optimal anti-gastric tumor antibody was C14 (anti-Y hapten), which recognized a mean of 66% of the large cells within a tumor at a mean antigen density of 4.4 X 10(5) sites/cell. The optimal anti-ovarian antibody was 115/D8, which recognized 54% of the large cells at a mean antigen density of 4.2 X 10(5) sites/cell. These antigen densities were similar to those calculated for HLA/ABC antigens in colorectal and ovarian cancers. However, the gastric tumors expressed elevated levels of major histocompatibility complex class I antigens, with a mean density of 7.3 X 10(5) sites/cell. Combinations of antibodies that recognize a high proportion of tumor cells are likely to be necessary for MAb-drug targeting to prevent tumor recurrence and/or metastases.
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PMID:Flow cytometric screening of monoclonal antibodies for drug or toxin targeting to human cancer. 246 79

In order to analyze the mucoid substance in the epithelial component of synovial sarcoma, electron microscopic and cytochemical studies were made on three of these neoplasms. The mucoid substances in the glandular lumen were intensely stained with ruthenium red (RR), appearing as granular, fibrillar and amorphous structures. RR staining of proteoglycans was diminished after treatment with chondroitinase AC or ABC, and was partially diminished by exposure to streptomyces hyaluronidase. Trypsin treatment did not affect RR staining of proteoglycans in the lumen. On thin sections stained with periodic acid-thiocarbo-hydrazide-silver proteinate (PA-TCH-SP), deposits of reaction product were observed on the mucoid substances within the lumen, and were localized in the Golgi complex, including the rough endoplasmic reticulum, small vesicle and lysosome-like dense body. Trypsin digestion decreased the stain intensity of PA-TCH-SP. These results indicate that the lumen of the gland-like component contains glycoproteins as well as proteoglycans mainly consisting of chondroitin sulfate and hyaluronic acid, and suggest that GERL (Novikoff) is closely related to production, storage and transport of glycoproteins in the cytoplasm of tumor cells.
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PMID:[Ultrastructural cytochemistry of epithelial gland-like component in synovial sarcoma]. 249 43

Glycosaminoglycans were prepared from the Engelbreth-Holm-Swarm mouse tumor. Enzymatic analysis demonstrated heparan sulfate (95.8%) and chondroitinase ABC-sensitive galactosaminoglycans (4.2%). HPLC analysis of the disaccharide units showed that heparan sulfate chains were undersulfated on average, comprising approximately 30% nonsulfated and 60% N-sulfated disaccharide units with small proportions of other monosulfated and disulfated disaccharide units. In contrast, galactosaminoglycan chains were oversulfated, containing an appreciable proportion (15%) of a 4,6-disulfated (so-called E-type) disaccharide unit in addition to 51% of a 4-sulfated, 22% of a 6-sulfated, and 11% of a nonsulfated disaccharide unit. The significance of the oversulfated disaccharide structure is discussed in relation to the possible regulation of functions of hybrid proteoglycans from which the galactosaminoglycan chains are derived.
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PMID:The Engelbreth-Holm-Swarm mouse tumor produces undersulfated heparan sulfate and oversulfated galactosaminoglycans. 252 30

The size of the heparan sulfate chains from the Engelbreth-Holm-Swarm (EHS) tumor heparan sulfate proteoglycan (PG) was measured by several techniques in order to resolve uncertainty about their size and the chains were chemically characterized for comparison with other basement membrane heparan sulfate PGs. Heparan sulfate size was determined by gel filtration (Mr = 5.5 - 6.0 x 10(4], by equilibrium sedimentation centrifugation (Mw = 6.8 x 10(4], and by end group analysis (Mn = 7.1 x 10(4]. A higher molecular weight (HMW) (Mw = 2.13 x 10(5] calculated from scattering measurements may reflect chain-chain interactions. Forty percent of newly synthesized chains eluted on gel filtration as a lower molecular weight (LMW) shoulder and in vivo turned over faster than the larger species. A large heparan sulfate PG was present after 4 hours of in vivo 35SO4 labeling in both a low density form and a high density, slightly smaller form with large heparan sulfate chains (Mr approximately 8.0 x 10(4]. Heparan sulfate PG of intermediate size (Kav = 0.3-0.65, Sepharose CL-4B) and of smaller size (Kav = 0.75, CL-4B) were found predominantly as high density species. These PGs contained chains (Mr = 3.5 x 10(4) and Mr = 1.2 x 10(4), respectively) which were partially sensitive to chondroitinase ABC (CABC) and may include a hybrid heparan sulfate/chondroitin sulfate PG. Heparan sulfate chains, possibly intracellular degradation products, were also found. Heparan sulfate chains were normal in N-sulfation (58% of hexosamine residues) and in iduronate content (approximately 30%). N-sulfation started within two disaccharides of the linkage region. The EHS heparan sulfate was unusually low in O-sulfation (10% of the total sulfation) and no 6-O sulfated, N-acetylated glucosamine residues adjacent to N-sulfated block regions were found.
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PMID:Analysis of heparan sulfate from the Engelbreth-Holm-Swarm (EHS) tumor. 253 57

The culture system of hepatocellular carcinoma (HCC) has been established and the effect of hepatotrophic factors on these cell lines have been studied. During this study the effect of the human epidermal growth factor intensifying anti-tumor action of anti-tumor agents will be evaluated. HCC cell lines (C-HC-4, C-HC-20) show logarithmic growth in the serum-free medium. These growth curves after administration of 1 x 10(-12- -8) M of hEGF were measured, and the existence of the hEGF receptors was evaluated using the ABC method. The growth curve of HC-4 transplanted into nude mice was measured in 4 groups; the control group, the hEGF group, the gamma Interferon (gamma IFN) group, and the hEGF + gamma IFN group. The hEGF enhanced the cell growth of C-HC-4 and C-HC-20, and EGF receptors were confirmed immunohistologically. In the hEGF+ gamma IFN group, growth inhibition seems to be most important. The hEGF may intensify the anti-tumor action of the anti-tumor agents.
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PMID:[Development of a new therapeutic method in hepatocellular carcinoma using a culture system--the intensifying effect of human epidermal growth factor (hEGF) on the antitumor action of antitumor agents]. 254 26


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