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Query: UMLS:C0025202 (melanoma)
 69,561 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In this paper we review the current data on the role of potentially lethal damage (PLD) recovery in human tumour cell lines, both in vitro and in vivo. In the case of cell lines studied in vitro, the mean recovery ratios found were higher for cells derived from tumours of low curability (glioblastoma, hypernephroma, osteosarcoma, melanoma) than for cells derived from tumours of high curability (breast carcinoma, neuroblastoma). Experiments were performed in vivo only with tumours of low and intermediate curability (melanoma, adenocarcinoma of the colon, pancreatic tumour). Although fragmentary and obtained only with established cell lines, these results argue in favour of the occurrence of PLD repair in human tumour, the amplitude of this repair being, in certain cases, sufficient to explain the incurability of a tumour by radiation therapy.
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PMID:Potentially lethal damage repair as a possible determinant of human tumour radiosensitivity. 650 62

Six monoclonal antibodies(Mabs) including 4 anti-melanoma, one anti-glioma, and one anti-HLA-DR have been tested in a 125I-protein A antibody binding assay using a panel of 34 different cell lines. This panel included 19 melanomas from different clinical and geographical origins, 10 fibroblast lines out of which 9 were established from melanoma patients, 2 glial cell lines, 1 osteosarcoma, 1 teratocarcinoma, and 1 murine melanoma. The reactivity pattern of the 4 anti-melanoma Mabs showed that they were not directed against antigens strictly restricted to melanoma, but rather against antigenic structures preferentially expressed on melanoma cells. These Mabs were found to crossreact with gliomas, thus they seem to recognize neuroectoderm associated differentiation antigens. The high crossreactivity of the anti-glioma Mab for melanoma was confirmed in this study. As expected from the literature, HLA-DR antigens were found to be expressed on more than 50% of the melanoma lines tested. The cellular distribution of the antigens recognized by two anti-melanoma Mabs on melanoma cells could be visualized by an autoradiographic procedure. From the labeling pattern it was concluded that only a proportion of the cells, varying from 13 to 38%, expressed the relevant antigen.
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PMID:Monoclonal antibodies to human melanoma associated antigens: study of their specificity and visualization at the cellular level of the antigenic distribution. 657 27

A salt-extractable low-molecular-weight fraction has been held responsible for the resistance of cartilage to invasion by malignant cells. To test this hypothesis, we have confronted in vitro fragments from bovine articular cartilage, from bovine nasal septum, from chick embryonic tibia, or from human knee meniscus with cells from the following malignant lines: LICR-HN-4 human squamous cell carcinoma; B16BL6 mouse melanoma; Hu-456 human transitional cell carcinoma; TE-85 and SAOS-2 human osteosarcoma; and MO4 mouse fibrosarcoma. Human embryo lung cells and chick embryonic heart cells were used as nonmalignant counterparts. Confronting cultures using living cartilage and cartilage extracted with 3 M guanidinium hydrochloride were examined light microscopically and ultrastructurally after 1 to 14 days. Neither invasion of malignant cells into the matrix of living or salt-extracted cartilage nor breakdown of collagen was observed in these cultures. In contrast, both malignant and nonmalignant cells occupied preexisting spaces in the matrix, namely, cut chondrocyte lacunae, cartilage canals, and fibrillation clefts. We concluded from these experiments that salt extraction did not alter the resistance of cartilage to invasion by malignant cells in vitro. This conclusion does not support the opinion that salt-extractable factors are solely responsible for the resistance of cartilage.
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PMID:Interaction of malignant cells with salt-extracted cartilage in vitro. 669 41

Antibodies specific for membrane-associated antigens of human osteosarcoma cells were isolated from sera of 12 patients with osteosarcoma (OS). Affinity columns were prepared by coupling purified membrane antigens from cultured human OS cell lines (TE-85 or LM) to CBrN-activated Sepharose 4B. The antigens were prepared by discontinuous sucrose gradient ultracentrifugation, papain digestion, and DEAE column chromatography. Diluted serum was passed over the affinity columns, and the adsorbed proteins were eluted with 2.5 M MgCl2 (pH 6.5). Immunodiffusion, indirect immunofluorescence, and complement fixation were used to assay antibody activity in the eluate. Specific anti-OS activity was found in the immunoglobulin (Ig) fraction isolated from the sera of the 12 OS patients, as confirmed by blocking experiments. No anti-OS antibody activity was found in sera from healthy individuals or patients with breast carcinoma, clear cell liposarcoma, or leukemia in this study. The anti-OS activity of the isolated Ig from OS patients was abolished after absorption with cultured human OS cells from lines LM, TE-85, or G292 but not after absorption with cells from lines WI-38 (embryonic lung), TE-32 (rhabdomyosarcoma), CAMA-1 or SW527 (breast carcinoma), or M-14 (melanoma). Absorption with rabbit antihuman IgG but not with rabbit antihuman IgM immunobeads completely eliminated the antibody activity.
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PMID:Osteosarcoma patients: isolation of serum antibodies by affinity chromatography. 679 43

"Crohn's Carcinoma" of a 34-year-old patient is presented in this paper. The fine structure of the tumour is discussed in detail, because there have been no previous reports of electron microscopic studies of this tumour. The adenocarcinoma cells were electron microscopically less differentiated than expected on the basis of light microscopic examinations. In the tumor cells, several round dense granules were observed. Similar granules were also described in the cells of intestinal type gastric and colon cancers, being considered a sign of pathologic mucus secretion. In a part of the tumour cells, intracisternal parallel tubular inclusions were seen like those described in malignant melanoma and osteosarcoma. In the dysplastic small-bowel mucosa adjacent to the tumour, the maturation disorder of the epithelial cells was similar to changes described in the precancerous states of the colon.
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PMID:Electron microscopic study of adenocarcinoma of the small bowel associated with Crohn's disease. 684 Feb 56

Uptake studies of the potential endoradiotherapeutic agent, 6-125I-iodo-2-methyl-1,4-naphthoquinol bis(diammonium phosphate) have been carried out in vitro on a wide range of normal and malignant human cells. In general, for a standardized dose of 0.1 microCi/ml, the uptake of the compound into normal cells was 0.0015-0.135 pCi/cell. Uptake into malignant cells was significantly higher than normal cells; uptakes of 0.89-11.3 pCi/cell were noted for melanoma, teratoma of testis, osteosarcoma and adenocarcinoma of colon and pancreas. Comparative uptake ratios for melanoma: Chang liver cells and testicular teratoma:normal testis were 29 23, respectively. Larger uptake ratios are usually observed with higher doses.
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PMID:The in vitro selective concentration of an 125I-iodinated compound in human tumor cells. 684 Nov 76

We have studied the repair of X-ray-induced, potentially lethal damage (PLD) in 9 human tumour lines derived from tumours of varying radiocurability. Cells derived from 3 tumours considered non-radiocurable (1 osteosarcoma, 2 melanoma) repaired significantly more X-ray PLD than cells from 3 tumours considered radiocurable (2 breast, 1 neuroblastoma). The remaining tumour lines were intermediate in their ability for repair, and included cells from another osteosarcoma, a hypernephroma and a glioblastoma. We conclude that the repair of X-ray PLD may be an important cellular determinant of clinical radiocurability.
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PMID:Cellular repair factors influencing radiocurability of human malignant tumours. 705 52

6-125-I-iodo-2-methyl-1,4-naphthoquinol bis (diammonium phosphate) (6-125I-iodo-MNDP) has been synthesised and studied as the prototype of a class of potential radio-halogenated anti-cancer agents. The incorporated 125I provides Auger electron radiations which behave like high LET radiations in the treatment of tumours, though the accompanying X- and gamma-radiations make an undesirable contribution to the total body dose. The in vitro experiments reported show that 6-125I-iodo-MNDP is selectively concentrated in the cells of some human malignant tumours by factor of about 15 to 20 or more in relation to the cells of normal origin studied. On the basis of dosimetric considerations and comparison with clinical treatment with tritiated methylnaphthoquinol diphosphate, practical dosage of 6-125I-iodo-MNDP is suggested and clinical indications and safety of use are discussed. The types of tumour of particular interest are inoperable cases of carcinoma of the colon, carcinoma of the pancreas, malignant melanoma and osteosarcoma. Further investigations are in progress.
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PMID:6-125I-iodo-2-methyl-1,4-naphthoquinol bis (diammonium phosphate) as a potential radio-halogenated anti-cancer agent: in vitro investigations and possible clinical implications. 706 13

We investigated the interaction of different human tumor types with resting and IL-1-activated human umbilical vein endothelial cells under laminar flow conditions using a parallel plate flow chamber. Three tumor cell lines (the HT-29M colon carcinoma, the OVCAR-3 ovarian carcinoma, and the T-47D breast carcinoma) showed limited adhesion to unstimulated endothelial cells at any of the shear stress levels tested, while rolling and massive adhesion of tumor cells were observed on IL-1-activated endothelial cells. Three other tumor cell lines (the A375M and A2058 melanomas and the MG-63 osteosarcoma) did not adhere on resting endothelial cells at high shear stress (> 1.5 dyn/cm2) and started to adhere with decreasing shear stress; the number of adherent cells increased steeply on IL-1-activated endothelial cells, but no cell rolling was observed even at the highest shear stress. These mechanisms of tumor cell interaction with endothelial cells were analyzed in detail using the HT-29M colon carcinoma and the A375M melanoma. Incubation of activated endothelial cells with a monoclonal antibody against E-selectin inhibited rolling and adhesion of HT-29M, but had no effect on the adhesion of A375M cells; monoclonal antibody against vascular cell adhesion molecule-1 reduced the adhesion of A375M cells and had no effect on HT-29M. The selective interaction of these two molecules with tumor cells was confirmed by measuring the adhesion of tumor cells on immobilized soluble proteins. On E-selectin-coated surfaces, HT-29M cells rolled during perfusion experiments without subsequent adhesion, while A375M cells did not adhere. On vascular cell adhesion molecule-1-coated surfaces, HT-29M cells neither adhered nor rolled, while A375M cells adhered massively without rolling. Under flow conditions, therefore, cells from different tumor types interact with the endothelial surface by different mechanisms, depending on adhesion molecules expressed on the tumor and endothelial cell surface.
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PMID:Rolling and adhesion of human tumor cells on vascular endothelium under physiological flow conditions. 750 97

We have found a monoclonal antibody, called BV7, that rapidly stimulated by 6-10-folds HT-29 colon carcinoma cell adhesion to resting human umbilical vein endothelial cells. This effect was directed to tumor cells and not to endothelial cells and was cell-specific. BV7 was also active on the HCCP-2998 but did not change adhesion to endothelial cells of other tumor cells (MG63 osteosarcoma, A375 melanoma, MHCC-1410 and Lovo colon carcinoma) even if, by flow cytometry, this monoclonal antibody could bind to them. Additionally, BV7 effect was substratum-specific, since it did not increase but rather blocked HT-29 adhesion to matrix proteins. Immunoprecipitation analysis and binding to specific transfectants revealed that BV7 recognizes beta 1-subunit of integrin receptors and antibody blocking experiments showed that alpha 2 beta 1 antibodies were able to counteract BV7 effect on HT-29 adhesion to endothelial cells. In contrast, antibodies directed to other integrins or endothelial adhesive receptors (E- and P-selectin, VCAM-1, ICAM-1, ICAM-2) were ineffective. Induction of HT-29 adhesion to endothelial cells by BV7 was Fc- and protein synthesis-independent but required metabolically active cells. The presence of physiological concentrations of divalent cations and of cytoskeletal integrity was not needed. Comparative studies with eight different prototypic beta 1 antibodies showed that five of them induced HT-29 adhesion to endothelial cells in a way unrelated to their ability to interfere with HT-29 adhesion to matrix proteins. Cross-blocking binding assays demonstrated that all the five antibodies recognized a topographically related epitope. Taken together these results provide evidence that beta 1 antibodies may trigger a novel pathway of HT-29 colon carcinoma adhesion to endothelial cells with different features in respect to other described mechanisms of tumor cell interaction with the endothelium.
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PMID:A novel mechanism of colon carcinoma cell adhesion to the endothelium triggered by beta 1 integrin chain. 750 99


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