concanavalin a/злокачественная опухоль

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Tumor dependency of concanavalin A-induced potentiation of tumor cell immunogenicity.

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The immunogenicity of concanavalin A (Con A)-treated tumor cells was examined in 4 histologically distinct tumors originated from 3 different strains of mice. In all of these tumors, Con A-treated tumor cells induced stronger tumor-specific immunity than Con A-free tumor cells as determined from the

Chemo-immunotherapy of methylchoranthrene-induced fibrosarcoma by concanavalin A-bound tumor vaccine, levamisole and mitomycin C.

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Concanavalin A (ConA)-bound-tumor cell vaccine of methylchoranthrene-induced fibrosarcoma (Meth 1) induced tumor-specific immunoprophylactic and immunotherapeutic response against an inoculum of live Meth 1 cells in histocompatible animals. ConA-free Meth 1 vaccine induced much less response under

Immunoprophylactic and immunotherapeutic response by concanavalin A-bound tumor vaccine enhanced by chemotherapeutic agents eliminating possible suppressors.

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The combined administration of mitomycin C (MMC) on Day 5 and concanavalin A (Con A)-bound L1210 murine leukemia vaccine on Days 1 and 8 induced an enhanced therapeutic response in animals bearing L1210 leukemia greater than that inducible by either of them. The enhancement was dependent on the

Induction of myeloid colony-stimulating activity in murine monocyte tumor cell lines by macrophage activators and in a T-cell line by concanavalin A.

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Certain fibrosarcoma lines in culture and the WEHI-3 myelomonocytic leukemia cell line have previously been shown to secrete myeloid colony-stimulating activity (CSA) spontaneously. We describe here other hematopoietic tumor cell lines in which CSA is either produced constitutively or inducible by

Cellular energy dependent agglutination of rat ascites tumor cells mediated by concanavalin A and Ricinus communis agglutinin.

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Effect of various metabolic inhibitors on the agglutination of rat ascites tumor cells mediated by concanavalin A and Ricinus communis agglutinin was studied using a quantitative assay method for agglutination in which turbidity of cell suspension is measured. Cell agglutination was inhibited by low

Effects of female sex steroids on concanavalin A-mediated agglutination of hepatocytes from nonregenerating and regenerating rat liver and hepatic tumor marker enzymes.

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Effect of treatment of female rats with an oral contraceptive agent (OCA), Ovulen-50, for 7 weeks on agglutination of hepatocytes with concanavalin A (con A) and activities of certain tumor marker enzymes were examined to find out if OCA treatment is related to preneoplastic or neoplastic processes.

Concanavalin A-peroxidase labeling in cervical exfoliative cytopathology. I. Labeling of normal squamous cells and the detection of cancer.

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The lectin binding capacity of the cell surface of normal flattened exfoliated epithelial cells of the uterine cervix was investigated looking for differences between specimens from normal and cancer patients. The method used was a modified concanavalin A-horseradish peroxidase (Con A-HRP) labeling

Concanavalin A receptors on the surfaces of human breast cancer cells in organ culture.

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The binding of concanavalin A (Con A) at the free apical membranes of surface tumor cells in human breast cancer explants grown in organ culture was studied cytochemically with horseradish peroxidase (HRP) as a marker. On the cell membranes in aldehyde-fixed explants or explants exposed to Con A at

Region-specific patterns of mucin reaction demonstrated by paradoxical concanavalin A-staining in normal colonic epithelium and in colorectal cancers induced in rats by 1,2-dimethylhydrazine.

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The histochemistry of mucin in normal large intestine and in experimental colorectal cancers induced in Wistar rats with 1,2-dimethylhydrazine was analyzed by modifications of the concanavalin A-horseradish peroxidase method (paradoxical concanavalin A-staining) and high-iron diamine-Alcian blue (pH

An increased level of the Concanavalin A-positive IgG in the serum of patients with gastric cancer as evaluated by a lectin enzyme-linked immunosorbent assay (LELISA).

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All human immunoglobulins are glycosylated. The changes in IgG glycosylation are associated with autoimmune disorders and pregnancy. Little is known about IgG glycosylation in patients with cancer. A lectin enzyme-linked immunosorbent assay (LELISA) based method was developed for measuring the

Alpha-fetoprotein-concanavalin A binding as a marker to discriminate between germ cell tumours and liver diseases.

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In order to differentiate whether slight alpha-fetoprotein (AFP) increases observed in any patient are due to germ cell tumours (GCT) or to liver diseases (including hepatotoxicity of chemotherapy), we measured the binding ratio of the AFP to concanavalin A (ConA). A total of 218 serum samples were

In vitro influence of Phaseolus vulgaris, Griffonia simplicifolia, concanavalin A, wheat germ, and peanut agglutinins on HCT-15, LoVo, and SW837 human colorectal cancer cell growth.

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OBJECTIVE Compared with normal colonic mucosa, lectin receptor expression is increased in hyperplastic and neoplastic tissues; some lectins have been shown to influence human colonic epithelial cell proliferation. The aim was to assess further the influence of five lectins (Phaseolus vulgaris (PNA),

Tandem lectin affinity chromatography monolithic columns with surface immobilised concanavalin A, wheat germ agglutinin and Ricinus communis agglutinin-I for capturing sub-glycoproteomics from breast cancer and disease-free human sera.

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In this study, a liquid-phase separation platform consisting of tandem lectin affinity chromatography was introduced for the selective capturing of sub-glycoproteomics that are affected in cancers, e.g. breast cancer. The platform is comprised of three monolithic columns with surface immobilised

Polyethylene glycol-modified concanavalin A as an effective agent to stimulate anti-tumor cytotoxicity.

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The jack bean lectin, concanavalin A (Con A), was modified with 2,4-bis[O-methoxypoly(ethylene glycol)]-6-chloro-s-triazine, activated PEG2, to form PEG-Con A. The immunoreactivity of PEG-Con A towards anti-Con A antibodies was reduced by increasing the degree of modification of amino groups in the

Induction of autophagy by concanavalin A and its application in anti-tumor therapy.

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Concanavalin A (Con A), a lectin from Jack bean seeds that, once bound to the mannose moiety on the cell membrane glycoprotein, is internalized preferentially to the mitochondria. A BNIP3-mediated mitochondria autophagy is then induced, and causes the tumor cells to undergo autophagic cell death.

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