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Side 1 fra 43 resultater
Usefulness of abrin as a positive control for the human tumor clonogenic assay.
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A series of approaches were tested in order to develop a simple technique for introducing a routine positive control into the Human Tumor Clonogenic Assay. Of the various techniques tested, the best proved to be the addition of the toxic plant lectin abrin to the culture system. When added to the
Molecular and biological properties of an abrin A chain immunotoxin designed for therapy of human small cell lung cancer.
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An immunotoxin (IT) comprising abrin A chain attached to the mouse monoclonal antibody SWA11, recognising a cell surface antigen highly associated with human small cell lung cancer (SCLC), was synthesised using a hindered disulphide crosslinker, N-succinimidyl 3-(2-pyridyldithio) butyrate (SPDB),
Comparison of two anti-Thy 1.1-abrin A-chain immunotoxins prepared with different cross-linking agents: antitumor effects, in vivo fate, and tumor cell mutants.
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The A-chain of the plant toxin abrin was covalently linked to monoclonal anti-Thy 1.1 antibody (OX7) with the use of either N-succinimidyl-3-(2-pyridyldithio)propionate (SPDP) or 2-iminothiolane hydrochloride (2IT). The SPDP reagent generates a linkage containing a disulfide bond and an amide bond,
Induction of antitumor immunity by tumor cells treated with abrin.
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Abrin is known as a cytotoxic lectin. Immunization with Meth-A tumor cells which were treated in vitro with abrin induced a strong antitumor immunity in syngeneic BALB/c mice. The immunizing effect was stronger than that produced by an irradiated Meth-A tumor cell vaccine. Studies on the mechanisms
Antitumour effect of abrin on transplanted tumours in mice.
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Abrin, a galactose specific lectin was purified using sepharose 4B affinity column from seeds of Abrus precatorius. It exhibited antitumour activity in mice when used at a sublethal dose of 7.5 micrograms/kg every alternate day for 10 days. Both intralesional and intraperiloneal (i.p.)
The mechanism of the anti-cancer activities of abrin and ricin.
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Two phytotoxic anti-tumor proteins: ricin and abrin. Isolation, crystallization, and preliminary x-ray study.
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[Study on anti-cancer activity of abrin: effects of abrin on leukocyte and lymphocyte in peripheral blood of rats (author's transl)].
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Abrin and ricin: new anti-tumour substances.
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Nude rat models for human tumor metastasis to CNS. Procedures for intracarotid delivery of cancer cells and drugs.
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Models for hematogenous spread of human cancer to the central nervous system (CNS) were established by injecting human tumor cells into the internal carotid artery of nude rats. With 4 out of 10 cell lines, belonging to four different tumor types, metastases developed in all injected animals. Tumor
Delivery of ricin and abrin A-chains to human carcinoma cells in culture following covalent linkage to monoclonal antibody LICR-LOND-Fib 75.
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With the object of generating specific cytotoxic agents, we have prepared covalent conjugates of the A-chains of ricin and of abrin with monoclonal antibody LICR-LOND-Fib 75 and investigated their toxicity toward a human tumor cell line in culture. Both conjugates proved to be potent cytotoxins
Treatment of micrometastases from Lewis lung carcinoma with abrin and cyclophosphamide, given singly and in combination.
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The effect of the plant toxin abrin and of cyclophosphamide given as adjuvant chemotherapy after irradiation of the primary tumor was studied in mice bearing intramuscularly growing Lewis lung carcinoma. The chemotherapy was given immediately after irradiation performed 9 days after inoculation of
Antibody formation against the cytotoxic proteins abrin and ricin in humans and mice.
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Antibody formation may limit the therapeutic use of cancerostatic proteins. To study the significance of antibody formation against abrin and ricin, highly sensitive ELISA procedures for determination of anti-abrin and anti-ricin were developed. In mice treated weekly with therapeutic doses of
Involvement of prohibitin upregulation in abrin-triggered apoptosis.
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Abrin (ABR), a protein purified from the seeds of Abrus precatorius, induces apoptosis in various types of cancer cells. However, the detailed mechanism remains largely uncharacterized. By using a cDNA microarray platform, we determined that prohibitin (PHB), a tumor suppressor protein, is
Radioimmunoassays of abrin and ricin in blood.
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Radioimmunoassays for abrin and ricin are described. There is little cross-reactivity between the two toxins. The procedures described are capable of determining blood concentrations down to 50-100 pg/ml, permitting identification of abrin and ricin poisoning and monitoring of the blood
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