Inhibition of a mouse hepatoma by the alkylating agent Trenimon linked to immunoglobulins

Trenimon was conjugated in active alkylating form to rabbit anti-mouse H6 hepatoma globulin (AHG) with retention of antibody activity. H6 hepatoma-inoculated mice were given various combinations of conjugates, free Trenimon, and unconjugated immunoglobulins in daily injections for 5 days. Linkage of...

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Veröffentlicht in:Cancer Immunology Immunotherapy 1982-01, Vol.13 (3), p.185-189
Hauptverfasser: Ghose, T, Guclu, A, Raman, R R, Blair, A H
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container_title Cancer Immunology Immunotherapy
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creator Ghose, T
Guclu, A
Raman, R R
Blair, A H
description Trenimon was conjugated in active alkylating form to rabbit anti-mouse H6 hepatoma globulin (AHG) with retention of antibody activity. H6 hepatoma-inoculated mice were given various combinations of conjugates, free Trenimon, and unconjugated immunoglobulins in daily injections for 5 days. Linkage of Trenimon to immunoglobulins reduced systemic toxicity of the drug, with comparative retention of its antitumor activity. The antitumor action of Trenimon was potentiated by AHG irrespective of whether the drug was directly linked to AHG or free AHG was administered along with Trenimon linked to normal rabbit globulin (NRG). In vitro, Trenimon bound to AHG was less inhibitory to hepatoma cells than free Trenimon, but more inhibitory than Trenimon-NRG conjugates. There was no significant endocytosis of conjugates by the hepatoma cells. This suggests that unlike free Trenimon, the target molecules of Trenimon-immunoglobulin conjugates are not intracellular DNA but are located on the surface of the hepatoma cells.
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H6 hepatoma-inoculated mice were given various combinations of conjugates, free Trenimon, and unconjugated immunoglobulins in daily injections for 5 days. Linkage of Trenimon to immunoglobulins reduced systemic toxicity of the drug, with comparative retention of its antitumor activity. The antitumor action of Trenimon was potentiated by AHG irrespective of whether the drug was directly linked to AHG or free AHG was administered along with Trenimon linked to normal rabbit globulin (NRG). In vitro, Trenimon bound to AHG was less inhibitory to hepatoma cells than free Trenimon, but more inhibitory than Trenimon-NRG conjugates. There was no significant endocytosis of conjugates by the hepatoma cells. This suggests that unlike free Trenimon, the target molecules of Trenimon-immunoglobulin conjugates are not intracellular DNA but are located on the surface of the hepatoma cells.</abstract><cop>Germany</cop><pub>Springer-Verlag</pub><pmid>6925984</pmid><doi>10.1007/BF00205386</doi><tpages>5</tpages></addata></record>
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source MEDLINE; Springer Nature - Complete Springer Journals; PubMed Central
subjects Alkylating Agents - administration & dosage
Animals
Antibodies, Neoplasm - immunology
Endocytosis
Female
hepatoma
immunoglobulins
Immunoglobulins - administration & dosage
immunotherapy
Liver Neoplasms, Experimental - drug therapy
Liver Neoplasms, Experimental - immunology
Mice
Mice, Inbred Strains
Neoplasm Transplantation
Original
Rabbits
triaziquone
Triaziquone - administration & dosage
title Inhibition of a mouse hepatoma by the alkylating agent Trenimon linked to immunoglobulins
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