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• W2743109543 abstract "Two monoclonal antibodies, 0C125 and OV-TL3, that are highly specific for ovarian cancer cells were compared in terms of their interaction with a particular ovarian cancer cell line (NIH:OVCAR-3). 0C125 recognized determinants on molecules with apparent molecular weights exceeding 200,000 dalton, while 0V-TL3 recognized determinants on molecules with apparent molecular weights of 20,000 and 40,000 dalton. When the antigens recognized by these two monoclonal antibodies were further examined, enzymatic studies revealed that both antigens are proteins, most likely glycoproteins. Cross inhibition experiments showed that the antibodies react with different epitopes on antigenic structures. The affinity constant of 0C125 was 0.9 x 10^ and was similar to that of 0V-TL3, which was 1.6 x K>9. The number of antigenic determinants per cell (NIH:0VCAR-3) was estimated to be 6.0 x 10*> for OC125 and 0.6 x 10 for 0V-TL3. Association of 0C125 was very slow (50% binding after 125 minutes), compared with that of 0V-TL3 (50% binding after 30 minutes), and dissociation rates for the two monoclonal antibodies also differed. OC125 dissociated with a Tl/2 of 125 minutes from fixed cells and a Tl/2 of 85 minutes from life cells, indicating that an active (shedding or modulation) process might be involved in its dissociation from life cells. OV-TL3 showed no significant difference in dissociation rates between life and fixed cells, although dissociation seemed to be biphasic, with Tl/2 of 60 and 300 minutes, indicating possible lowand high affinity binding sites. OC125 binding could be inhibited by serum or ascites samples from ovarian cancer patients whereas 0V-TL3 binding was not inhibited by either of these samples, suggesting that OC125 antigen is shed from ovarian cancer cells and is therefore found in the serum and ascites of ovarian cancer patients. The antibody uptake into human ovarian cancer xenografts in nude mice was more persistent for 0V-TL3 than for 0C125. OV-TL3 might be a more favorable candidate for immunotherapy or inmunoscintigraphy than OC125 because of a) the similar histological reactivity of 0C125 and 0V-TL3 with ovarian cancer, b) the lack of shedding of the 0V-TL3 antigen, c) a faster association rate of 0V-TL3 and d) the slower dissociation rate of 0V-TL3 compared to 0C125." @default.
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• W2743109543 date "1987-01-01" @default.
• W2743109543 modified "2023-09-27" @default.
• W2743109543 title "Monoclonal antibodies and cancer: studies on the use of monoclonal antibodies for imaging and therapy of cancer, with special emphasis on ovarian carcinoma" @default.
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