Abstract
Cancer patients treated with one anticancer agent often develop resistance to a broad spectrum of chemotherapeutic agents. This type of multiple drug resistance (MDR) is often accompanied by a decrease in drug accumulation and an increase in expression of a 170,000-Da plasma membrane glycoprotein (P-170) that can effectively pump various anticancer agents out of cytoplasm. A panel of 12 IgG1, IgG2a, or IgG2b monoclonal antibodies was generated against the extracellular portion of P-glycoprotein by immunizing mice with a human MDR1 gene-transfected BA3T3 fibroblast line. We have characterized two of the anti-P-glycoprotein monoclonal antibodies, 15D3 and 17F9, in some detail. Both antibodies immunoprecipitate a 170- to 180-kDa protein from MDR cells, but do not block binding of the known anti-P-glycoprotein antibody MRK16, suggesting that 15D3 and 17F9 bind to a different epitope on the extracellular domain of P-glycoprotein than MRK16. Scatchard analysis revealed that 15D3 and 17F9 had association constants of 1.3 and 1.1 x 10(8) M-1, respectively. 15D3 and 17F9 had little effect on MDR cell growth except for a minor inhibition of KB-V1 cells when the cells were incubated in the presence of vinblastine. Neither antibody inhibit...Continue Reading
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