ATP and GTP as alternative energy sources for vinblastine transport by P-170 in KB-V1 plasma membrane vesicles.
Purified plasma membrane vesicles isolated from multidrug-resistant human KB-V1 cells accumulate [3H]vinblastine in an energy-dependent manner. The accumulation of [3H]vinblastine in the presence of ATP is a saturable process. ATP can be replaced by other purine nucleotide triphosphates, of which GTP is the most efficient.
Laboratory of Cell Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.
I H
IH
Lelong
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Padmanabhan
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Lovelace
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Pastan
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Gottesman
D020168:ATP Binding Cassette Transporter, Subfamily B, Member 1; D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D001693:Biological Transport, Active; D002462:Cell Membrane / Q000378:metabolism*; D004351:Drug Resistance / Q000502:physiology; D006160:Guanosine Triphosphate / Q000378:metabolism*; D006168:Guinea Pigs; D006801:Humans; D007223:Infant; D008562:Membrane Glycoproteins / Q000378:metabolism*; D009711:Nucleotides / Q000378:metabolism; D013379:Substrate Specificity; D014407:Tumor Cells, Cultured; D014747:Vinblastine / Q000378:metabolism*
D020168:ATP Binding Cassette Transporter, Subfamily B, Member 1; D008562:Membrane Glycoproteins; D009711:Nucleotides; D014747:Vinblastine; D006160:Guanosine Triphosphate; D000255:Adenosine Triphosphate