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.
Lelong
I H
IH
Laboratory of Cell Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.
Padmanabhan
R
R
Lovelace
E
E
Pastan
I
I
Gottesman
M M
MM
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