ATP and GTP as alternative energy sources for vinblastine transport by P-170 in KB-V1 plasma membrane vesicles

FEBS Lett. 1992 Jun 15;304(2-3):256-60. doi: 10.1016/0014-5793(92)80632-q.

Abstract

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.

MeSH terms

  • ATP Binding Cassette Transporter, Subfamily B, Member 1
  • Adenosine Triphosphate / metabolism*
  • Animals
  • Biological Transport, Active
  • Cell Membrane / metabolism*
  • Drug Resistance / physiology
  • Guanosine Triphosphate / metabolism*
  • Guinea Pigs
  • Humans
  • Infant
  • Membrane Glycoproteins / metabolism*
  • Nucleotides / metabolism
  • Substrate Specificity
  • Tumor Cells, Cultured
  • Vinblastine / metabolism*

Substances

  • ATP Binding Cassette Transporter, Subfamily B, Member 1
  • Membrane Glycoproteins
  • Nucleotides
  • Vinblastine
  • Guanosine Triphosphate
  • Adenosine Triphosphate