L-glutamine transport in native vesicles isolated from Ehrlich ascites tumor cell membranes

J Bioenerg Biomembr. 1991 Aug;23(4):689-97. doi: 10.1007/BF00785818.

Abstract

Native vesicles isolated from Ehrlich ascites tumor cells accumulate glutamine by means of Na(+)-dependent transport systems; thiocyanate seems to be the more effective anion. The apparent affinity constant for the process was 0.38 mM. The Arrhenius plot gave an apparent activation energy of 12.3 kJ/mol. The structural analogs of glutamine, acivicin (2.5 mM) and azaserine (2.5 mM), inhibited the net uptake by 67 and 70%, respectively. The sulfhydryl reagents mersalyl, PCMBS, NEM, and DTNB also inhibited net uptake, suggesting that sulfhydryl groups may be involved in the activity of the carrier protein. A strong inhibition was detected when the vesicles were incubated in the presence of alanine, cysteine, or serine; in addition, histidine, but not glutamate or leucine, had a negative effect on glutamine transport.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Biological Transport
  • Carcinoma, Ehrlich Tumor
  • Cell Membrane / metabolism*
  • Cell Membrane / ultrastructure
  • Glutamine / antagonists & inhibitors
  • Glutamine / metabolism*
  • Kinetics
  • Mice
  • Osmolar Concentration
  • Temperature
  • Tumor Cells, Cultured

Substances

  • Glutamine