Three kinds of currents in the canine betaine-GABA transporter BGT-1 expressed in Xenopus laevis oocytes

Biochim Biophys Acta. 2001 Apr 23;1538(2-3):172-80. doi: 10.1016/s0167-4889(00)00144-0.

Abstract

The cloned canine betaine-GABA cotransporter BGT-1 has been heterologously expressed in Xenopus laevis oocytes in order to characterize its electrophysiological properties. Voltage-clamp experiments on transfected oocytes reveal the presence of three types of membrane current which are absent in non-injected oocytes: (i) an organic substrate-independent current (uncoupled current); (ii) a transport-associated current, seen upon addition of betaine or GABA; (iii) presteady-state currents induced by voltage changes. The three kinds of current are analogous to those reported in structurally similar cotransporters. The transport-associated current is strictly dependent on the presence of Na(+). The good correlation between the amount of charge underlying the presteady-state currents and the transport-associated current indicates that both processes are due to the activity of the transporter.

MeSH terms

  • Animals
  • Betaine / metabolism*
  • Carrier Proteins / biosynthesis
  • Carrier Proteins / chemistry*
  • Carrier Proteins / genetics
  • Cations, Monovalent
  • Dogs
  • GABA Plasma Membrane Transport Proteins
  • Membrane Potentials
  • Oocytes / metabolism
  • Patch-Clamp Techniques
  • Transfection
  • Xenopus laevis
  • gamma-Aminobutyric Acid / metabolism

Substances

  • Carrier Proteins
  • Cations, Monovalent
  • GABA Plasma Membrane Transport Proteins
  • betaine plasma membrane transport proteins
  • Betaine
  • gamma-Aminobutyric Acid