L-glutamate transporter derived from mRNAs of primary glial cultures: expression in Xenopus laevis oocytes

Brain Res Mol Brain Res. 1992 Sep;15(1-2):167-70. doi: 10.1016/0169-328x(92)90166-9.

Abstract

A high-affinity sodium-dependent L-glutamate transporter was expressed in Xenopus oocytes after microinjection of poly(A)+ RNA from primary astrocyte cultures from rat brain cortex. mRNA-induced L-glutamate transport was saturable by substrate and shows kinetic features similar to those found in intact glial cell preparations. L-Glutamate accumulation was prevented by rising the external K+ concentration or by coincubation with L-, D-aspartate or D-glutamate. After fractionation by sucrose density gradient, the mRNA encoding for the expressed L-glutamate transporter from glial cells was found in fractions containing messages of 2.05-2.9 kilobases (kb) in length.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkaline Phosphatase / metabolism
  • Amino Acid Transport System X-AG
  • Animals
  • Cells, Cultured
  • Glycoproteins / biosynthesis
  • Glycoproteins / metabolism*
  • Kinetics
  • Neuroglia / metabolism*
  • Oocytes / metabolism*
  • Poly A / metabolism
  • RNA, Messenger / biosynthesis*
  • Rats
  • Rats, Wistar
  • Xenopus laevis

Substances

  • Amino Acid Transport System X-AG
  • Glycoproteins
  • RNA, Messenger
  • Poly A
  • Alkaline Phosphatase