Increased [(3)H]tiagabine binding to GAT-1 in the cingulate cortex in schizophrenia

Neuropsychobiology. 2002;45(1):7-11. doi: 10.1159/000048666.

Abstract

Postmortem samples from individuals with schizophrenia (n = 13) and control subjects (n = 10) were investigated for binding of [(3)H]tiagabine to GABA transporter-1 GAT-1. The binding was analyzed in the cingulate cortex and the caudate nucleus. There were no differences in binding affinity between the groups in any of the investigated areas. The maximum number of binding sites (B(max)) was elevated in the schizophrenic cingulate cortex compared to controls (1,264 +/- 96 vs. 860 +/- 123 fmol/mg of protein). The B(max) in the caudate nucleus for schizophrenics (426 +/- 40 fmol/mg of protein) was the same as for controls (495 +/- 69 fmol/mg of protein). The increase in GAT-1 in schizophrenia could be explained by a modulatory upregulation in the cingulate cortex.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aged
  • Aged, 80 and over
  • Brain / metabolism
  • Carrier Proteins / drug effects*
  • Carrier Proteins / metabolism
  • Case-Control Studies
  • Caudate Nucleus / metabolism*
  • Chronic Disease
  • Female
  • GABA Agonists / pharmacology*
  • GABA Plasma Membrane Transport Proteins
  • Gyrus Cinguli / metabolism*
  • Humans
  • In Vitro Techniques
  • Male
  • Membrane Proteins / drug effects*
  • Membrane Proteins / metabolism
  • Membrane Transport Proteins*
  • Middle Aged
  • Neurotransmitter Uptake Inhibitors / pharmacology*
  • Nipecotic Acids / pharmacology*
  • Organic Anion Transporters*
  • Schizophrenia / metabolism*
  • Tiagabine
  • Up-Regulation
  • gamma-Aminobutyric Acid / metabolism

Substances

  • Carrier Proteins
  • GABA Agonists
  • GABA Plasma Membrane Transport Proteins
  • Membrane Proteins
  • Membrane Transport Proteins
  • Neurotransmitter Uptake Inhibitors
  • Nipecotic Acids
  • Organic Anion Transporters
  • SLC6A1 protein, human
  • gamma-Aminobutyric Acid
  • Tiagabine