Developmentally regulated glycosylation of dopamine transporter

Brain Res Dev Brain Res. 1994 Nov 18;83(1):53-8. doi: 10.1016/0165-3806(94)90178-3.


The dopamine transporter (DAT) in rat striatum was examined during postnatal development and aging after photolabeling with [125I]DEEP. The DAT-[125I]DEEP protein complex from adult rats (2 months) appeared as a broad diffuse band in SDS-PAGE gels with average apparent molecular mass of about 80,000 Da as previously found. However, the molecular mass was lower at birth (day 0) and at postnatal ages 4 and 14 days. In aged rats (104 weeks), the molecular mass was slightly higher than that found in young adults (60 days). In binding experiments with [3H]BTCP, there were age-related differences in Kd and Bmax with decreases in both Kd and Bmax found in aged rats. Treatment of photolabeled membranes with neuraminidase caused a reduction in DAT molecular mass, but age-related differences were maintained. Treatment with N-glycanase greatly reduced or eliminated the age-related differences. Several DAT peptide-specific polyclonal antibodies immunoprecipitated DAT-[125I]DEEP protein complex at different developmental ages. Taken together, these results suggest differential glycosylation of rat DAT occurs during postnatal development and aging; the increase is due to increases in the N-linked sugars rather than changes in either sialic acid content or the polypeptide.

MeSH terms

  • Aging / metabolism*
  • Amino Acid Sequence
  • Animals
  • Azides / metabolism
  • Carrier Proteins / chemistry
  • Carrier Proteins / metabolism*
  • Cell Membrane / metabolism
  • Cell Membrane / ultrastructure
  • Dopamine / metabolism
  • Dopamine Agonists / metabolism
  • Dopamine Plasma Membrane Transport Proteins
  • Female
  • Glycosylation
  • Kinetics
  • Male
  • Membrane Glycoproteins*
  • Membrane Transport Proteins*
  • Molecular Sequence Data
  • Nerve Tissue Proteins*
  • Phencyclidine / analogs & derivatives
  • Phencyclidine / metabolism
  • Piperazines / metabolism
  • Pregnancy
  • Protein Processing, Post-Translational*
  • Protein Structure, Secondary
  • Rats
  • Rats, Sprague-Dawley
  • Sialic Acids / analysis


  • Azides
  • Carrier Proteins
  • Dopamine Agonists
  • Dopamine Plasma Membrane Transport Proteins
  • Membrane Glycoproteins
  • Membrane Transport Proteins
  • Nerve Tissue Proteins
  • Piperazines
  • Sialic Acids
  • Slc6a3 protein, rat
  • 1-(1-(2-benzo(b)thienyl)cyclohexyl)piperidine
  • 1-(2-(diphenylmethoxy)ethyl)-4-(2-(4-azido-3-iodophenyl)ethyl)piperazine
  • Phencyclidine
  • Dopamine