Identification of a dopamine-binding protein on the membrane of the human platelet

Biochem J. 1992 Oct 1;287 ( Pt 1)(Pt 1):45-50. doi: 10.1042/bj2870045.

Abstract

The binding of [3H]dopamine to platelet membranes has been examined in an attempt to identify the putative dopamine-uptake mechanism of the platelet. [3H]Dopamine has been shown to bind to a 42,000 Da glycoprotein in platelet membrane with high affinity (Kd = 22.6 nM) and binding of [3H]dopamine was competed for by dopamine, molecules with catechol moieties, 5-hydroxytryptamine, GSH and ascorbic acid. Differences in pharmacological profile and molecular mass suggest that [3H]dopamine does not bind to a known receptor, a neuronal-type dopamine transporter or the platelet 5-hydroxytryptamine-uptake site. It is proposed that this novel binding site for dopamine, which has been purified 1000-fold from particulate platelet membrane, is likely to be a component of the dopamine-uptake mechanism of the human platelet.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biological Transport
  • Blood Platelets / metabolism*
  • Cell Membrane / metabolism
  • Humans
  • In Vitro Techniques
  • Platelet Membrane Glycoproteins / chemistry
  • Platelet Membrane Glycoproteins / metabolism*
  • Protein Binding
  • Receptors, Dopamine / physiology

Substances

  • Platelet Membrane Glycoproteins
  • Receptors, Dopamine