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

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

B Dean 1, A J McAdam 1, S Sundram 1, G Pavey 1, L C Harrison 1, D L Copolov 1
PMCID: PMC1133121  PMID: 1417789

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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