Primary Structure of the Human Platelet Serotonin Uptake Site: Identity with the Brain Serotonin Transporter
Article first published online: 5 OCT 2006
Journal of Neurochemistry
Volume 60, Issue 6, pages 2319–2322, June 1993
How to Cite
Lesch, K.-P., Wolozin, B. L., Murphy, D. L. and Riederer, P. (1993), Primary Structure of the Human Platelet Serotonin Uptake Site: Identity with the Brain Serotonin Transporter. Journal of Neurochemistry, 60: 2319–2322. doi: 10.1111/j.1471-4159.1993.tb03522.x
- Issue published online: 5 OCT 2006
- Article first published online: 5 OCT 2006
- Resubmitted manuscript received February 23, 1993; accepted February 23, 1993.
- Serotonin transporter;
- Primary structure;
Abstract: A cDNA encoding the human platelet serotonin (5-HT) uptake site was isolated and sequenced using the PCR. The cDNA represents a ˜3.1-kb mRNA transcript and contains an open reading frame encoding a hydrophobic polypeptide of 630 amino acids with 12 membrane-spanning segments, a calculated molecular mass of 70,320 Da, and an estimated isoelectrical point of 5.84. The human platelet 5-HT uptake site is identical with the human brain 5-HT transporter and ˜92% homologous to the rat protein. Hydropathicity analysis indicates 12 membrane-spanning segments with two putative glycosylation sites within the second extracellular loop. The human platelet 5-HT uptake site contains two intraplasmatic consensus phosphorylation sites for cyclic AMP-dependent protein kinase recognition located in the cytoplasmatic N-terminal region and three potential protein kinase C phosphorylation sites. The identity of the human platelet 5-HT uptake site and the brain 5-HT transporter indicates that both proteins are encoded by the same single-copy gene, which has been assigned to the human chromosome 17. Our findings are likely to facilitate molecular pharmacologic and genetic investigations of the 5-HT transporter in psychiatric disorders.