Genomic organisation and functional expression of the gene encoding the human serotonin 5-HT2C receptor
| Autor: | C. Van Alebeek, Jan Klomp, Nico J. Stam, A. M. L. Van Delft, Wiebe Olijve, P. M. L. Vanderheyden, T. De Boer |
|---|---|
| Přispěvatelé: | Experimental Pharmacology, Molecular and Biochemical Pharmacology, Department of Bio-engineering Sciences |
| Rok vydání: | 1994 |
| Předmět: |
DNA
Complementary Molecular Sequence Data Restriction Mapping Biology Transfection Binding Competitive Hippocampus Polymerase Chain Reaction Antiparkinson Agents Exon Mice Gene expression Receptor Serotonin 5-HT2C Animals Humans Comparative Study 5-HT5A receptor GABBR2 Amino Acid Sequence RNA Messenger GABBR1 Cloning Molecular Ergolines Receptor DNA Primers Pharmacology Base Sequence 3T3 Cells Exons Molecular biology Alpha-2B adrenergic receptor 5-HT2C receptor Blotting Southern Gene Expression Regulation Receptors Serotonin Type C Phospholipases |
| Zdroj: | European journal of pharmacology. 269(3) |
| ISSN: | 0014-2999 |
| Popis: | The 5-HT 2C receptor gene is unique among the members of the 5-HT receptor family by virtue of its genomic organisation. The human 5-HT 2C receptor gene, unlike many other genes for guanine nucleotide binding (G)-proteins, contains three introns which interrupt the coding sequence into four exons. The first two introns are at equivalent positions as compared to the intervening sequences previously found in the 5-HT 2(A) receptor gene, suggesting a close evolutionary relationship between both genes. Southern blot analysis shows that the 5-HT 2C receptor gene is a single copy gene. Furthermore, we report the functional expression of a complementary DNA for the 5-HT 2C receptor, cloned from hippocampal RNA. Membranes prepared from NIH 3T3 cells stably expressing the 5-HT 2C receptor cDNA, displayed a single population of high affinity sites for the antagonist [ 3 H]mesulergine ( K d = 2.9 ± 0.4 nM, B max = 44.3 ± 7.2 pmol/mg protein) as well as for [ 3 H]5-HT ( K d = 9.9 ± 0.7 nM, B max = 13.6 ± 1.0 pmol/mg protein). Displacement of [ 3 H]mesulergine and [ 3 H]5HT binding by ligands indicated a pharmacological similarity of these binding sites with porcine and rat choroid plexus 5-HT 2C receptors. Furthermore, activation of the 5-HT 2C receptor with 5-HT results in an increased phospholipase C activity. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|