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Molecular characterisation, expression and localisation of human neurokinin‐3 receptor
Author(s) -
Buell G.,
Schulz M.F.,
Arkinstall S.J.,
Maury K.,
Missotten M.,
Adami N.,
Talabot F.,
Kawashima E.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80107-r
Subject(s) - tachykinin receptor 1 , neurokinin a , biology , complementary dna , microbiology and biotechnology , gabbr1 , receptor , interleukin 21 receptor , enzyme linked receptor , exon , 5 ht5a receptor , peptide sequence , xenopus , gene , protease activated receptor 2 , biochemistry , substance p , neuropeptide
The complete amino acid sequence of the human neurokinin‐3 receptor was deduced by DNA sequence analysis of human genomic fragments. Comparison of the predicted primary structure with those for the human neurokinin receptors 1 and 2 shows a highly conserved pattern of seven hydrophobic regions with maximum divergence occuring at the amino‐ and carboxy‐termini. The position of intron‐exon junctions are identical to those in other reported neurokinin genes. Using a chimeric genomic‐cDNA gene, the human NK‐3 receptor was expressed in Xenopus laevis oocytes where it mediates membrane conductance changes in response to its agonist, neurokinin B. More significantly, expression of the gene in mammalian cells resulted in detection of receptor binding as well as neurokinin‐stimulated calcium mobilization and arachidonic acid release, all displaying the pharmacological characteristics expected of a neurokinin‐3 receptor, By using the polymerase chain reaction we have shown that mRNA for the human neurokinin‐3 receptor is expressed predominantly in the central nervous system.