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Functional analysis of synthetic insectatachykinin analogs on recombinant neurokinin receptor expressing cell lines.

par Torfs, Herbert;Akerman, Karl E;Nachman, Ronald J;Oonk, Hendrica B;Detheux, Michel;Poels, Jeroen;Loy, Tom Van;Loof, Arnold De;Meloen, Rob H;Vassart, Gilbert ;Parmentier, Marc ;Broeck, Jozef Vanden
Référence Peptides, 23, 11, page (1999-2005)
Publication Publié, 2002-11

Article révisé par les pairs

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Résumé :

The activity of a series of synthetic tachykinin-like peptide analogs was studied by means of microscopic calcium imaging on recombinant neurokinin receptor expressing cell lines. A C-terminal pentapeptide (FTGMRa) is sufficient for activation of the stomoxytachykinin receptor (STKR) expressed in Schneider 2 cells. Replacement of amino acid residues at the position of the conserved phenylalanine (F) or arginine (R) residues by alanine (A) results in inactive peptides (when tested at 1microM), whereas A-replacements at other positions do not abolish the biological activity of the resulting insectatachykinin-like analogs. Calcium imaging was also employed to compare the activity of C-terminally substituted tachykinin analogs on three different neurokinin receptors. The results indicate that the major pharmacological and evolutionary difference between tachykinin-related agonists for insect (STKR) and human (NK1 and NK2) receptors resides in the C-terminal amino acid residues (R versus M). A single C-terminal amino acid change can turn an STKR-agonist into an NK-agonist and vice versa.