| Autor: |
Torfs H; Laboratory for Developmental Physiology and Molecular Biology, Zoological Institute K.U. Leuven, Naamsestraat 59, Belgium., Akerman KE, Nachman RJ, Oonk HB, Detheux M, Poels J, Loy TV, Loof AD, Meloen RH, Vassart G, Parmentier M, Broeck JV |
| Jazyk: |
angličtina |
| Zdroj: |
Peptides [Peptides] 2002 Nov; Vol. 23 (11), pp. 1999-2005. |
| DOI: |
10.1016/s0196-9781(02)00187-0 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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