In frog skin, tachykinins stimulate ion transport by interaction with NK1-like receptors. The structural requirements of the peptide are the presence of the C-terminal sequence Phe-X-Gly-Leu-Met-NH2 and at least one Pro residue in the N-terminal sequence. In this paper, we demonstrate that the C-terminal amino acid must be amidated but it can be different from Met, and that the sequence cannot be longer or shorter than 11-12 amino acids. Unexpectedly, Ranamargarin (14 amino acids, no Pro residue) increased the short circuit current value by 48 +/- 0.3%. On the basis of considerable experimental evidence, we suggest that Ranamargarin interacts with a receptor different from those of other tachykinins.
Differences between Ranamargarin and other tachykinins in the stimulation of ion transport in frog skin
LIPPE, Claudio;BELLANTUONO, VITO;CASSANO, Giuseppe;QUARANTA, Angelo;ARDIZZONE, Concetta
2001-01-01
Abstract
In frog skin, tachykinins stimulate ion transport by interaction with NK1-like receptors. The structural requirements of the peptide are the presence of the C-terminal sequence Phe-X-Gly-Leu-Met-NH2 and at least one Pro residue in the N-terminal sequence. In this paper, we demonstrate that the C-terminal amino acid must be amidated but it can be different from Met, and that the sequence cannot be longer or shorter than 11-12 amino acids. Unexpectedly, Ranamargarin (14 amino acids, no Pro residue) increased the short circuit current value by 48 +/- 0.3%. On the basis of considerable experimental evidence, we suggest that Ranamargarin interacts with a receptor different from those of other tachykinins.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
