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Minimum biological domain of xenin-25 required to induce anion secretion in the rat ileum.
- Source :
-
Peptides [Peptides] 2022 Jan; Vol. 147, pp. 170680. Date of Electronic Publication: 2021 Oct 29. - Publication Year :
- 2022
-
Abstract
- Xenin-25 has a variety of physiological functions in the gastrointestinal tract, including ion transport and motility. Xenin-25 and neurotensin show sequence homology, especially near their C-terminal regions. The sequence similarity between xenin-25 and neurotensin indicates that the effects of xenin-25 is mediated by the neurotensin receptor but some biological actions of xenin-25 are independent. We have previously reported that xenin-25 modulates intestinal ion transport and colonic smooth muscle activity. However, minimal biological domain of xenin-25 to induce ion transport was not clear. To improve the mechanistic understanding of xenin-25 and to gain additional insights into the functions of xenin-25, the present study was designed to determine the minimal biological domain of xenin-25 required for ion transport in the rat ileum using various truncated xenin fragments and analogues in an Ussing chamber system. The present results demonstrate that the minimum biological domain of xenin-25 to induce Cl <superscript>-</superscript> /HCO <subscript>3</subscript> <superscript>-</superscript> secretion in the ileum contains the C-terminal pentapeptide. Furthermore, Arg at position 21 is important to retain the biological activity of xenin-25 and induces Cl <superscript>-</superscript> /HCO <subscript>3</subscript> <superscript>-</superscript> secretion in the rat ileum.<br /> (Copyright © 2021 The Author(s). Published by Elsevier Inc. All rights reserved.)
- Subjects :
- Animals
Ileum drug effects
Male
Neurotensin analogs & derivatives
Neurotensin genetics
Neurotensin pharmacology
Protein Domains
Pyrazoles pharmacology
Quinolines pharmacology
Rats, Sprague-Dawley
Receptors, Neurotensin antagonists & inhibitors
Rats
Anions metabolism
Ileum metabolism
Neurotensin metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1873-5169
- Volume :
- 147
- Database :
- MEDLINE
- Journal :
- Peptides
- Publication Type :
- Academic Journal
- Accession number :
- 34757144
- Full Text :
- https://doi.org/10.1016/j.peptides.2021.170680