Abstract
Xenin is a regulatory peptide first isolated from the human gastric mucosa. Using an open-access protein database MEDLINE (33 million molecules; 11 billion amino acid residues) and our original computer program, we conducted a search for the xenin motifs in the primary structure of proteins across almost the entire taxonomic range of evolution. Motifs with 40% homology to human xenin are already present in prokaryotes. Homology reaches 84–96% in single-cell algae and plants, becoming complete since bony fishes. We suppose that this regulatory peptide is more ancient and significant than is usually thought.
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References
Feurle GE, Hamscher G, Kusiek R, Meyer HE, Metzger JW (1992) Identification of xenin, a xenopsin-related peptide, in the human gastric mucosa and its effect on exocrine pancreatic secretion. J Biol Chem 267:22305–22309
Feurle GE (1998) Xenin—a review. Peptides 19:609–615
Mazella J, Béraud-Dufour S, Devader C, Massa F, Coppola T (2012) Neurotensin and its receptors in the control of glucose homeostasis. Front Endocrinol (Lausanne) 3:143
Hamscher G, Meyer HE, Feurle GE (1996) Identification of proxenin as a precursor of the peptide xenin with sequence homology to yeast and mammalian coat protein alpha. Peptides 17:889–893
Maryanovich AT (2014) Foundations of peptide regulation of the physiological functions: blood-brain barrier and evolution of viscera-to-brain communications. Mechinkov Northwestern State Medical University Press, St. Petersburg
Mar’yanovich AT (2014) Early stages of phylogenesis of peptide regulation. J Evol Biochem Physiol 50:460–471
Hedges SB, Dudley J, Kumar S (2006) TimeTree a public knowledge-base of divergence times among organisms. Bioinformatics 22:2971–2972
Hedges SB, Kumar S (2009) The timetree of life. Oxford University Press, New York
Kim ER, Mizuno TM (2010) Role of neurotensin receptor 1 in the regulation of food intake by neuromedinsand neuromedin-related peptides. Neurosci Lett 468:64–67
Collier E, Watkinson A, Cleland CF, Roth J (1987) Partial purification and characterization of an insulin-like material from spinach and Lemna gibba G3. J Biol Chem 262:6238–6247
Chow VT, Sakharkar MK, Lim DP, Yeo WM (2001) Phylogenetic relationships of the seven coat protein subunits of the coatomer complex, and comparative sequence analysis of murine xenin and proxenin. Biochem Genet 39(5–6):201–211
Martin CM, Parthsarathy V, Hasib A, Ng MT, McClean S, Flatt PR, Gault VA, Irwin N (2016) Biological activity and antidiabetic potential of c-terminal octapeptide fragments of the gut-derived hormone xenin. PLoS ONE 11(3):e0152818. https://doi.org/10.1371/journal.pone.0152818
Taylor AI, Irwin N, McKillop AM, Patterson S, Flatt PR, Gault VA (2010) Evaluation of the degradation and metabolic effects of the gut peptide xenin on insulin secretion, glycaemic control and satiety. J Endocrinol 207(1):87–93. https://doi.org/10.1677/JOE-10-0085
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This work was not supported by any fund or organization. It is an authors’ initiative project funded exclusively from their personal sources.
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Maryanovich, A.T., Kormilets, D.Y. & Polyanovsky, A.D. Xenin: the oldest after insulin?. Mol Biol Rep 45, 143–150 (2018). https://doi.org/10.1007/s11033-018-4147-2
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DOI: https://doi.org/10.1007/s11033-018-4147-2