Host-defense and trefoil factor family peptides in skin secretions of the Mawa clawed frog Xenopus boumbaensis (Pipidae).

Abstract

Peptidomic analysis of norepinephrine-stimulated skin secretions from the octoploid Mawa clawed frog Xenopus boumbaensis Loumont, 1983 led to the identification and characterization of 15 host-defense peptides belonging to the magainin (two peptides), peptide glycine-leucine-amide (PGLa; three peptides), xenopsin precursor fragment (XPF; three peptides), caerulein precursor fragment (CPF; two peptides), and caerulein precursor fragment-related peptide (CPF-RP; five peptides) families. In addition, caerulein and three peptides with structural similarity to the trefoil factor family (TFF) peptides, xP2 and xP4 from Xenopus laevis were also present in the secretions. Consistent with data from comparisons of the nucleotides sequence of mitochondrial and nuclear genes, the primary structures of the peptides suggest a close phylogenetic relationship between X. boumbaensis and the octoploid frogs Xenopus amieti and Xenopus andrei. As the three species occupy disjunct ranges within Cameroon, it is suggested that they diverged from a common ancestor by allopatric speciation.

• Authors: J Michael Conlon, Milena Mechkarska, Jolanta Kolodziejek, Jérôme Leprince, Laurent Coquet, Thierry Jouenne, Hubert Vaudry, Norbert Nowotny, Jay D King
• Journal: Peptides (Peptides) Vol. 72 Pg. 44-9 (Oct 2015) ISSN: 1873-5169 [Electronic] United States
• PMID: 25849343 (Publication Type: Journal Article)
• Copyright: Copyright © 2015 Elsevier Inc. All rights reserved.

Chemical References

• Amphibian Proteins
• Peptides
• Trefoil Factor-2

Topics

• Amphibian Proteins (chemistry, genetics, metabolism)
• Animals
• Peptides (chemistry, genetics, metabolism)
• Skin (metabolism)
• Trefoil Factor-2
• Xenopus