![]() Experientia 38:679–680įlucher BE, Lenglachner-Bachinger C, Pohlhammer K, Adam H, Mollay C (1986) Skin peptides in Xenopus laevis: morphological requirements for precursor processing in developing and regenerating granular skin glands. Trends Pharmacol Sci 10:391–395įeurle GE, Bacá I, Knauf W Schwab A, Araki T, Carraway R (1982) Xenopsin stimulates exocrine pancreatic secretion in the dog. J Cell Biol 64:724–733Įrspamer V, Melchiorri P (1980) Active polypeptides: From amphibian skin to gastrointestinal tract and brain of mammals. Endocrinology 110:1094–1101ĭockray GJ, Hopkins CR (1975) Caerulein secretion by dermal glands in Xenopus laevis. Br Med Bull 38:239–245Ĭarraway RE, Ruane SE, Feurle GE, Taylor S (1982) Amphibian neurotensin (NT) is not xenopsin (XP): dual presence of NT-like and XP-like peptides in various Amphibia. Annu Rev Biochem 59:395–414īrown DR, Miller RJ (1982) Neurotensin. Pharmacol Biochem Behav 30:957–959īevins CL, Zasloff MA (1990) Peptides from frog skin. Yakugaku Zasshi 99:466–470īarthalmus GT, Zielinski WJ (1988) Xenopus skin mucus induces oral dyskinesias that promote escape from snakes. Chem Pharm Bull (Tokyo) 23:3132–3140Īraki K, Tachibana S, Kato Y, Tajima T (1979) Comparative studies of xenopsin and neurotensin on some biological activities. Chem Pharm Bull (Tokyo) 21:2801–2804Īraki K, Tachibana S, Uchiyama M, Nakajima T, Yasuhara T (1975) Isolation and structure of a new active peptide xenopsin on rat stomach strip and some biogenic amines in the skin of Xenopus laevis. In contrast, the observation that certain cells of the duodenum and large intestine display only one peptide immunoreactivity suggests an alternative phenomenon, possibly involving selective peptide accumulation or expression of a different gene.Īraki K, Tachibana S, Uchiyama M, Nakajima T, Yasuhara T (1973) Isolation and structure of a new active peptide “xenopsin” on the smooth muscle, especially on a strip of fundus from a rat stomach from the skin of Xenopus laevis. The immunochemical co-localization of the two peptides in specific cells of the skin, lower esophagus and stomach suggests that the same gene is expressed in each of these cells, and that the precursor molecule undergoes similar post-translational processing. However, only Xp-like immunoreactivity, not XPF-like immunoreactivity, was detected in tall, thin cells of the duodenum and in club-shaped cells of the large intestine. We report here that Xp-like and XPF-like immuno-reactivities co-exist in the granular glands of the skin and specific granular cells in the lower esophagus and stomach. The present immunohistochemical study was undertaken to determine the specific cellular localization of these two peptides in the skin and also in the gastrointestinal tract of adult Xenopus. The data indicate, therefore, that nonfunctionalization (gene deletion) has been the most common fate of duplicated antimicrobial peptide genes following polyploidization events in the Silurana and Xenopus lineages.Xenopsin (Xp) and xenopsin precursor fragment (XPF) are bioactive peptides derived from a single precursor molecule both were isolated previously from extracts of Xenopus laevis skin. borealis, and five from the tetraploid frog X. tropicalis, nine from the tetraploid frog X. Under the same experimental conditions, seven orthologous antimicrobial peptides were previously isolated from the diploid frog S. andrei components comprised two peptides from the magainin family, (magainin-AN1 and -AN2), two from the XPF family (XPF-AN1 and -AN2), two from the PGLa family(PGLa-AN1 and -AN2), and one caerulein-precursor fragment (CPF-AN1).The primary structures of these peptides indicate a close phylogenetic relationship between X. The CPF peptides showed potent, broad-spectrum antimicrobial activity. paratropicalis components comprised three peptides belonging to the caerulein-precursor fragment family (CPF-SP1, -SP2 and -SP3), two peptides from the xenopsin-precursor fragment family (XPF-SP1 and -SP2), and one peptide orthologous to peptide glycine-leucine-amide (PGLa-SP1). Structural characterization demonstrated that the S. andrei led to identification of multiple peptides with growth-inhibitory activity against Escherichia coli and Staphylococcus aureus. Peptidomic analysis of norepinephrine-stimulated skin secretions of S. paratropicalis and a second polyploidization within the Xenopus lineage has produced the octoploid frog X. ![]() A putative genome duplication event within the Silurana lineage has given rise to the tetraploid frog S. ![]()
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