The CPF peptides show potential for development into agents for the treatment of Type 2 diabetes. The mechanism of action of the CPF peptides involves, at least in part, membrane depolarization and an increase in intracellular Ca2+ concentration. No CPF peptide stimulated release of the cytosolic enzyme, lactate dehydrogenase from BRIN-BD11 cells at concentrations up to 3 μM indicating that the integrity of the plasma membrane had been preserved. In addition, CPF-SE1 (GFLGPLLKLGLKGVAKVIPHLIPSRQQ), previously isolated from skin secretions of the tetraploid frog Silurana epitropicalis, produced a significant (P < 0.05) increase in the rate of insulin release at 0.03 nM with a 514 ± 13% increase over basal rate at 3 μM. CPF-7 (GFGSFLGKALKAALKIGANALGGAPQQ) produced the maximum stimulation of insulin release (571 ± 30% of basal rate at 3 μM). CPF-1, CPF-3, CPF-5 and CPF-6 were the most potent producing a significant (P < 0.05) increase in the rate of insulin release at concentration of 0.03 nM. These peptides were purified to near homogeneity and structural characterization showed that they belong to the magainin (2 peptides), peptide glycine-leucine-amide (PGLa) (1 peptide), xenopsin precursor fragment (1 peptide), and caerulein precursor fragment (CPF) (6 peptides) families. 429-435 ISSN: 0300-9084 Subject: Xenopus laevis, calcium, frogs, insulin, lactate dehydrogenase, mechanism of action, noninsulin-dependent diabetes mellitus, peptides, plasma membrane, rats, tetraploidy Abstract: Peptidomic analysis of norepinephrine-stimulated skin secretions of the tetraploid clawed frog Xenopus laevis (Pipidae) led to the identification of 10 peptides with the ability to stimulate the release of insulin from the rat BRIN-BD11 clonal β cell line. Michael Conlon Source: Biochimie 2013 v.95 pp. All rights reserved.Caerulein precursor fragment (CPF) peptides from the skin secretions of Xenopus laevis and Silurana epitropicalis are potent insulin-releasing agents Author: Dinesh Srinivasan, Milena Mechkarska, Yasser H.A. amieti show potential for development into anti-infective agents for use against antibiotic-resistant gram-negative bacteria.Ĭopyright © 2011 Elsevier Inc. While some duplicated gene products retain high antimicrobial potency (subfunctionalization), the very low activity of others suggests that they may be evolving towards a new biological role (neofunctionalization). The data indicate, therefore, that nonfunctionalization (gene silencing) has been the most common fate of antimicrobial peptide genes following polyploidization. paratropicalis was not greater than that of S. Magainins were not identified in skin secretions of Silurana frogs and the multiplicity of the PGLa, CPF, and XPF peptides from S. However, the numbers of paralogs from the octoploid frogs were not significantly greater than the corresponding numbers from the tetraploid frogs. All Xenopus antimicrobial peptides may be classified in the magainin, peptide glycine-leucine-amide (PGLa), caerulein-precursor fragment (CPF), and xenopsin-precursor fragment (XPF) families. The peptide has been shown to enhance binding of agonists to A1 adenosine receptors (Daly et al, 1992 Moni et al, 1995). Similarly, components in skin secretions from the diploid frog Silurana tropicalis may be compared with those from the tetraploid frog Silurana paratropicalis. Adenoregulin ( GLWSKIKEVGKEAAKAAAKAAGKAALGAVSEAV) is a peptide isolated from skin secretions of the South-American frog Phyllomedusa bicolor (Daly et al, 1992). muelleri West", and Xenopus petersii may be compared with those from the octoploid frogs Xenopus amieti and X. Xenopsin (Xp) and xenopsin precursor frag- ment (XPF) are bioactive peptides derived from a single precursor molecule both were isolated previously from extracts of Xenopus laevis skin. The primary structures and distributions of host-defense peptides from the tetraploid frogs Xenopus borealis, Xenopus clivii, Xenopus laevis, Xenopus muelleri, "X. Allopolyploidization events within the Xenopodinae have given rise to tetraploid, octoploid, and dodecaploid species. African clawed frogs of the Xenopodinae (Xenopus+Silurana) constitute a well-defined system in which to study the evolutionary trajectory of duplicated genes and are a source of antimicrobial peptides with therapeutic potential. Structural characterization of the peptides demonstrated that they were orthologous to magainin-2 (1 peptide), peptide glycineleucine-amide, PGLa (2 peptides), caerulein-precursor fragments, CPF (4 peptides), and xenopsin-precursor fragments, XPF (2 peptides), previously isolated from Xenopus laevis and X.
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