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Isolation and structural characterisation of a novel 13-amino acid insulin-releasing peptide from the skin secretion of Agalychnis calcarifer

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Veröffentlicht/Copyright: 7. Juli 2005
Biological Chemistry
Aus der Zeitschrift Band 386 Heft 6

Abstract

We describe the isolation and characterisation of an insulinotropic peptide from the skin secretions of Agalychnis calcarifer frogs. Peptides in crude secretions obtained by mild electrical stimulation from the dorsal skin surface were purified by reversed-phase HPLC, yielding fractions in two zones with insulin-releasing activity (p<0.001). The peaks showing greatest in vitro insulin-releasing activity were subsequently purified to homogeneity, revealing a novel insulinotropic 13-amino-acid (1653.2 Da) peptide with the primary structure RRKPLFPLIPRPK (RK-13). A database search for RK-13 showed 53.8% similarity with the N-terminal region of proline-arginine-rich antimicrobial peptide (PR-39). Synthetic RK-13 stimulated insulin release in a dose-dependent, glucose-sensitive manner, exerting its effects through a cyclic AMP-protein kinase A pathway independent of pertussis toxin-sensitive G proteins. Unlike PR-39, RK-13 lacks antimicrobial effects on the growth of yeast, and Gram-positive and Gram-negative bacteria. Our data indicate that skin secretions of Agalychnis calcarifer frogs contain insulin-releasing peptides, including RK-13, which merit further investigation as insulin secretagogues.

Keywords: Agalychnis calcarifer; amphibian peptides; insulin secretion; insulinotropic peptide, RK-13
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Corresponding author

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Published Online: 2005-07-07
Published in Print: 2005-06-01

© Walter de Gruyter Berlin New York

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  3. The seven E. coli ribosomal RNA operon upstream regulatory regions differ in structure and transcription factor binding efficiencies
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  8. Assembly of natural and recombinant prion protein into fibrils
  9. Isolation and structural characterisation of a novel 13-amino acid insulin-releasing peptide from the skin secretion of Agalychnis calcarifer
  10. Insularinase A, a prothrombin activator from Bothrops insularis venom, is a metalloprotease derived from a gene encoding protease and disintegrin domains
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https://doi.org/10.1515/BC.2005.068
Schlagwörter für diesen Artikel
Agalychnis calcarifer; amphibian peptides; insulin secretion; insulinotropic peptide, RK-13

Artikel in diesem Heft

  1. A role for constitutive androstane receptor in the regulation of human intestinal MDR1 expression
  2. Molecular structure and transcriptional regulation by nuclear factor-κB of the mouse kinin B1 receptor gene
  3. The seven E. coli ribosomal RNA operon upstream regulatory regions differ in structure and transcription factor binding efficiencies
  4. Mapping of B-cell epitopes in E. coli asparaginase II, an enzyme used in leukemia treatment
  5. Characterisation of human histone H1x
  6. Biochemical characterization of a cinnamoyl-CoA reductase from wheat
  7. Kunitz-type Bauhinia bauhinioides inhibitors devoid of disulfide bridges: isolation of the cDNAs, heterologous expression and structural studies
  8. Assembly of natural and recombinant prion protein into fibrils
  9. Isolation and structural characterisation of a novel 13-amino acid insulin-releasing peptide from the skin secretion of Agalychnis calcarifer
  10. Insularinase A, a prothrombin activator from Bothrops insularis venom, is a metalloprotease derived from a gene encoding protease and disintegrin domains
  11. Evidence for a common regulation in the activation of a polyphenol oxidase by trypsin and sodium dodecyl sulfate
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