A novel frog skin peptide containing function to induce muscle relaxation

Biochimie. 2012 Dec;94(12):2508-13. doi: 10.1016/j.biochi.2012.06.029. Epub 2012 Jul 4.

Abstract

A novel bioactive peptide (polypedarelaxin 1) was identified from the skin secretions of the tree frog, Polypedates pingbianensis. Polypedarelaxin 1 is composed of 21 amino acid residues with a sequence of QGGLLGKVSNLANDALGILPI. Its primary structure was further confirmed by cDNA cloning and mass spectrometry analysis. Polypedarelaxin 1 was found to elicit concentration-dependent relaxation effects on isolated rat ileum. It has no antimicrobial and serine protease inhibitory activities. BLAST search revealed that polypedarelaxin 1 did not show similarity to known proteins or peptides. Especially, polypedarelaxin 1 do not contain conserved structural motifs of other amphibian myotropic peptides, such as bradykinins, bombesins, cholecystokinin (CCK), and tachykinins, indicating that polypedarelaxin 1 belongs to a novel family of amphibian myotropic peptide.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amphibian Proteins / genetics
  • Amphibian Proteins / isolation & purification
  • Amphibian Proteins / pharmacology*
  • Animals
  • Anura / genetics
  • Anura / metabolism*
  • Base Sequence
  • Cloning, Molecular
  • DNA, Complementary / chemistry
  • DNA, Complementary / genetics
  • Dose-Response Relationship, Drug
  • Female
  • Ileum / drug effects
  • Ileum / physiology
  • In Vitro Techniques
  • Male
  • Molecular Sequence Data
  • Muscle Relaxation / drug effects*
  • Peptides / genetics
  • Peptides / isolation & purification
  • Peptides / pharmacology*
  • Rats
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid
  • Skin / metabolism*

Substances

  • Amphibian Proteins
  • DNA, Complementary
  • Peptides
  • polypedarelaxin 1, Polypedates pingbianensis