Bombinakinin M gene associated peptide, a novel bioactive peptide from skin secretions of the toad Bombina maxima

Peptides. 2003 Feb;24(2):199-204. doi: 10.1016/s0196-9781(03)00027-5.


A novel 28-amino acid peptide, termed bombinakinin-GAP, was purified and characterized from skin secretions of the toad Bombina maxima. Its primary structure was established as DMYEIKQYKTAHGRPPICAPGEQCPIWV-NH(2), in which two cysteines form a disulfide bond. A FASTA search of SWISS-PROT databank detected a 32% sequence identity between the sequences of the peptide and a segment of rat cocaine- and amphetamine-regulated transcript (CART). Intracerebroventricular (i.c.v.) administration of the peptide induced a significant decrease in food intake in rats, suggesting that it played a role in the control of feeding by brain. Analysis of its cDNA structure revealed that this peptide is coexpressed with bombinakinin M, a bradykinin-related peptide from the same toad. Bombinakinin-GAP appears to be the first example of a novel class of bioactive peptides from amphibian skin, which may be implicated in feeding behavior.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Anura / genetics*
  • Anura / metabolism
  • Base Sequence
  • Chromatography, High Pressure Liquid
  • Cloning, Molecular
  • DNA, Complementary / chemistry
  • DNA, Complementary / genetics
  • Dose-Response Relationship, Drug
  • Eating / drug effects
  • Injections, Intraventricular
  • Kinins / chemistry
  • Kinins / genetics*
  • Kinins / pharmacology
  • Male
  • Molecular Sequence Data
  • Nerve Tissue Proteins / genetics
  • Rats
  • Rats, Wistar
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid
  • Skin / metabolism*
  • Time Factors


  • DNA, Complementary
  • Kinins
  • Nerve Tissue Proteins
  • bombinakinin M gene associated peptide, Bombina maxima
  • cocaine- and amphetamine-regulated transcript protein

Associated data

  • GENBANK/AF515613