Kassinakinin S: a novel histamine-releasing heptadecapeptide from frog (Kassina senegalensis) skin secretion.
Amphibian defensive skin secretions remain a largely untapped resource for the peptide biochemist with an interest in the identification, structural characterization, and precursor cDNA cloning of novel bioactive peptides. Here we report the isolation, structural characterization, functional profiling, and nucleotide sequence of precursor cDNA of a novel histamine-releasing heptadecapeptide, FIPVTLLALHKIKEKLN-amide, from the defensive skin secretion of the African running frog, Kassina senegalensis. This peptide was found to be a potent histamine secretagogue (EC(50) = 6 microM; maximal release = 25 microM) in a rat peritoneal mast cell model system and was accordingly named kassinakinin S. The open-reading frame of the cDNA encoding prepro-kassinakinin S was found to consist of 71 amino acid residues containing a single copy of kassinakinin S and its glycyl residue amide donor at the C-terminus. Kassinakinin S can thus be added to the growing list of amphibian skin bioactive peptide prototypes.
Chen
Tianbao
T
School of Pharmacy, Queen's University, Belfast, Northern Ireland, UK.
Reid
Cherith N
CN
Walker
Brian
B
Zhou
Mei
M
Shaw
Chris
C
D000595:Amino Acid Sequence; D000818:Animals; D001001:Anura; D001483:Base Sequence; D018076:DNA, Complementary / Q000032:analysis / Q000378:metabolism; D004305:Dose-Response Relationship, Drug; D006636:Histamine Release / Q000502:physiology*; D036341:Intercellular Signaling Peptides and Proteins; D008407:Mast Cells / Q000187:drug effects; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D010455:Peptides / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology; D010529:Peritoneal Cavity / Q000166:cytology; D017433:Protein Structure, Secondary; D051381:Rats; D012867:Skin / Q000737:chemistry* / Q000378:metabolism
D018076:DNA, Complementary; D036341:Intercellular Signaling Peptides and Proteins; D010455:Peptides; C506314:kassinakinin S