TY - JOUR
T1 - Kassinakinin S: A novel histamine-releasing heptadecapeptide from frog (Kassina senegalensis) skin secretion
AU - Chen, Tianbao
AU - Reid, Cherith N.
AU - Walker, Brian
AU - Zhou, Mei
AU - Shaw, Chris
PY - 2005/11/18
Y1 - 2005/11/18
N2 - 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[5][0]=6 µM; maximal release = 25 µM) 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.
AB - 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[5][0]=6 µM; maximal release = 25 µM) 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.
UR - http://www.scopus.com/inward/record.url?scp=26444433270&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2005.09.072
DO - 10.1016/j.bbrc.2005.09.072
M3 - Article
VL - 337
SP - 474
EP - 480
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -