Bombinakinin-GAP
(Bombinakinin M gene associated peptide)
A New Obesity Peptide
Bombinakinin M gene associated peptide,
a novel bioactive peptide from skin secretions of the
toad Bombina maxima
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.
Lai R, Liu H, Lee WH, Zhang Y. Peptides 2003 Feb;24(2):199-204
A novel bradykinin-related peptide from skin
secretions of toad Bombina maxima and its precursor
containing six identical copies of the final product
Amphibian skin contains rich bradykinin-related peptides,
but the mode of biosynthesis of these peptides is unknown.
In the present study, a novel bradykinin-related peptide,
termed bombinakinin M, was purified from skin secretions
of the Chinese red belly toad Bombina maxima. Its primary
sequence was established as DLPKINRKGPRPPGFSPFR that
comprises bradykinin extended from its N-terminus by
a 10-residue segment DLPKINRKGP. The cDNA structure
of bombinakinin M was found to contain a coding region
of 624 nucleotides. The encoded precursor of bombinakinin
M is composed of a signal peptide, an acidic peptide,
six 100% identical copies of a 28-amino-acid peptide
unit including bombinakinin M plus a spacer peptide.
The sequence of bombinakinin M is preceded by a single
basic residue (arginine), which represents the site
of cleavage for releasing of mature bombinakinin M.
This is the first cDNA cloning of bradykinin-related
peptides from amphibian skin. The unique cDNA structure
encoding bombinakinin M suggests that the generation
modes of bradykinin-related peptides in amphibian skin
and in mammalian blood system are different.
Lai R, Liu H, Hui Lee W, Zhang Y. Biochem Biophys Res
Commun 2001 Aug 17;286(2):259-63
