Isolation and Structural Characterisation of Herring Gull (Larus argentatus) Pancreatic Polypeptide

Barton, C.L.; Shaw, Christopher; Halton, D.W.; Thim, Lars

doi:10.1006/gcen.1994.1029

Cited by 7 publications

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“…This intriguing observation, rather than leading to a dubious speculation that, in some way, the frog skin BRP is a defence against passerine bird predation, suggests that the name, ornithokinin (avian bradykinin), given originally to the chicken ( Gallus gallus ) BRP (RPPGFTPLR), is not universally applicable across this taxon. In previous reports relating to the pancreatic polypeptide (PP) hormone [ 18 , 19 ], it was likewise found that the homologue present in passerine bird (crow) pancreas [ 20 ] significantly-differed from the archetypal avian PP originally isolated from chicken pancreas by the presence of an N -terminal Ala (A) residue and a Pro (P) residue at Position 34, rather than the Gly (G) residue at Position 1 and the His (H) residue at Position 34 found in chicken, goose ( Anser anser ; order Anseriformes), ostrich ( Struthio camelus ; Struthioniformes) and herring gull ( Larus argentatus ; order Charadriiformes) peptides [ 21 , 22 , 23 , 24 ]. It may be that the bioinformatic analysis of this frog skin BRP has revealed that in birds, there are at least two forms of BRP, similar to the findings of previous studies on their endogenous pancreatic polypeptides.…”

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confidence: 99%

A Novel Bradykinin-Related Dodecapeptide (RVALPPGFTPLR) from the Skin Secretion of the Fujian Large-Headed Frog (Limnonectes fujianensis) Exhibiting Unusual Structural and Functional Features

Shi

Luo

et al. 2014

Toxins

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Bradykinin-related peptides (BRPs) are significant components of the defensive skin secretions of many anuran amphibians, and these secretions represent the source of the most diverse spectrum of such peptides so far encountered in nature. Of the many families of bioactive peptides that have been identified from this source, the BRPs uniquely appear to represent homologues of counterparts that have specific distributions and receptor targets within discrete vertebrate taxa, ranging from fishes through mammals. Their broad spectra of actions, including pain and inflammation induction and smooth muscle effects, make these peptides ideal weapons in predator deterrence. Here, we describe a novel 12-mer BRP (RVALPPGFTPLR-RVAL-(L1, T6, L8)-bradykinin) from the skin secretion of the Fujian large-headed frog (Limnonectes fujianensis). The C-terminal 9 residues of this BRP (-LPPGFTPLR) exhibit three amino acid substitutions (L/R at Position 1, T/S at Position 6 and L/F at Position 8) when compared to canonical mammalian bradykinin (BK), but are identical to the kinin sequence present within the cloned kininogen-2 from the Chinese soft-shelled turtle (Pelodiscus sinensis) and differ from that encoded by kininogen-2 of the Tibetan ground tit (Pseudopodoces humilis) at just a single site (F/L at Position 8). These data would imply that the novel BRP is an amphibian defensive agent against predation by sympatric turtles and also that the primary structure of the avian BK, ornithokinin (RPPGFTPLR), is not invariant within this taxon. Synthetic RVAL-(L1, T6, L8)-bradykinin was found to be an antagonist of BK-induced rat tail artery smooth muscle relaxation acting via the B2-receptor.

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