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

Toxins

Daning Shi²  Yu Luo¹  Qiang Du²  Lei Wang²  Mei Zhou²  Jie Ma²  Renjie Li²  Tianbao Chen² 

[1] School of Medicine, Dentistry and Biomedical Sciences, Queen’s University, Belfast BT9 7BL, Northern Ireland, UK; E-Mail:;Natural Drug Discovery Group, School of Pharmacy, Queen’s University, Belfast BT9 7BL, Northern Ireland, UK; E-Mails:

关键词: amphibian;    skin secretion;    molecular cloning;    bradykinin;    smooth muscle;   

DOI  :  10.3390/toxins6102886

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2014 by the authors; licensee MDPI, Basel, Switzerland.