A Novel Bradykinin-Related Peptide, RVA-Thr6-BK, from the Skin Secretion of the Hejiang Frog; Ordorrana hejiangensis: Effects of Mammalian Isolated Smooth Muscle

Yue Wu, Daning Shi , Xiaoling Chen, Lei Wang, Yuan Ying, Chengbang Ma, Xinping Xi, Mei Zhou, Tianbao Chen, Chris Shaw

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Abstract

A novel naturally-occurring bradykinin-related peptide (BRP) with an N-terminal extension, named RVA-Thr6-Bradykinin (RVA-Thr6-BK), was here isolated and identified from the cutaneous secretion of Odorrana hejiangensis (O. hejiangensis). Thereafter, in order to evaluate the difference in myotropic actions, a leucine site-substitution variant from Amolops wuyiensis skin secretion, RVA-Leu1, Thr6-BK, was chemically synthesized. Myotropic studies indicated that single-site arginine (R) replacement by leucine (L) at position-4 from the N-terminus, altered the action of RVA-Thr6-BK from an agonist to an antagonist of BK actions on rat ileum smooth muscle. Additionally, both BK N-terminal extended derivatives (RVA-Thr6-BK and RVA-Leu1, Thr6-BK) exerted identical myotropic actions to BK, such as increasing the frequency of contraction, contracting and relaxing the rat uterus, bladder and artery preparations, respectively.
Original languageEnglish
Article number376
Number of pages10
JournalToxins
Volume11
Issue number7
DOIs
Publication statusPublished - 28 Jun 2019

Keywords

  • bradykinin-related peptide (BRP); RVA-Thr6-BK; site-substitution variant; agonist; antagonist; myotropic actions

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