Toxins (Jun 2019)

A Novel Bradykinin-Related Peptide, RVA-Thr<sup>6</sup>-BK, from the Skin Secretion of the Hejiang Frog; <i>Ordorrana hejiangensis</i>: 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

DOI
https://doi.org/10.3390/toxins11070376
Journal volume & issue
Vol. 11, no. 7
p. 376

Abstract

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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.

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