Next Article in Journal
Ochratoxin A-Induced Hepatotoxicity through Phase I and Phase II Reactions Regulated by AhR in Liver Cells
Next Article in Special Issue
The Dual α-Amidation System in Scorpion Venom Glands
Previous Article in Journal
Potential Therapeutic Applications of Bee Venom on Skin Disease and Its Mechanisms: A Literature Review
Article Menu
Issue 7 (July) cover image

Export Article

Open AccessArticle

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

1
Natural Drug Discovery Group, School of Pharmacy, Queen’s University Belfast, Belfast BT9 7BL, Northern Ireland, UK
2
School of Government, Peking University, No 114, The Leo KoGuan Building, Beijing 100871, China
*
Authors to whom correspondence should be addressed.
These authors contributed equally to this work.
Toxins 2019, 11(7), 376; https://doi.org/10.3390/toxins11070376
Received: 26 May 2019 / Revised: 25 June 2019 / Accepted: 25 June 2019 / Published: 28 June 2019
  |  
PDF [2218 KB, uploaded 28 June 2019]
  |  

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. View Full-Text
Keywords: bradykinin-related peptide (BRP); RVA-Thr6-BK; site-substitution variant; agonist; antagonist; myotropic actions bradykinin-related peptide (BRP); RVA-Thr6-BK; site-substitution variant; agonist; antagonist; myotropic actions
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).
SciFeed

Share & Cite This Article

MDPI and ACS Style

Wu, Y.; Shi, D.; Chen, X.; Wang, L.; Ying, Y.; Ma, C.; Xi, X.; Zhou, M.; Chen, T.; Shaw, C. A Novel Bradykinin-Related Peptide, RVA-Thr6-BK, from the Skin Secretion of the Hejiang Frog; Ordorrana hejiangensis: Effects of Mammalian Isolated Smooth Muscle. Toxins 2019, 11, 376.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Toxins EISSN 2072-6651 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top