Next Article in Journal
Structure, Evolution, and Functions of Bacterial Type III Toxin-Antitoxin Systems
Previous Article in Journal
BmP02 Atypically Delays Kv4.2 Inactivation: Implication for a Unique Interaction between Scorpion Toxin and Potassium Channel
Article Menu
Issue 10 (October) cover image

Export Article

Open AccessArticle
Toxins 2016, 8(10), 283; doi:10.3390/toxins8100283

Ex Vivo Smooth Muscle Pharmacological Effects of a Novel Bradykinin-Related Peptide, and Its Analogue, from Chinese Large Odorous Frog, Odorrana livida Skin Secretions

1
Natural Drug Discovery Group, School of Pharmacy, Queen’s University Belfast, Belfast BT9 7BL, Northern Ireland, UK
2
School of Pharmaceutical Sciences, China Medical University, Shenyang 110001, China
3
Department of Nutrition and Food Science, College of Agriculture and Life Sciences, Texas A&M University, 123A Cater Mattil Hall, 2253 TAMU, College Station, TX 77843, USA
*
Authors to whom correspondence should be addressed.
Academic Editor: R. Manjunatha Kini
Received: 3 September 2016 / Revised: 19 September 2016 / Accepted: 21 September 2016 / Published: 27 September 2016
(This article belongs to the Section Animal Venoms)
View Full-Text   |   Download PDF [4697 KB, uploaded 27 September 2016]   |  

Abstract

Bradykinin-related peptides (BRPs) are one of the most extensively studied frog secretions-derived peptide families identified from many amphibian species. The diverse primary structures of BRPs have been proven essential for providing valuable information in understanding basic mechanisms associated with drug modification. Here, we isolated, identified and characterized a dodeca-BRP (RAP-L1, T6-BK), with primary structure RAPLPPGFTPFR, from the skin secretions of Chinese large odorous frogs, Odorrana livida. This novel peptide exhibited a dose-dependent contractile property on rat bladder and rat ileum, and increased the contraction frequency on rat uterus ex vivo smooth muscle preparations; it also showed vasorelaxant activity on rat tail artery smooth muscle. In addition, the analogue RAP-L1, T6, L8-BK completely abolished these effects on selected rat smooth muscle tissues, whilst it showed inhibition effect on bradykinin-induced rat tail artery relaxation. By using canonical antagonist for bradykinin B1 or B2 type receptors, we found that RAP-L1, T6-BK -induced relaxation of the arterial smooth muscle was very likely to be modulated by B2 receptors. The analogue RAP-L1, T6, L8-BK further enhanced the bradykinin inhibitory activity only under the condition of co-administration with HOE140 on rat tail artery, suggesting a synergistic inhibition mechanism by which targeting B2 type receptors. View Full-Text
Keywords: bradykinin related peptide (BRP); B2 receptor; rat tail artery; agonist and antagonist; smooth muscle bradykinin related peptide (BRP); B2 receptor; rat tail artery; agonist and antagonist; smooth muscle
Figures

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).

Supplementary material

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Xiang, J.; Wang, H.; Ma, C.; Zhou, M.; Wu, Y.; Wang, L.; Guo, S.; Chen, T.; Shaw, C. Ex Vivo Smooth Muscle Pharmacological Effects of a Novel Bradykinin-Related Peptide, and Its Analogue, from Chinese Large Odorous Frog, Odorrana livida Skin Secretions. Toxins 2016, 8, 283.

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