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

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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.
LanguageEnglish
Article number376
Number of pages10
JournalToxins
Volume11
Issue number7
DOIs
Publication statusPublished - 28 Jun 2019

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Bradykinin
Anura
Smooth Muscle
Muscle
Skin
Peptides
Leucine
Rats
Ileum
Uterus
Arginine
Urinary Bladder
Substitution reactions
Arteries
Derivatives

Keywords

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

Cite this

@article{1c9a26d3c45b4d51b0c7eeb5e1072951,
title = "A Novel Bradykinin-Related Peptide, RVA-Thr6-BK, from the Skin Secretion of the Hejiang Frog; Ordorrana hejiangensis: Effects of Mammalian Isolated Smooth Muscle",
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.",
keywords = "bradykinin-related peptide (BRP); RVA-Thr6-BK; site-substitution variant; agonist; antagonist; myotropic actions",
author = "Yue Wu and Daning Shi and Xiaoling Chen and Lei Wang and Yuan Ying and Chengbang Ma and Xinping Xi and Mei Zhou and Tianbao Chen and Chris Shaw",
year = "2019",
month = "6",
day = "28",
doi = "10.3390/toxins11070376",
language = "English",
volume = "11",
journal = "Toxins",
issn = "2072-6651",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
number = "7",

}

TY - JOUR

T1 - A Novel Bradykinin-Related Peptide, RVA-Thr6-BK, from the Skin Secretion of the Hejiang Frog; Ordorrana hejiangensis: Effects of Mammalian Isolated Smooth Muscle

AU - Wu, Yue

AU - Shi , Daning

AU - Chen, Xiaoling

AU - Wang, Lei

AU - Ying, Yuan

AU - Ma, Chengbang

AU - Xi, Xinping

AU - Zhou, Mei

AU - Chen, Tianbao

AU - Shaw, Chris

PY - 2019/6/28

Y1 - 2019/6/28

N2 - 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.

AB - 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.

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

U2 - 10.3390/toxins11070376

DO - 10.3390/toxins11070376

M3 - Article

VL - 11

JO - Toxins

T2 - Toxins

JF - Toxins

SN - 2072-6651

IS - 7

M1 - 376

ER -