Functional and structural characterization of a novel member of the natriuretic family of peptides from the venom of Pseudocerastes persicus

被引:27
作者
Amininasab, M
Elmi, MM
Endlich, N
Endlich, K
Parekh, N
Naderi-Manesh, H
Schaller, J
Mostafavi, H
Sattler, M
Sarbolouki, MN [1 ]
Muhle-Goll, C
机构
[1] Univ Tehran, Inst Biochem & Biophys, Tehran, Iran
[2] Heidelberg Univ, Inst Anat & Zellbiol, Heidelberg, Germany
[3] Heidelberg Univ, Dept Physiol & Pathophysiol, Heidelberg, Germany
[4] Tarbiat Modares Univ, Fac Sci, Tehran, Iran
[5] Univ Bern, Dept Chem & Biochem, Bern, Switzerland
[6] European Mol Biol Lab, D-69117 Heidelberg, Germany
[7] Univ Klinikum Mannheim, Inst Anasthesiol & Operat Intensivmed, D-68135 Mannheim, Germany
[8] Natl Res Ctr Genet & Biotechnol, Tehran, Iran
关键词
natriuretic peptide; snake venom; nuclear magnetic resonance characterization;
D O I
10.1016/S0014-5793(03)01455-8
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A novel peptide, PNP (Pseudocerastes persicus natriuretic peptide), was isolated from the venom of the Iranian viper P. persicus. Amino acid sequencing revealed that the 37-residue peptide belongs to the family of natriuretic peptides. The physiological effects of intra-venously PNP infused into anesthetized rats on urine flow, sodium excretion and blood pressure were comparable to those of atrial natriuretic peptide (ANP). In PC12 cells that were treated with either PNP, ANP, or C-type natriuretic peptide, PNP induced a similar cGMP response as ANP. Since PC12 cells only express the natriuretic peptide receptor (NPR)-A receptor we conclude that PNP binds to the NPR-A receptor. The solution conformation of PNP was characterized using H-1 nuclear magnetic resonance spectroscopy and indicates a high degree of conformational flexibility. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:104 / 108
页数:5
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