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

Mehriar Amininasab; Maryam M. Elmi; Nicole Endlich; Karlhans Endlich; Niranjah Parekh; Hossein Naderi-Manesh; Johann Schaller; Hossein Mostafavi; Michael Sattler; Mohammad N. Sarbolouki; Claudia Muhle-Goll

doi:10.1016/S0014-5793(03)01455-8

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

Mehriar Amininasab
, Maryam M. Elmi
, Nicole Endlich
, Karlhans Endlich
, Niranjah Parekh
, Hossein Naderi-Manesh
, Johann Schaller
, Hossein Mostafavi
, Michael Sattler
, Mohammad N. Sarbolouki
, Claudia Muhle-Goll

University of Tehran
Heidelberg University
Tarbiat Modares University
University of Bern
Natl. Res. Ctr. Genet. and Biotech.
European Molecular Biology Laboratory Heidelberg
Universitätsmedizin Mannheim

Research output: Contribution to journal › Article › peer-review

31 Scopus citations

Abstract

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 ¹H nuclear magnetic resonance spectroscopy and indicates a high degree of conformational flexibility.

Original language	English
Pages (from-to)	104-108
Number of pages	5
Journal	FEBS Letters
Volume	557
Issue number	1-3
DOIs	https://doi.org/10.1016/S0014-5793(03)01455-8
State	Published - 16 Jan 2004
Externally published	Yes

Keywords

Natriuretic peptide
Nuclear magnetic resonance characterization
Snake venom

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10.1016/S0014-5793(03)01455-8

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Amininasab, M., Elmi, M. M., Endlich, N., Endlich, K., Parekh, N., Naderi-Manesh, H., Schaller, J., Mostafavi, H., Sattler, M., Sarbolouki, M. N., & Muhle-Goll, C. (2004). Functional and structural characterization of a novel member of the natriuretic family of peptides from the venom of Pseudocerastes persicus. FEBS Letters, 557(1-3), 104-108. https://doi.org/10.1016/S0014-5793(03)01455-8

@article{53f60741a30547b6b0502a73484c305b,

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

abstract = "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 1H nuclear magnetic resonance spectroscopy and indicates a high degree of conformational flexibility.",

keywords = "Natriuretic peptide, Nuclear magnetic resonance characterization, Snake venom",

author = "Mehriar Amininasab and Elmi, \{Maryam M.\} and Nicole Endlich and Karlhans Endlich and Niranjah Parekh and Hossein Naderi-Manesh and Johann Schaller and Hossein Mostafavi and Michael Sattler and Sarbolouki, \{Mohammad N.\} and Claudia Muhle-Goll",

note = "Funding Information: This project was sponsored by the Research Council of Tehran University and generous helps from Tarbiat Modarres University. C.M.-G. is an Emmy Noether fellow of the DFG (Mu-1606-1). Supporting information available. One table with 1 H chemical shifts and J HN,Hα of PNP and one with statistical parameters of the structure calculation comparing {\textquoteleft}open{\textquoteright} and {\textquoteleft}closed{\textquoteright} conformations.",

year = "2004",

month = jan,

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doi = "10.1016/S0014-5793(03)01455-8",

language = "English",

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journal = "FEBS Letters",

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Amininasab, M, Elmi, MM, Endlich, N, Endlich, K, Parekh, N, Naderi-Manesh, H, Schaller, J, Mostafavi, H, Sattler, M, Sarbolouki, MN & Muhle-Goll, C 2004, 'Functional and structural characterization of a novel member of the natriuretic family of peptides from the venom of Pseudocerastes persicus', FEBS Letters, vol. 557, no. 1-3, pp. 104-108. https://doi.org/10.1016/S0014-5793(03)01455-8

TY - JOUR

T1 - Functional and structural characterization of a novel member of the natriuretic family of peptides from the venom of Pseudocerastes persicus

AU - Amininasab, Mehriar

AU - Elmi, Maryam M.

AU - Endlich, Nicole

AU - Endlich, Karlhans

AU - Parekh, Niranjah

AU - Naderi-Manesh, Hossein

AU - Schaller, Johann

AU - Mostafavi, Hossein

AU - Sattler, Michael

AU - Sarbolouki, Mohammad N.

AU - Muhle-Goll, Claudia

N1 - Funding Information: This project was sponsored by the Research Council of Tehran University and generous helps from Tarbiat Modarres University. C.M.-G. is an Emmy Noether fellow of the DFG (Mu-1606-1). Supporting information available. One table with 1 H chemical shifts and J HN,Hα of PNP and one with statistical parameters of the structure calculation comparing ‘open’ and ‘closed’ conformations.

PY - 2004/1/16

Y1 - 2004/1/16

N2 - 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 1H nuclear magnetic resonance spectroscopy and indicates a high degree of conformational flexibility.

AB - 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 1H nuclear magnetic resonance spectroscopy and indicates a high degree of conformational flexibility.

KW - Natriuretic peptide

KW - Nuclear magnetic resonance characterization

KW - Snake venom

UR - https://www.scopus.com/pages/publications/9144224758

U2 - 10.1016/S0014-5793(03)01455-8

DO - 10.1016/S0014-5793(03)01455-8

M3 - Article

C2 - 14741349

AN - SCOPUS:9144224758

SN - 0014-5793

VL - 557

SP - 104

EP - 108

JO - FEBS Letters

JF - FEBS Letters

IS - 1-3

ER -

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

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Keywords

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