Cloning and characterization of natriuretic peptides from the venom glands of Australian elapids

St Pierre, Liam, Flight, Simone M., Masci, Paul P., Hanchard, Kim J., Lewis, Richard J., Alewood, Paul F., De Jersey, John and Lavin, Martin F. (2006) Cloning and characterization of natriuretic peptides from the venom glands of Australian elapids. Biochimie, 88 12: 1923-1931. doi:10.1016/j.biochi.2006.06.014

Author St Pierre, Liam
Flight, Simone M.
Masci, Paul P.
Hanchard, Kim J.
Lewis, Richard J.
Alewood, Paul F.
De Jersey, John
Lavin, Martin F.
Title Cloning and characterization of natriuretic peptides from the venom glands of Australian elapids
Journal name Biochimie   Check publisher's open access policy
ISSN 0300-9084
Publication date 2006-12-01
Sub-type Article (original research)
DOI 10.1016/j.biochi.2006.06.014
Volume 88
Issue 12
Start page 1923
End page 1931
Total pages 9
Editor M. Grunberg-Manago
R. H. Buckingham
C. Forest
J. Hershey
L. Kisselev
J. L. Mergny
Y. Nakamura
Place of publication Paris
Publisher Elsevier
Language eng
Subject C1
320305 Medical Biochemistry - Proteins and Peptides
780103 Chemical sciences
Abstract The venom from Australian elapid snakes contains a complex mixture of polypeptide toxins that adversely affect multiple homeostatic systems within their prey in a highly specific and targeted manner. Included in these toxin families are the recently described venom natriuretic peptides, which display similar structure and vasoactive functions to mammalian natriuretic peptides. This paper describes the identification and detailed comparative analysis of the cDNA transcripts coding for the mature natriuretic peptide from a total of nine Australian elapid snake species. Multiple isoforms were identified in a number of species and represent the first description of a natriuretic peptide from the venom gland for most of these snakes. Two distinct natriuretic peptide isoforms were selected from the common brown snake (Pseudonaja textilis), PtNP-a, and the mulga (Pseudechis australis), PaNP-c, for recombinant protein expression and functional analysis. Only one of these peptides, PtNP-a, displayed cGMP stimulation indicative of normal natriuretic peptide activity. Interestingly, both recombinant peptides demonstrated a dose-dependent inhibition of angiotensin converting enzyme (ACE) activity, which is predictive of the vasoactive effects of the toxin. The natriuretic peptides, however, did not possess any coagulopathic activity, nor did they inhibit or potentiate thrombin, adenosine diphosphate or arachidonic acid induced platelet aggregation. The data presented in this study represent a significant resource for understanding the role of various natriuretic peptides isoforms during the envenomation process by Australian elapid snakes. (c) 2006 Published by Elsevier Masson SAS.
Keyword Biochemistry & Molecular Biology
Australian snakes
natriuretic peptide
ACE inhibition
cGMP elevation
Angiotensin-converting Enzyme
Bradykinin-potentiating Peptides
Q-Index Code C1

Document type: Journal Article
Sub-type: Article (original research)
Collections: Faculty of Science Publications
Excellence in Research Australia (ERA) - Collection
2007 Higher Education Research Data Collection
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 23 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 25 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Wed, 15 Aug 2007, 20:00:57 EST