Tags

Type your tag names separated by a space and hit enter

Cloning and characterisation of natriuretic peptides from the venom glands of Australian elapids.
Biochimie. 2006 Dec; 88(12):1923-31.B

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.

Authors+Show Affiliations

The Queensland Institute of Medical Research, Brisbane, Australia.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16908092

Citation

St Pierre, Liam, et al. "Cloning and Characterisation of Natriuretic Peptides From the Venom Glands of Australian Elapids." Biochimie, vol. 88, no. 12, 2006, pp. 1923-31.
St Pierre L, Flight S, Masci PP, et al. Cloning and characterisation of natriuretic peptides from the venom glands of Australian elapids. Biochimie. 2006;88(12):1923-31.
St Pierre, L., Flight, S., Masci, P. P., Hanchard, K. J., Lewis, R. J., Alewood, P. F., de Jersey, J., & Lavin, M. F. (2006). Cloning and characterisation of natriuretic peptides from the venom glands of Australian elapids. Biochimie, 88(12), 1923-31.
St Pierre L, et al. Cloning and Characterisation of Natriuretic Peptides From the Venom Glands of Australian Elapids. Biochimie. 2006;88(12):1923-31. PubMed PMID: 16908092.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Cloning and characterisation of natriuretic peptides from the venom glands of Australian elapids. AU - St Pierre,Liam, AU - Flight,Simone, AU - Masci,Paul P, AU - Hanchard,Kim J, AU - Lewis,Richard J, AU - Alewood,Paul F, AU - de Jersey,John, AU - Lavin,Martin F, Y1 - 2006/08/04/ PY - 2006/03/17/received PY - 2006/06/18/accepted PY - 2006/8/16/pubmed PY - 2007/4/26/medline PY - 2006/8/16/entrez SP - 1923 EP - 31 JF - Biochimie JO - Biochimie VL - 88 IS - 12 N2 - 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. SN - 0300-9084 UR - https://www.unboundmedicine.com/medline/citation/16908092/Cloning_and_characterisation_of_natriuretic_peptides_from_the_venom_glands_of_Australian_elapids_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0300-9084(06)00147-7 DB - PRIME DP - Unbound Medicine ER -