Mechanism of in vivo anticoagulant and haemolytic activity by a neutral phospholipase A2 purified from Daboia russelii russelii venom: Correlation with clinical manifestations in Russell's Viper envenomed patients

A 13.0 kDa neutral phospholipase A2 (NEUPHOLIPASE) purified from venom of Daboia russelii russelii from eastern India was identified by peptide mass fingerprinting analysis. It exerted dose-dependent PLA2, anticoagulant and indirect haemolytic activities. NEUPHOLIPASE showed preferential binding fol...

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Bibliographic Details
Published in:Toxicon (Oxford) 2013-02, Vol.76, p.291-300
Main Authors: Saikia, Debashree, Majumdar, Sourav, Mukherjee, Ashis K.
Format: Article
Language:English
Subjects:
Anticoagulant activity
Anticoagulants
Biocompatibility
Biomedical materials
Correlation
Daboia russelii russelii
dose response
erythrocytes
Haemolysis
hemolysis
Hydrolysis
leukocytes
liver
Mice
Neutral PLA2
pathogenesis
Patients
phosphatidylcholines
phosphatidylethanolamines
phosphatidylserines
Phospholipase
phospholipase A2
Phospholipids hydrolysis
plasma membrane
Russell's Viper venom
Surgical implants
toxicity
venoms
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Summary:A 13.0 kDa neutral phospholipase A2 (NEUPHOLIPASE) purified from venom of Daboia russelii russelii from eastern India was identified by peptide mass fingerprinting analysis. It exerted dose-dependent PLA2, anticoagulant and indirect haemolytic activities. NEUPHOLIPASE showed preferential binding followed by hydrolysis of phosphatidylserine > phosphatidylcholine >> phosphatidylethanolamine. Circular dichroism analysis of NEUPHOLIPASE showed a high content of alpha helix (54.6%) followed by beta-turn (29.7%) in its secondary structure. Gas-chromatographic analysis of plasma from PLA2-treated mice suggested preferential hydrolysis of pro-coagulant phospholipid PS was the primary mechanism to account for in vivo anticoagulant effect of NEUPHOLIPASE. The NEUPHOLIPASE-treated mice blood showed a significant decrease (p 
ISSN:0041-0101
1879-3150
DOI:10.1016/j.toxicon.2013.10.001