Document Detail

A new acidic myotoxic, anti-platelet and prostaglandin I2 inductor phospholipase A2 isolated from Bothrops moojeni snake venom.
MedLine Citation:
PMID:  18929590     Owner:  NLM     Status:  MEDLINE    
Phospholipase A2 (PLA2, EC, a major component of snake venoms, specifically catalyzes the hydrolysis of fatty acid ester bonds at position 2 of 1,2-diacyl-sn-3-phosphoglycerides in the presence of calcium. This article reports the purification and biochemical/functional characterization of BmooTX-I, a new myotoxic acidic phospholipase A2 from Bothrops moojeni snake venom. The purification of the enzyme was carried out through three chromatographic steps (ion-exchange on DEAE-Sepharose, molecular exclusion on Sephadex G-75 and hydrophobic chromatography on Phenyl-Sepharose). BmooTX-I was found to be a single-chain protein of 15,000 Da and pI 4.2. The N-terminal sequence revealed a high homology with other acidic Asp49 PLA2s from Bothrops snake venoms. It displayed a high phospholipase activity and platelet aggregation inhibition induced by collagen or ADP. Edema and myotoxicity in vivo were also induced by BmooTX-I. Analysis of myotoxic activity was carried out by optical and ultrastructural microscopy, demonstrating high levels of leukocytary infiltrate. Previous treatment of BmooTX-I with BPB reduced its enzymatic and myotoxic activities, as well as the effect on platelet aggregation. Acidic myotoxic PLA2s from Bothrops snake venoms have been little explored and the knowledge of its structural and functional features will be able to contribute for a better understanding of their action mechanism regarding enzymatic and toxic activities.
Norival A Santos-Filho; Lucas B Silveira; Clayton Z Oliveira; Carolina P Bernardes; Danilo L Menaldo; André L Fuly; Eliane C Arantes; Suely V Sampaio; Carla C N Mamede; Marcelo E Beletti; Fábio de Oliveira; Andreimar M Soares
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-09-27
Journal Detail:
Title:  Toxicon : official journal of the International Society on Toxinology     Volume:  52     ISSN:  0041-0101     ISO Abbreviation:  Toxicon     Publication Date:  2008 Dec 
Date Detail:
Created Date:  2008-12-05     Completed Date:  2009-03-12     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  1307333     Medline TA:  Toxicon     Country:  England    
Other Details:
Languages:  eng     Pagination:  908-17     Citation Subset:  IM    
Departamento de Análises Clínicas, Toxicológicas e Bromatológicas, Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de São Paulo, FCFRP-USP, Ribeirão Preto, SP, Brazil.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Amino Acid Sequence
Analysis of Variance
Chromatography, Ion Exchange
Crotalid Venoms / chemistry*
Epoprostenol / metabolism*
Hydrogen-Ion Concentration
Isoelectric Focusing
Molecular Sequence Data
Muscles / drug effects*,  pathology
Phospholipases A2 / chemistry,  isolation & purification,  metabolism*,  toxicity*
Platelet Aggregation Inhibitors / chemistry,  isolation & purification,  metabolism,  toxicity
Sequence Alignment
Transcriptional Activation
Reg. No./Substance:
0/Crotalid Venoms; 0/Platelet Aggregation Inhibitors; 35121-78-9/Epoprostenol; EC A2

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Propiverine-induced accumulation of nuclear and cytosolic protein in F344 rat kidneys: isolation and...
Next Document:  Visual deficits in pre-readers at familial risk for dyslexia.