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Exploring and understanding the functional role, and biochemical and structural characteristics of an acidic phospholipase A 2, AplTx-I, purified from Agkistrodon piscivorus leucostoma snake venom.

التفاصيل البيبلوغرافية
العنوان: Exploring and understanding the functional role, and biochemical and structural characteristics of an acidic phospholipase A 2, AplTx-I, purified from Agkistrodon piscivorus leucostoma snake venom.
المؤلفون: Resende LM; Department of Biochemistry and Tissue Biology, Institute of Biology, Campinas State University (UNICAMP), Campinas, SP, Brazil., Almeida JR; IKIAM - Universidad Regional Amazónica, Km 7 Via Muyuna, Tena, Napo, Ecuador; International Network of Ecuadorian Snakes Venom Studies (RIEVSE), Ecuador. Electronic address: rafael.dealmeida@ikiam.edu.ec., Schezaro-Ramos R; Department of Pharmacology, Faculty of Medical Sciences, State University of Campinas (UNICAMP), Campinas, SP, Brazil., Collaço RC; Department of Pharmacology, Faculty of Medical Sciences, State University of Campinas (UNICAMP), Campinas, SP, Brazil., Simioni LR; Department of Pharmacology, Faculty of Medical Sciences, State University of Campinas (UNICAMP), Campinas, SP, Brazil., Ramírez D; Centro de Bioinformática y Simulación Molecular (CBSM), Universidad de Talca, 2 Norte 685, Casilla 721, Talca, Chile., González W; Centro de Bioinformática y Simulación Molecular (CBSM), Universidad de Talca, 2 Norte 685, Casilla 721, Talca, Chile; International Network of Ecuadorian Snakes Venom Studies (RIEVSE), Ecuador., Soares AM; Oswaldo Cruz Foundation (FIOCRUZ), CEBio, Fiocruz Rondônia and Federal University of Rondônia, Porto Velho, RO, Brazil; International Network of Ecuadorian Snakes Venom Studies (RIEVSE), Ecuador., Calderon LA; Oswaldo Cruz Foundation (FIOCRUZ), CEBio, Fiocruz Rondônia and Federal University of Rondônia, Porto Velho, RO, Brazil; International Network of Ecuadorian Snakes Venom Studies (RIEVSE), Ecuador., Marangoni S; Department of Biochemistry and Tissue Biology, Institute of Biology, Campinas State University (UNICAMP), Campinas, SP, Brazil., da Silva SL; IKIAM - Universidad Regional Amazónica, Km 7 Via Muyuna, Tena, Napo, Ecuador; International Network of Ecuadorian Snakes Venom Studies (RIEVSE), Ecuador.
المصدر: Toxicon : official journal of the International Society on Toxinology [Toxicon] 2017 Mar 01; Vol. 127, pp. 22-36. Date of Electronic Publication: 2017 Jan 04.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Pergamon Press Country of Publication: England NLM ID: 1307333 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1879-3150 (Electronic) Linking ISSN: 00410101 NLM ISO Abbreviation: Toxicon Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Oxford ; New York : Pergamon Press, c1962-
مواضيع طبية MeSH: Agkistrodon*, Crotalid Venoms/*toxicity , Phospholipases A2/*toxicity, Animals ; Chickens ; Crotalid Venoms/chemistry ; Mice ; Molecular Weight ; Neuromuscular Junction/drug effects ; Neuromuscular Junction/physiology ; Phospholipases A2/chemistry ; Phrenic Nerve/drug effects ; Phrenic Nerve/physiology ; Protein Isoforms ; Rats, Wistar
مستخلص: Phospholipases A 2 (PLA 2 s) constitute a class of extensively studied toxins, isolated from snake venoms. Basic PLA 2 isoforms mediate various toxicological effects, while the acidic isoforms generally have higher enzymatic activities, but do not promote evident toxic effects. The functions of these acidic isoforms in snake venoms are still not completely understood and more studies are needed to characterize the biological functions and diversification of acidic toxins in order to justify their abundant presence in these secretions. Recently, Lomonte and collaborators demonstrated, in a proteomic and toxicological study, high concentrations of PLA 2 s in the venom of Agkistrodon piscivorus leucostoma. We have, herein, purified and characterized an acidic PLA 2 from this snake venom, denominated AplTx-I, in order to better understand its biochemical and structural characteristics, as well as its biological effects. AplTx-I was purified using two chromatographic steps, in association with enzymatic and biological assays. The acidic toxin was found to be one of the most abundant proteins in the venom of A. p. leucostoma; the protein was monomeric with a molecular mass of 13,885.8 Da, as identified by mass spectrometry ESI-TOF and electrophoresis. The toxin has similar primary and tridimensional structures to those of other acidic PLA 2 s, a theoretical and experimental isoelectric point of ≈5.12, and a calcium-dependent enzyme activity of 25.8985 nM/min/mg, with maximum values at 37 °C and pH 8.0. Despite its high enzymatic activity on synthetic substrate, AplTx-I did not induce high or significant myotoxic, coagulant, anticoagulant, edema, neuromuscular toxicity in mouse phrenic nerve-diaphragm preparations or antibacterial activities. Interestingly, AplTx-I triggered a high and selective neuromuscular toxicity in chick biventer cervicis preparations. These findings are relevant to provide a deeper understanding of the pharmacology, role and diversification of acidic phospholipase A 2 isoforms in snake venoms.
(Copyright © 2017 Elsevier Ltd. All rights reserved.)
التعليقات: Erratum in: Toxicon. 2017 Mar 15;128:61. (PMID: 28185673)
فهرسة مساهمة: Keywords: Acidic phospholipase A(2); Agkistrodon piscivorus leucostoma; Pharmacological activity; Snake venom
المشرفين على المادة: 0 (Crotalid Venoms)
0 (Protein Isoforms)
EC 3.1.1.4 (Phospholipases A2)
تواريخ الأحداث: Date Created: 20170109 Date Completed: 20170926 Latest Revision: 20170926
رمز التحديث: 20221213
DOI: 10.1016/j.toxicon.2017.01.002
PMID: 28063838
قاعدة البيانات: MEDLINE
الوصف
تدمد:1879-3150
DOI:10.1016/j.toxicon.2017.01.002