Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/200085
Type: Artigo de periódico
Title: Lmrtx, A Basic Pla₂ (d49) Purified From Lachesis Muta Rhombeata Snake Venom With Enzymatic-related Antithrombotic And Anticoagulant Activity.
Author: Damico, Daniela C S
Vassequi-Silva, T
Torres-Huaco, F D
Nery-Diez, A C C
de Souza, R C G
Da Silva, S L
Vicente, C P
Mendes, C B
Antunes, E
Werneck, C C
Marangoni, Sérgio
Abstract: A basic phospholipase A₂ (LmrTX) isoform was isolated from Lachesis muta rhombeata snake venom and partially characterized. The venom was fractionated by molecular exclusion chromatography in ammonium bicarbonate buffer followed by reverse-phase HPLC on a C-5 Discovery® Bio Wide column. From liquid chromatography-electrospray ionization/mass spectrometry, the molecular mass of LmrTX was measured as 14.277.50 Da. The amino acid sequence showed a high degree of homology between PLA₂ LmrTX from L. muta rhombeata and other PLA₂ from snake venoms, like CB1 and CB2 from Crotalus durissus terrificus; LmTX-I and LmTX-II from Lachesis muta muta. LmrTX had PLA₂ activity in the presence of a synthetic substrate and alkylation of histidine residues significantly inhibited (P < 0.05) the enzymatic activity of LmrTX and its anticoagulant and antithrombotic activity. In this study, we examined the ability of the LmrTX in altering thrombus formation in living mouse, using a photochemically induced arterial thrombosis model. The control animals that did not receive protein injection showed a normal occlusion time, which was around 57 ± 7.8 min. LmrTX, the PLA₂ from L. muta rhombeata venom, caused a change in the occlusion time to 99 ± 10 min with doses of 7.5 μg/mice. Additionally, LmrTX showed the anticoagulant activity in vitro and ex vivo and prolonging the time aggregation in wash platelet induced by ADP and Thrombin.
Subject: Amino Acid Sequence
Animals
Base Sequence
Chromatography, Gel
Chromatography, High Pressure Liquid
Chromatography, Liquid
Crotalid Venoms
Mass Spectrometry
Mice
Molecular Sequence Data
Phospholipases A2
Sequence Analysis, Dna
Species Specificity
Thrombosis
Rights: fechado
Identifier DOI: 10.1016/j.toxicon.2012.06.010
Address: http://www.ncbi.nlm.nih.gov/pubmed/22750534
Date Issue: 2012
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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