Harpalycin 2 inhibits the enzymatic and platelet aggregation activities of PrTX-III, a D49 phospholipase A2 from Bothrops pirajai venom

  title={Harpalycin 2 inhibits the enzymatic and platelet aggregation activities of PrTX-III, a D49 phospholipase A2 from Bothrops pirajai venom},
  author={Rafael M Ximenes and Renata de Sousa Alves and Ticiana Praciano Pereira and Renata Mendonça Ara{\'u}jo and Edilberto Rocha Silveira and Marcelo Montenegro Rabello and Marcelo Zaldini Hernandes and Veronica C G Soares and Daniel Bristot and Camila Lehnhardt Pires and Daniela de Oliveira Toyama and Henrique Hessel Gaeta and Helena Serra Azul Monteiro and Marcos Hikari Toyama},
  journal={BMC Complementary and Alternative Medicine},
  pages={139 - 139}
BackgroundHarpalycin 2 (HP-2) is an isoflavone isolated from the leaves of Harpalyce brasiliana Benth., a snakeroot found in northeast region of Brazil and used in folk medicine to treat snakebite. Its leaves are said to be anti-inflammatory. Secretory phospholipases A2 are important toxins found in snake venom and are structurally related to those found in inflammatory conditions in mammals, as in arthritis and atherosclerosis, and for this reason can be valuable tools for searching new anti… 
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A structure-based proposal for a comprehensive myotoxic mechanism of phospholipase A2-like proteins from viperid snake venoms.
The data summarized here for the PLA2-like myotoxins could provide a useful molecular basis for the search for novel neutralizing strategies to improve the treatment of envenomation by viperid snakes.
Effect of Chlorogenic Acid (5-Caffeoylquinic Acid) Isolated from Baccharis oxyodonta on the Structure and Pharmacological Activities of Secretory Phospholipase A2 from Crotalus durissus terrificus
The results showed the potential application of 5CQA in the snake poisoning treatment and modulation of the pathological effect of inflammation induced by secretory PLA2, which induced massive bacterial cell destruction.
Plants and phytocompounds active against Bothrops venoms.
Natural compounds isolated from plants, mainly from those used in folk medicine to treat snakebite, are a good choice for finding new lead compounds to improve snakebite treatment and minimize its consequences for the victims.
Perspective on the Therapeutics of Anti-Snake Venom
Specific therapeutic snakebite envenomation treatments are described and an increased number of literature reports on the ability of natural sources, particularly plants, to treat snakebites are covered, along with their mechanisms, drawbacks and future perspectives.
Evaluation of in vitro Cytotoxic Effects of Especifico Pessoa Phytotherapic Tincture on Ehrlich Tumor Cells and Mice Spleen Cells
Especifico Pessoa (EP) is traditionally used for the treatment of snakebite envenoming. The traditional use of EP and its properties have been reported. In this study, we evaluated the in vitro
Avaliação dos efeitos dos polissacarídeos sulfatados de macroalgas marinhas sobre a Fosfolipase A2 de Crotalus durissus terrificus
XV 1. INTRODUCAO 16 1.1. Produtos naturais marinhos 16 1.2. Algas 16 1.3. Polissacarideo sulfatado de Rhodophyta 17 1.4. Polissacarideo sulfatado de Heterokontophyta 19 1.5. Polissacarideo sulfatado


Dissociation of enzymatic and pharmacological properties of piratoxins-I and -III, two myotoxic phospholipases A2 from Bothrops pirajai snake venom.
Analysis of structural changes by circular dichroism spectroscopy demonstrated significant changes in the secondary structure only in the case of N-terminal octapeptide cleavage, which indicates that Pr TX-I and PrTX-III possess regions other than the catalytic site, which determine their toxic and pharmacological activities.
Effect of umbelliferone (7-hydroxycoumarin, 7-HOC) on the enzymatic, edematogenic and necrotic activities of secretory phospholipase A2 (sPLA2) isolated from Crotalus durissus collilineatus venom.
The data suggest that 7-HOC interacts with s PLA2 and causes some structural modifications that lead to a sharp decrease or inhibition of the edematogenic and myotoxic activities of this enzyme, indicating its potential use to suppress inflammation induced by sPLA2 from the snake venom.
Modulation of the pharmacological effects of enzymatically-active PLA2 by BTL-2, an isolectin isolated from the Bryothamnion triquetrum red alga
The unexpected results observed for the PLA2-BTL-2 complex strongly suggest that the pharmacological activity of this PLA2 is not solely dependent on the presence of enzymatic activity, and that other pharmacological regions may also be involved.
Effects of morin on snake venom phospholipase A2 (PLA2).
It is observed that a treatment of PLA2 with morin induces several modifications in the aromatic amino acids, with accompanying changes in its amino acid composition, which may be an indication that PLA2 possess a second pharmacological site which does not affect or depend on the enzymatic activity.
Flavonoids as Phospholipase A2 Inhibitors: Importance of Their Structure for Selective Inhibition of Group II Phospholipase A2
Results obtained indicate that the hydroxyl group in 5-position as well as the double bond and the double-bonded oxygen in the oxane ring are all important for the overall ability of flavonoids to inhibit PLA2 activity, and that the Hydroxyl groups in 3′- and 4′-position are required for selective inhibition of PLA2-II.
Morelloflavone, a novel biflavonoid inhibitor of human secretory phospholipase A2 with anti-inflammatory activity.
Morelloflavone is an inhibitor of secretory PLA2 with selectivity for groups II and III enzymes and may be a pharmacological tool, and shows anti-inflammatory activity apparently not related to the synthesis of eicosanoids, but likely dependent on other mechanisms such as scavenging of reactive oxygen species.
Isolation and Enzymatic Characterization of a Basic Phospholipase A2 from Bothrops jararacussu Snake Venom
A novel basic phospholipase A2 (PLA2) isoform was isolated from Bothrops jararacussu snake venom and partially characterized and had high PLA2 activity and produced moderate myonecrosis in skeletal muscle, but showed no neuromuscular activity in mouse phrenic nerve-diaphragm preparations.
An overview of lysine-49 phospholipase A2 myotoxins from crotalid snake venoms and their structural determinants of myotoxic action.
It is proposed that all the toxic activities of Lys49 PLA2s are related to their ability to destabilize natural and artificial membranes, using a cationic/hydrophobic effector site located at their C-terminal loop.
Purification and Amino Acid Sequence of MP-III 4R D49 Phospholipase A2 from Bothrops pirajai Snake Venom, a Toxin with Moderate PLA2 and Anticoagulant Activities and High Myotoxic Activity
Based on the N-terminal sequence and biological activities, MP-III 4R was identified as similar to piratoxin-III (PrTX-III), which was isolated by conventional chromatography based on molecular exclusion ion exchange chromatography.
Crystallization and preliminary X-ray diffraction studies of piratoxin III, a D-49 phospholipase A2 from the venom of Bothrops pirajai.
Piratoxin III (PrTX-III) is a phospholipase A2 (PLA2, E.C.3.1.4, phosphatide sn-2 acylhydrolase) isolated from Bothrops pirajai, using bothropstoxin I from the venom of B. jararacussu as a search model.