scholarly journals Bioaffinity Fishing Procedure Using Secretory Phospholipase A2 for Screening for Bioactive Components: Modulation of Pharmacological Effect Induced by sPLA2 from Crotalus durissus terrificus by Hispidulin from Moquiniastrum floribundum

Molecules ◽  
2020 ◽  
Vol 25 (2) ◽  
pp. 282 ◽  
Author(s):  
Adeilso Bispo dos Santos Junior ◽  
Cinthia I. Tamayose ◽  
Marcelo J. P. Ferreira ◽  
Mariana N. Belchor ◽  
Caroline R. C. Costa ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
High Selectivity ◽  
Secretory Phospholipase A2 ◽  
Bioactive Components ◽  
Crotalus Durissus Terrificus ◽  
Secretory Phospholipase ◽  
Spla2 Activity ◽  
Screening And Identification ◽  
Isolated Compound ◽  
Crotalus Durissus

Bioaffinity capturing of molecules allows the discovery of bioactive compounds and decreases the need for various stages in the natural compound isolation process. Despite the high selectivity of this technique, the screening and identification methodology depends on the presence of a protein to capture potential ligands. However, some proteins, such as snake secretory phospholipase A2 (sPLA2), have never been investigated using this approach. The purpose of this study was to evaluate the use of a new method for screening natural compounds using a bioaffinity-guided ultrafiltration method on Crotalus durissus terrificus sPLA2 followed by HPLC-MS to identify the compounds, and this method could be used to discover new anti-inflammatory compounds from the various organisms originating from biodiversity. Different extracts were selected to evaluate their ability to inhibit sPLA2 activity. The extracts were incubated with sPLA2 and the resulting mixture was ultrafiltrated to elute unbound components. The resulting compounds were identified by HPLC-MS. We identified hispidulin as one of the components present in the Moquiniastrum floribundum leaf and evaluated the ability of this isolated compound to neutralize the inflammatory activity of sPLA2 from Crotalus durissus terrificus.

Fast and efficient procedure for purification of secretory phospholipase A2 (SPLA2) from Crotalus durissus terrificus venom using a solid phase extraction

Toxicon ◽  
2020 ◽  
Vol 177 ◽  
pp. S49
Author(s):  
Airam Roggero dos Santos Silva ◽  
Laila Lucyane Ferreira de Moraes ◽  
Mariana Novo Belchor ◽  
Caroline R.C. Costa ◽  
Danielle P. Novaes ◽  
...  
Keyword(s):  
Solid Phase Extraction ◽  
Phospholipase A2 ◽  
Solid Phase ◽  
Phase Extraction ◽  
Secretory Phospholipase A2 ◽  
Efficient Procedure ◽  
Crotalus Durissus Terrificus ◽  
Secretory Phospholipase ◽  
Crotalus Durissus

Evaluation of a hydrolysable tannin purified from Laguncularia racemosa leaves against edema and myonecrosis induced by secretory phospholipase A2 isolated from Crotalus durissus terrificus venom

Toxicon ◽  
2020 ◽  
Vol 177 ◽  
pp. S48-S49
Author(s):  
Caroline Fabri Bittencourt Rodrigues ◽  
Marcelo José Pena Ferreira ◽  
Mariana Novo Belchor ◽  
Caroline R.C. Costa ◽  
Danielle P. Novaes ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
Laguncularia Racemosa ◽  
Secretory Phospholipase A2 ◽  
Hydrolysable Tannin ◽  
Crotalus Durissus Terrificus ◽  
Secretory Phospholipase ◽  
Crotalus Durissus

scholarly journals Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (Laguncularia racemosa) Leaves, on Snake Venom Secretory Phospholipase A2

Marine Drugs ◽  
2019 ◽  
Vol 17 (7) ◽  
pp. 403 ◽  
Author(s):  
Caroline Fabri Bittencourt Rodrigues ◽  
Marcelo José Pena Ferreira ◽  
Mariana Novo Belchor ◽  
Caroline R. C. Costa ◽  
Danielle P. Novaes ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
Biological Effects ◽  
Laguncularia Racemosa ◽  
Laser Desorption Ionization ◽  
Secretory Phospholipase A2 ◽  
Ionization Time ◽  
Secretory Phospholipase ◽  
Flight Mass Spectrometry ◽  
Inhibitory Potential ◽  
Crotalus Durissus

Ellagitannins constitute the largest group of hydrolyzable tannins of plants, and, from this group, casuarictin (Casu) was identified in some plant species. However, to our knowledge, no investigation of secretory phospholipase A2 (sPLA2) inhibition by Casu has been performed yet. Casuarictin was isolated by chromatography n-butanol (n-BuOH) partition of Laguncularia racemosa leaves. The pharmacological and biological effects of Casu were evaluated on isolated sPLA2 from the rattlesnake (Crotalus durissus terrificus) and using a plant bacterial strain. The compound was able to form a protein complex consisting of a stable sPLA2 + Casu complex. Analyses carried out with matrix-assisted laser desorption ionization-time-of-flight mass spectrometry (MALDI-TOF) revealed that the molecular mass of sPLA2 increased from 14,425.62 to 15,362.74 Da. The enzymatic activity of the sPLA2 + Casu complex was significantly lower than that of native sPLA2. Besides, molecular interactions of Casu with sPLA2 were able to virtually abolish the native edematogenic effect as well as myonecrosis induced by the protein when injected 10 min after sPLA2. Therefore, Casu may be considered a potential anti-inflammatory that can be used to treat edema and myonecrosis induced by serine-secreting phospholipase A2. In addition, the compound also showed great antimicrobial potential.

scholarly journals Modulation of the Pharmacological Activities of Secretory Phospholipase A2 from Crotalus durissus cascavella Induced by Naringin

Molecules ◽  
2011 ◽  
Vol 16 (1) ◽  
pp. 738-761 ◽  
Author(s):  
Marcelo L. Santos ◽  
Daniela O. Toyama ◽  
Simone C. B. Oliveira ◽  
Camila A. Cotrim ◽  
Eduardo B. S. Diz-Filho ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
Secretory Phospholipase A2 ◽  
Pharmacological Activities ◽  
Secretory Phospholipase ◽  
Crotalus Durissus Cascavella ◽  
Crotalus Durissus

scholarly journals Effect of cooling on lung secretory phospholipase A2 activity in vitro, ex vivo, and in vivo

2019 ◽  
Vol 316 (3) ◽  
pp. L498-L505 ◽  
Author(s):  
Chiara Autilio ◽  
Shivani Shankar-Aguilera ◽  
Angelo Minucci ◽  
Lhoussaine Touqui ◽  
Daniele De Luca
Keyword(s):  
Bronchoalveolar Lavage ◽  
Phospholipase A2 ◽  
Bile Acids ◽  
Ex Vivo ◽  
Whole Body ◽  
Secretory Phospholipase A2 ◽  
Secretory Phospholipase ◽  
Spla2 Activity

Hypothermia can modify surfactant composition and function. Secretory phospholipase A2 (sPLA2) hydrolyses surfactant phospholipids and is important in the pathobiology of several critical respiratory disorders. We hypothesize that sPLA2 activity might be influenced by the temperature partially explaining surfactant changes. This study aims to evaluate comprehensively the effect of hypothermia on sPLA2 activity. We measured sPLA2 activity at different temperatures, alone or combined with bile acids, in vitro (incubating human recombinant sPLA2-IIA and porcine sPLA2-IB), ex vivo (by cooling bronchoalveolar lavage samples from neonates with respiratory distress syndrome or no lung disease), and in vivo (using lavage samples obtained before and after 72 h of whole body cooling in neonates with hypoxic-ischemic encephalopathy). We also measured concentrations of various sPLA2 subtypes and natural sPLA2 inhibitors in in vivo cooled samples. Results were corrected for protein content and dilution. In vitro cooling did not show any effect of hypothermia on sPLA2. Ex vivo cooling did not alter total sPLA2 activity, and the addition of bile acids increased sPLA2 activity irrespective of the temperature and the type of sampled patient. In vivo hypothermia reduced median sPLA2 activity from 16.6 [15.2–106.7] IU/mg to 3.3 [2.7–8.5] IU/mg ( P = 0.026) and mean sPLA2-IIA from 1.1 (0.8) pg/μg to 0.6 (0.4) pg/μg ( P = 0.047), whereas dioleylphosphatidylglycerol increased from 8.3 (3.9)% to 12.8 (5.1)% ( P = 0.02). Whole body hypothermia decreases in vivo global sPLA2 activity in bronchoalveolar lavage fluids through the reduction of sPLA2-IIA and increment of dioleylphosphatidylglycerol. This effect is absent during in vitro or ex vivo hypothermia.

scholarly journals AKTIVITAS FOSFOLIPASE-A2 SEKRETORIS PLASMA TROMBOSITOPENIA DEMAM BERDARAH DENGUE

2018 ◽  
Vol 17 (1) ◽  
pp. 12
Author(s):  
Endang Retnowati K ◽  
Wiyanda Hidayati S ◽  
Liana .
Keyword(s):  
Phospholipase A2 ◽  
Proinflammatory Cytokines ◽  
Pearson Correlation ◽  
World Health ◽  
Assay Method ◽  
Secretory Phospholipase A2 ◽  
Secretory Phospholipase ◽  
Spla2 Activity ◽  
The Mean ◽  
Phospholipase A2 Activity

Infected macrophages by dengue virus will produce phospholipase-A2 (PLA2) enzyme, that can promote arachidonic acidmetabolism that produce inflammatory mediators, causing endhothelial damage and severe plasma leakage. Capillary endothelialdamage can cause platelet adhesion and aggregation, so that many platelets will be consumed. The role of sPLA2 (secretoryphospholipase-A2), which is a part of PLA2 in dengue and thrombocytopenia up to now has not been widely studied. The objective ofthe study is to analyze the association between the activity of plasma secretory phospholipase-A2 and the degree of thrombocytopeniain DHF adult patients. the study is carried out by a cross sectional, observational analytical study on 45 hospitalized adult patientssuffering dengue hemorrhagic fever in the Tropical Infection Ward, Department of Internal Medicine, Dr. Soetomo Hospital Surabaya,which has been conducted from February–December 2009. The diagnosis of Dengue Haemorrhagic Fever (DHF) was based on the1997 World Health Organization (WHO) criteria, that minimally had one positive serology marker of dengue. Venous blood wastaken from the patient for examining the activity of secretory phospholipase-A2 by correlated enzyme assay method, and plateletcount using automated hematology analyzer. The results of the secretory phospholipase-A2 activity and degree of thrombocytopeniawere analyzed by Pearson correlation test to determine the correlation between the two variables. In this study so far was foundthat the secretory phospholipase-A2 activity in DHF patients was 36.9–195.6 unit/mL (mean 97.49 unit/mL, SD 30.06 unit/mL).The mean of secretory phospholipase-A2 activity was increased according to the degree of thrombocytopenia severity. The mean ofsecretory phospholipase-A2 activities were 91.65 unit/mL, 98.94 unit/mL, and 110.47 unit/mL. The degree of thrombocytopeniawas divided into mild, moderate, and severe. Most of the patients showed mild thrombocytopenia. The sPLA2 activity in this studywas increased in DHF patients with second day of fever, and then decreased at the third and forth day of fever, and increased inDBD patients suffering fifth day of fever. The statistical analyzes show a non significant correlation between secretory phospholipaseA2 activity and degree of thrombocytopenia (p = 0.579). This result may be caused by several factors which influencing thethrombocytopenia in DHF, such as bone marrow suppression, dengue viral serotype, influence of cytosolic phospholipase-A2 (cPLA2)activity, and other proinflammatory cytokines which in this study could not be controlled. Statistical analyzes show a significantcorrelation between sPLA2 activity and the day of fever (p = 0.04). Further studies should have to be carried out in order to knowthe pattern of sPLA2 activity in DHF grade I, II, III, and IV, and to know the influence of other proinflammatory cytokines and viralserotypes in sPLA2 activities.

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