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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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Author(s):
Bittencourt Rodrigues, Caroline Fabri [1, 2] ; Pena Ferreira, Marcelo Jose [3] ; Belchor, Mariana Novo [2] ; Costa, Caroline R. C. [2] ; Novaes, Danielle P. [2] ; dos Santos Junior, Adeilso Bispo [2] ; Tamayose, Cinthia I. [3] ; Terashima Pinho, Marcus Vinicius [2] ; de Oliveira, Marcos Antonio [4] ; Toyama, Marcos Hikari [2]
Total Authors: 10
Affiliation:
[1] Inst Butantan, Lab Herpetol, BR-05503900 Sao Paulo, SP - Brazil
[2] UNESP, Inst Biociencias, Lab Bioquim & Biol Mol Peptideos BIOMOLPEP, Campus Litoral Paulista, BR-11330900 Sao Vicente, SP - Brazil
[3] Univ Sao Paulo, Inst Biociencias, Dept Bot, BR-05508090 Sao Paulo - Brazil
[4] UNESP, Inst Biociencias, Lab Biol Mol Estrutural LABIMES, Campus Litoral Paulista, BR-11330900 Sao Vicente, SP - Brazil
Total Affiliations: 4
Document type: Journal article
Source: MARINE DRUGS; v. 17, n. 7 JUL 2019.
Web of Science Citations: 0
Abstract

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. (AU)

FAPESP's process: 17/20291-0 - Characterization of the proinflammatory activity of a new serine protease (cdtsp-2) purified from the total venom of Crotalus durissus terrificus
Grantee:Marcos Hikari Toyama
Support Opportunities: Regular Research Grants
FAPESP's process: 14/20932-8 - PHYTOCHEMISTRY, CHEMOSYSTEMATIC STUDY AND BIOLOGICAL ACTIVITIES OF Moquiniastrum AND Richterago SPECIES
Grantee:Cinthia Indy Tamayose
Support Opportunities: Scholarships in Brazil - Doctorate
FAPESP's process: 14/21593-2 - Baccharis L. (Asteraceae) and endophytic fungi: secondary metabolites and biological activities
Grantee:Marcelo José Pena Ferreira
Support Opportunities: Regular Research Grants
FAPESP's process: 13/10938-6 - Investigation of low molecular weight seaweeds sulfated polysaccharides on the structure and function of secretory phospholipase A2 Crotalus durissus terrificus
Grantee:Marcos Hikari Toyama
Support Opportunities: Regular Research Grants