Sulfated polysaccharide extracted of the green algae Caulerpa racemosa increase the enzymatic activity and paw edema induced by sPLA2 from Crotalus durissus terrificus venom

Sulfated polysaccharides derived from seaweed have shown great potential for use in the development of new drugs. In this study, we observed that a low-molecular-weight sulfated polysaccharide from Caulerpa racemosa, termed CrSP, could interact with secretory phospholipase A2 (sPLA2) isolated from Crotalus durissus terrificus venom. When native sPLA2 (14 kDa) was incubated with CrSP, they formed a molecular complex (sPLA2:CrSP) with a molecular mass of 32 kDa, approximately. Size exclusion chromatography experiments suggested that CrSP formed a stable complex with sPLA2. We belived that sPLA2 and SPCr are involved an ionic interaction between negatively charged CrSP and the positively charged basic amino acid residues of sPLA2, because this interaction induced significant changes in sPLA2 enzymatic and pharmacological activities. CrSP caused a significant increase in sPLA2 enzymatic and bactericidal activity and increased its edematogenic effect. A pharmacological assay showed that the myotoxic activity of sPLA2:CrSP is unrelated to its enzymatic activity and that sPLA2:CrSP may have a practical application as a natural antibacterial agent for use in humans and commercially raised animals.

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Main Authors: Pires,Camila L., Rodrigues,Selma D., Bristot,Daniel, Gaeta,Henrique Hessel, Toyama,Daniela de Oliveira, Farias,Wladimir Ronald Lobo, Toyama,Marcos Hikari
Format: Digital revista
Language:English
Published: Sociedade Brasileira de Farmacognosia 2013
Online Access:http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0102-695X2013000400010
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spelling oai:scielo:S0102-695X20130004000102013-09-23Sulfated polysaccharide extracted of the green algae Caulerpa racemosa increase the enzymatic activity and paw edema induced by sPLA2 from Crotalus durissus terrificus venomPires,Camila L.Rodrigues,Selma D.Bristot,DanielGaeta,Henrique HesselToyama,Daniela de OliveiraFarias,Wladimir Ronald LoboToyama,Marcos Hikari Crotalus durissus terrificus edematogenic effect myotoxic activity seaweed secretory phospholipase A2 sulfated polysaccharides Sulfated polysaccharides derived from seaweed have shown great potential for use in the development of new drugs. In this study, we observed that a low-molecular-weight sulfated polysaccharide from Caulerpa racemosa, termed CrSP, could interact with secretory phospholipase A2 (sPLA2) isolated from Crotalus durissus terrificus venom. When native sPLA2 (14 kDa) was incubated with CrSP, they formed a molecular complex (sPLA2:CrSP) with a molecular mass of 32 kDa, approximately. Size exclusion chromatography experiments suggested that CrSP formed a stable complex with sPLA2. We belived that sPLA2 and SPCr are involved an ionic interaction between negatively charged CrSP and the positively charged basic amino acid residues of sPLA2, because this interaction induced significant changes in sPLA2 enzymatic and pharmacological activities. CrSP caused a significant increase in sPLA2 enzymatic and bactericidal activity and increased its edematogenic effect. A pharmacological assay showed that the myotoxic activity of sPLA2:CrSP is unrelated to its enzymatic activity and that sPLA2:CrSP may have a practical application as a natural antibacterial agent for use in humans and commercially raised animals.info:eu-repo/semantics/openAccessSociedade Brasileira de FarmacognosiaRevista Brasileira de Farmacognosia v.23 n.4 20132013-08-01info:eu-repo/semantics/articletext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0102-695X2013000400010en10.1590/S0102-695X2013005000050
institution SCIELO
collection OJS
country Brasil
countrycode BR
component Revista
access En linea
databasecode rev-scielo-br
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region America del Sur
libraryname SciELO
language English
format Digital
author Pires,Camila L.
Rodrigues,Selma D.
Bristot,Daniel
Gaeta,Henrique Hessel
Toyama,Daniela de Oliveira
Farias,Wladimir Ronald Lobo
Toyama,Marcos Hikari
spellingShingle Pires,Camila L.
Rodrigues,Selma D.
Bristot,Daniel
Gaeta,Henrique Hessel
Toyama,Daniela de Oliveira
Farias,Wladimir Ronald Lobo
Toyama,Marcos Hikari
Sulfated polysaccharide extracted of the green algae Caulerpa racemosa increase the enzymatic activity and paw edema induced by sPLA2 from Crotalus durissus terrificus venom
author_facet Pires,Camila L.
Rodrigues,Selma D.
Bristot,Daniel
Gaeta,Henrique Hessel
Toyama,Daniela de Oliveira
Farias,Wladimir Ronald Lobo
Toyama,Marcos Hikari
author_sort Pires,Camila L.
title Sulfated polysaccharide extracted of the green algae Caulerpa racemosa increase the enzymatic activity and paw edema induced by sPLA2 from Crotalus durissus terrificus venom
title_short Sulfated polysaccharide extracted of the green algae Caulerpa racemosa increase the enzymatic activity and paw edema induced by sPLA2 from Crotalus durissus terrificus venom
title_full Sulfated polysaccharide extracted of the green algae Caulerpa racemosa increase the enzymatic activity and paw edema induced by sPLA2 from Crotalus durissus terrificus venom
title_fullStr Sulfated polysaccharide extracted of the green algae Caulerpa racemosa increase the enzymatic activity and paw edema induced by sPLA2 from Crotalus durissus terrificus venom
title_full_unstemmed Sulfated polysaccharide extracted of the green algae Caulerpa racemosa increase the enzymatic activity and paw edema induced by sPLA2 from Crotalus durissus terrificus venom
title_sort sulfated polysaccharide extracted of the green algae caulerpa racemosa increase the enzymatic activity and paw edema induced by spla2 from crotalus durissus terrificus venom
description Sulfated polysaccharides derived from seaweed have shown great potential for use in the development of new drugs. In this study, we observed that a low-molecular-weight sulfated polysaccharide from Caulerpa racemosa, termed CrSP, could interact with secretory phospholipase A2 (sPLA2) isolated from Crotalus durissus terrificus venom. When native sPLA2 (14 kDa) was incubated with CrSP, they formed a molecular complex (sPLA2:CrSP) with a molecular mass of 32 kDa, approximately. Size exclusion chromatography experiments suggested that CrSP formed a stable complex with sPLA2. We belived that sPLA2 and SPCr are involved an ionic interaction between negatively charged CrSP and the positively charged basic amino acid residues of sPLA2, because this interaction induced significant changes in sPLA2 enzymatic and pharmacological activities. CrSP caused a significant increase in sPLA2 enzymatic and bactericidal activity and increased its edematogenic effect. A pharmacological assay showed that the myotoxic activity of sPLA2:CrSP is unrelated to its enzymatic activity and that sPLA2:CrSP may have a practical application as a natural antibacterial agent for use in humans and commercially raised animals.
publisher Sociedade Brasileira de Farmacognosia
publishDate 2013
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0102-695X2013000400010
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