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Sulfated polysaccharide extracted of the green algae Caulerpa racemosa increase the enzymatic activity and paw edema induced by sPLA2 from Crotalus durissus terrificus venom
Pires, Camila L.; Rodrigues, Selma D.; Bristot, Daniel; Gaeta, Henrique Hessel; Toyama, Daniela de Oliveira; Farias, Wladimir Ronald Lobo; Toyama, Marcos Hikari.
Affiliation
  • Pires, Camila L.; Universidade Estadual Paulista. Laboratório de Biologia Molecular e Peptídeos. BR
  • Rodrigues, Selma D.; Universidade Estadual Paulista. Laboratório de Biologia Molecular e Peptídeos. BR
  • Bristot, Daniel; Universidade Estadual Paulista. Laboratório de Biologia Molecular e Peptídeos. BR
  • Gaeta, Henrique Hessel; Universidade Estadual Paulista. Laboratório de Biologia Molecular e Peptídeos. BR
  • Toyama, Daniela de Oliveira; Universidade Estadual Paulista. Laboratório de Biologia Molecular e Peptídeos. BR
  • Farias, Wladimir Ronald Lobo; Universidade Estadual Paulista. Laboratório de Biologia Molecular e Peptídeos. BR
  • Toyama, Marcos Hikari; Universidade Estadual Paulista. Laboratório de Biologia Molecular e Peptídeos. BR
Rev. bras. farmacogn ; 23(4): 635-643, Aug. 2013. graf
Article in English | LILACS | ID: lil-686636
Responsible library: BR1.1
ABSTRACT
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 (sPLA2CrSP) 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 sPLA2CrSP is unrelated to its enzymatic activity and that sPLA2CrSP may have a practical application as a natural antibacterial agent for use in humans and commercially raised animals.


Full text: Available Collection: International databases Database: LILACS Language: English Journal: Rev. bras. farmacogn Journal subject: Pharmacy Year: 2013 Document type: Article / Project document Affiliation country: Brazil Institution/Affiliation country: Universidade Estadual Paulista/BR

Full text: Available Collection: International databases Database: LILACS Language: English Journal: Rev. bras. farmacogn Journal subject: Pharmacy Year: 2013 Document type: Article / Project document Affiliation country: Brazil Institution/Affiliation country: Universidade Estadual Paulista/BR
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