Publication:
Modulation of the pharmacological effects of enzymatically-active PLA 2 by BTL-2, an isolectin isolated from the Bryothamnion triquetrum red alga

dc.contributor.authorOliveira, Simone C.B.
dc.contributor.authorFonseca, Fabiana V.
dc.contributor.authorAntunes, Edson
dc.contributor.authorCamargo, Enilton A.
dc.contributor.authorMorganti, Rafael P.
dc.contributor.authorAparício, Ricardo
dc.contributor.authorToyama, Daniela O.
dc.contributor.authorBeriam, Luís O.S.
dc.contributor.authorNunes, Eudismar V.
dc.contributor.authorCavada, Benildo S.
dc.contributor.authorNagano, Celso S.
dc.contributor.authorSampaio, Alexandre H.
dc.contributor.authorNascimento, Kyria S.
dc.contributor.authorToyama, Marcos H. [UNESP]
dc.contributor.institutionUniversidade Estadual de Campinas (UNICAMP)
dc.contributor.institutionUniversity of Mackenzie
dc.contributor.institutionBiological Institute
dc.contributor.institutionIBV
dc.contributor.institutionFederal University of Ceará
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-27T11:23:36Z
dc.date.available2014-05-27T11:23:36Z
dc.date.issued2008-07-11
dc.description.abstractBackground. An interaction between lectins from marine algae and PLA 2 from rattlesnake was suggested some years ago. We, herein, studied the effects elicited by a small isolectin (BTL-2), isolated from Bryothamnion triquetrum, on the pharmacological and biological activities of a PLA 2 isolated from rattlesnake venom (Crotalus durissus cascavella), to better understand the enzymatic and pharmacological mechanisms of the PLA 2 and its complex. Results. This PLA2 consisted of 122 amino acids (approximate molecular mass of 14 kDa), its pI was estimated to be 8.3, and its amino acid sequence shared a high degree of similarity with that of other neurotoxic and enzymatically-active PLA2s. BTL-2 had a molecular mass estimated in approximately 9 kDa and was characterized as a basic protein. In addition, BTL-2 did not exhibit any enzymatic activity. The PLA2 and BTL-2 formed a stable heterodimer with a molecular mass of approximately 24-26 kDa, estimated by molecular exclusion HPLC. In the presence of BTL-2, we observed a significant increase in PLA2 activity, 23% higher than that of PLA2 alone. BTL-2 demonstrated an inhibition of 98% in the growth of the Gram-positive bacterial strain, Clavibacter michiganensis michiganensis (Cmm), but only 9.8% inhibition of the Gram-negative bacterial strain, Xanthomonas axonopodis pv passiflorae (Xap). PLA2 decreased bacterial growth by 27.3% and 98.5% for Xap and Cmm, respectively, while incubating these two proteins with PLA2-BTL-2 inhibited their growths by 36.2% for Xap and 98.5% for Cmm. PLA2 significantly induced platelet aggregation in washed platelets, whereas BTL-2 did not induce significant platelet aggregation in any assay. However, BTL-2 significantly inhibited platelet aggregation induced by PLA2. In addition, PLA 2 exhibited strong oedematogenic activity, which was decreased in the presence of BTL-2. BTL-2 alone did not induce oedema and did not decrease or abolish the oedema induced by the 48/80 compound. Conclusion. 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. In addition, we describe for the first time an interaction between two different molecules, which form a stable complex with significant changes in their original biological action. This opens new possibilities for understanding the function and action of crude venom, an extremely complex mixture of different molecules. © 2008 Oliveira et al; licensee BioMed Central Ltd.en
dc.description.affiliationBiochemistry Department Biology Institute UNICAMP, Campinas, São Paulo
dc.description.affiliationPharmacology Department University of Medical Science UNICAMP, Campinas, São Paulo
dc.description.affiliationChemistry Institute UNICAMP, Campinas, São Paulo
dc.description.affiliationUniversity of Biological and EXaperimental Sciences University of Mackenzie, São Paulo, São Paulo
dc.description.affiliationLaboratory of Vegetal Bacteriology Experimental Center Biological Institute, Campinas, São Paulo
dc.description.affiliationInstitute of Biomedicine of Valencia IBV, Valencia
dc.description.affiliationLab. of Marine Biochemistry -BioMar-Lab. Fishing Engeneer Department Federal University of Ceará, Fortaleza, Ceará
dc.description.affiliationUNESP Litoral Paulista Campus, São Vicente, São Paulo
dc.description.affiliationUnespUNESP Litoral Paulista Campus, São Vicente, São Paulo
dc.identifierhttp://dx.doi.org/10.1186/1471-2091-9-16
dc.identifier.citationBMC Biochemistry, v. 9, n. 1, 2008.
dc.identifier.doi10.1186/1471-2091-9-16
dc.identifier.file2-s2.0-46649109942.pdf
dc.identifier.issn1471-2091
dc.identifier.scopus2-s2.0-46649109942
dc.identifier.urihttp://hdl.handle.net/11449/70479
dc.language.isoeng
dc.relation.ispartofBMC Biochemistry
dc.relation.ispartofjcr1.595
dc.relation.ispartofsjr0,708
dc.rights.accessRightsAcesso aberto
dc.sourceScopus
dc.subjectbryothamnion triquerum lectin 2
dc.subjectheterodimer
dc.subjectlectin
dc.subjectphospholipase A2
dc.subjectsnake venom
dc.subjectalgal protein
dc.subjectamino acid sequence
dc.subjectbacterial growth
dc.subjectbacterial strain
dc.subjectcontrolled study
dc.subjectedema
dc.subjectenzyme activity
dc.subjectGram positive bacterium
dc.subjectgrowth inhibition
dc.subjecthigh performance liquid chromatography
dc.subjectmethodology
dc.subjectmolecular weight
dc.subjectnonhuman
dc.subjectprotein analysis
dc.subjectprotein isolation
dc.subjectred alga
dc.subjectthrombocyte aggregation
dc.subjectXanthomonas axonopodis
dc.subjectanimal
dc.subjectchemistry
dc.subjectenzymology
dc.subjectisolation and purification
dc.subjectmetabolism
dc.subjectmolecular genetics
dc.subjectalgae
dc.subjectBacteria (microorganisms)
dc.subjectBryothamnion triquetrum
dc.subjectClavibacter michiganensis subsp. michiganensis
dc.subjectCrotalus durissus cascavella
dc.subjectNegibacteria
dc.subjectPosibacteria
dc.subjectRhodophyta
dc.subjectAlgae, Red
dc.subjectAlgal Proteins
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectChromatography, High Pressure Liquid
dc.subjectCrotalid Venoms
dc.subjectLectins
dc.subjectMolecular Sequence Data
dc.subjectPhospholipases A2
dc.titleModulation of the pharmacological effects of enzymatically-active PLA 2 by BTL-2, an isolectin isolated from the Bryothamnion triquetrum red algaen
dc.typeArtigo
dcterms.licensehttp://www.biomedcentral.com/about/license
dspace.entity.typePublication
unesp.campusUniversidade Estadual Paulista (UNESP), Instituto de Biociências, São Vicentept
unesp.departmentCiências Biológicas - IBCLPpt

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