Modulation Of The Pharmacological Effects Of Enzymatically-active Pla 2 By Btl-2, An Isolectin Isolated From The Bryothamnion Triquetrum Red Alga

dc.creatorOliveira S.C.B.
dc.creatorFonseca F.V.
dc.creatorAntunes E.
dc.creatorCamargo E.A.
dc.creatorMorganti R.P.
dc.creatorAparicio R.
dc.creatorToyama D.O.
dc.creatorBeriam L.O.S.
dc.creatorNunes E.V.
dc.creatorCavada B.S.
dc.creatorNagano C.S.
dc.creatorSampaio A.H.
dc.creatorNascimento K.S.
dc.creatorToyama M.H.
dc.date2008
dc.date2015-06-30T19:13:08Z
dc.date2015-11-26T14:39:33Z
dc.date2015-06-30T19:13:08Z
dc.date2015-11-26T14:39:33Z
dc.date.accessioned2018-03-28T21:45:18Z
dc.date.available2018-03-28T21:45:18Z
dc.identifier
dc.identifierBmc Biochemistry. , v. 9, n. 1, p. - , 2008.
dc.identifier14712091
dc.identifier10.1186/1471-2091-9-16
dc.identifierhttp://www.scopus.com/inward/record.url?eid=2-s2.0-46649109942&partnerID=40&md5=7fd6f1612c5c7e3bd9c4a020f460dc33
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/105290
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/105290
dc.identifier2-s2.0-46649109942
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1250046
dc.descriptionBackground. 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.
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dc.languageen
dc.publisher
dc.relationBMC Biochemistry
dc.rightsaberto
dc.sourceScopus
dc.titleModulation Of The Pharmacological Effects Of Enzymatically-active Pla 2 By Btl-2, An Isolectin Isolated From The Bryothamnion Triquetrum Red Alga
dc.typeArtículos de revistas


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