Modulation of the pharmacological effects of enzymatically-active PLA 2 by BTL-2, an isolectin isolated from the Bryothamnion triquetrum red alga
Autor(a) principal: | |
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Data de Publicação: | 2008 |
Outros Autores: | , , , , , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1186/1471-2091-9-16 http://hdl.handle.net/11449/70479 |
Resumo: | Background. 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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Modulation of the pharmacological effects of enzymatically-active PLA 2 by BTL-2, an isolectin isolated from the Bryothamnion triquetrum red algabryothamnion triquerum lectin 2heterodimerlectinphospholipase A2snake venomalgal proteinamino acid sequencebacterial growthbacterial straincontrolled studyedemaenzyme activityGram positive bacteriumgrowth inhibitionhigh performance liquid chromatographymethodologymolecular weightnonhumanprotein analysisprotein isolationred algathrombocyte aggregationXanthomonas axonopodisanimalchemistryenzymologyisolation and purificationmetabolismmolecular geneticsalgaeBacteria (microorganisms)Bryothamnion triquetrumClavibacter michiganensis subsp. michiganensisCrotalus durissus cascavellaNegibacteriaPosibacteriaRhodophytaAlgae, RedAlgal ProteinsAmino Acid SequenceAnimalsChromatography, High Pressure LiquidCrotalid VenomsLectinsMolecular Sequence DataPhospholipases A2Background. 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.Biochemistry Department Biology Institute UNICAMP, Campinas, São PauloPharmacology Department University of Medical Science UNICAMP, Campinas, São PauloChemistry Institute UNICAMP, Campinas, São PauloUniversity of Biological and EXaperimental Sciences University of Mackenzie, São Paulo, São PauloLaboratory of Vegetal Bacteriology Experimental Center Biological Institute, Campinas, São PauloInstitute of Biomedicine of Valencia IBV, ValenciaLab. of Marine Biochemistry -BioMar-Lab. Fishing Engeneer Department Federal University of Ceará, Fortaleza, CearáUNESP Litoral Paulista Campus, São Vicente, São PauloUNESP Litoral Paulista Campus, São Vicente, São PauloUniversidade Estadual de Campinas (UNICAMP)University of MackenzieBiological InstituteIBVFederal University of CearáUniversidade Estadual Paulista (Unesp)Oliveira, Simone C.B.Fonseca, Fabiana V.Antunes, EdsonCamargo, Enilton A.Morganti, Rafael P.Aparício, RicardoToyama, Daniela O.Beriam, Luís O.S.Nunes, Eudismar V.Cavada, Benildo S.Nagano, Celso S.Sampaio, Alexandre H.Nascimento, Kyria S.Toyama, Marcos H. [UNESP]2014-05-27T11:23:36Z2014-05-27T11:23:36Z2008-07-11info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://dx.doi.org/10.1186/1471-2091-9-16BMC Biochemistry, v. 9, n. 1, 2008.1471-2091http://hdl.handle.net/11449/7047910.1186/1471-2091-9-162-s2.0-466491099422-s2.0-46649109942.pdfScopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengBMC Biochemistry1.5950,708info:eu-repo/semantics/openAccess2023-11-02T06:08:52Zoai:repositorio.unesp.br:11449/70479Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T16:42:55.198566Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Modulation of the pharmacological effects of enzymatically-active PLA 2 by BTL-2, an isolectin isolated from the Bryothamnion triquetrum red alga |
title |
Modulation of the pharmacological effects of enzymatically-active PLA 2 by BTL-2, an isolectin isolated from the Bryothamnion triquetrum red alga |
spellingShingle |
Modulation of the pharmacological effects of enzymatically-active PLA 2 by BTL-2, an isolectin isolated from the Bryothamnion triquetrum red alga Oliveira, Simone C.B. bryothamnion triquerum lectin 2 heterodimer lectin phospholipase A2 snake venom algal protein amino acid sequence bacterial growth bacterial strain controlled study edema enzyme activity Gram positive bacterium growth inhibition high performance liquid chromatography methodology molecular weight nonhuman protein analysis protein isolation red alga thrombocyte aggregation Xanthomonas axonopodis animal chemistry enzymology isolation and purification metabolism molecular genetics algae Bacteria (microorganisms) Bryothamnion triquetrum Clavibacter michiganensis subsp. michiganensis Crotalus durissus cascavella Negibacteria Posibacteria Rhodophyta Algae, Red Algal Proteins Amino Acid Sequence Animals Chromatography, High Pressure Liquid Crotalid Venoms Lectins Molecular Sequence Data Phospholipases A2 |
title_short |
Modulation of the pharmacological effects of enzymatically-active PLA 2 by BTL-2, an isolectin isolated from the Bryothamnion triquetrum red alga |
title_full |
Modulation of the pharmacological effects of enzymatically-active PLA 2 by BTL-2, an isolectin isolated from the Bryothamnion triquetrum red alga |
title_fullStr |
Modulation of the pharmacological effects of enzymatically-active PLA 2 by BTL-2, an isolectin isolated from the Bryothamnion triquetrum red alga |
title_full_unstemmed |
Modulation of the pharmacological effects of enzymatically-active PLA 2 by BTL-2, an isolectin isolated from the Bryothamnion triquetrum red alga |
title_sort |
Modulation of the pharmacological effects of enzymatically-active PLA 2 by BTL-2, an isolectin isolated from the Bryothamnion triquetrum red alga |
author |
Oliveira, Simone C.B. |
author_facet |
Oliveira, Simone C.B. Fonseca, Fabiana V. Antunes, Edson Camargo, Enilton A. Morganti, Rafael P. Aparício, Ricardo Toyama, Daniela O. Beriam, Luís O.S. Nunes, Eudismar V. Cavada, Benildo S. Nagano, Celso S. Sampaio, Alexandre H. Nascimento, Kyria S. Toyama, Marcos H. [UNESP] |
author_role |
author |
author2 |
Fonseca, Fabiana V. Antunes, Edson Camargo, Enilton A. Morganti, Rafael P. Aparício, Ricardo Toyama, Daniela O. Beriam, Luís O.S. Nunes, Eudismar V. Cavada, Benildo S. Nagano, Celso S. Sampaio, Alexandre H. Nascimento, Kyria S. Toyama, Marcos H. [UNESP] |
author2_role |
author author author author author author author author author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual de Campinas (UNICAMP) University of Mackenzie Biological Institute IBV Federal University of Ceará Universidade Estadual Paulista (Unesp) |
dc.contributor.author.fl_str_mv |
Oliveira, Simone C.B. Fonseca, Fabiana V. Antunes, Edson Camargo, Enilton A. Morganti, Rafael P. Aparício, Ricardo Toyama, Daniela O. Beriam, Luís O.S. Nunes, Eudismar V. Cavada, Benildo S. Nagano, Celso S. Sampaio, Alexandre H. Nascimento, Kyria S. Toyama, Marcos H. [UNESP] |
dc.subject.por.fl_str_mv |
bryothamnion triquerum lectin 2 heterodimer lectin phospholipase A2 snake venom algal protein amino acid sequence bacterial growth bacterial strain controlled study edema enzyme activity Gram positive bacterium growth inhibition high performance liquid chromatography methodology molecular weight nonhuman protein analysis protein isolation red alga thrombocyte aggregation Xanthomonas axonopodis animal chemistry enzymology isolation and purification metabolism molecular genetics algae Bacteria (microorganisms) Bryothamnion triquetrum Clavibacter michiganensis subsp. michiganensis Crotalus durissus cascavella Negibacteria Posibacteria Rhodophyta Algae, Red Algal Proteins Amino Acid Sequence Animals Chromatography, High Pressure Liquid Crotalid Venoms Lectins Molecular Sequence Data Phospholipases A2 |
topic |
bryothamnion triquerum lectin 2 heterodimer lectin phospholipase A2 snake venom algal protein amino acid sequence bacterial growth bacterial strain controlled study edema enzyme activity Gram positive bacterium growth inhibition high performance liquid chromatography methodology molecular weight nonhuman protein analysis protein isolation red alga thrombocyte aggregation Xanthomonas axonopodis animal chemistry enzymology isolation and purification metabolism molecular genetics algae Bacteria (microorganisms) Bryothamnion triquetrum Clavibacter michiganensis subsp. michiganensis Crotalus durissus cascavella Negibacteria Posibacteria Rhodophyta Algae, Red Algal Proteins Amino Acid Sequence Animals Chromatography, High Pressure Liquid Crotalid Venoms Lectins Molecular Sequence Data Phospholipases A2 |
description |
Background. 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. |
publishDate |
2008 |
dc.date.none.fl_str_mv |
2008-07-11 2014-05-27T11:23:36Z 2014-05-27T11:23:36Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1186/1471-2091-9-16 BMC Biochemistry, v. 9, n. 1, 2008. 1471-2091 http://hdl.handle.net/11449/70479 10.1186/1471-2091-9-16 2-s2.0-46649109942 2-s2.0-46649109942.pdf |
url |
http://dx.doi.org/10.1186/1471-2091-9-16 http://hdl.handle.net/11449/70479 |
identifier_str_mv |
BMC Biochemistry, v. 9, n. 1, 2008. 1471-2091 10.1186/1471-2091-9-16 2-s2.0-46649109942 2-s2.0-46649109942.pdf |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
BMC Biochemistry 1.595 0,708 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
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1808128690915115008 |