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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 alga

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 f...

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Autores principales: Oliveira, Simone CB, Fonseca, Fabiana V, Antunes, Edson, Camargo, Enilton A, Morganti, Rafael P, Aparício, Ricardo, Toyama, Daniela O, Beriam, Luís OS, Nunes, Eudismar V, Cavada, Benildo S, Nagano, Celso S, Sampaio, Alexandre H, Nascimento, Kyria S, Toyama, Marcos H
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2443151/
https://www.ncbi.nlm.nih.gov/pubmed/18534036
http://dx.doi.org/10.1186/1471-2091-9-16
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author Oliveira, Simone CB
Fonseca, Fabiana V
Antunes, Edson
Camargo, Enilton A
Morganti, Rafael P
Aparício, Ricardo
Toyama, Daniela O
Beriam, Luís OS
Nunes, Eudismar V
Cavada, Benildo S
Nagano, Celso S
Sampaio, Alexandre H
Nascimento, Kyria S
Toyama, Marcos H
author_facet Oliveira, Simone CB
Fonseca, Fabiana V
Antunes, Edson
Camargo, Enilton A
Morganti, Rafael P
Aparício, Ricardo
Toyama, Daniela O
Beriam, Luís OS
Nunes, Eudismar V
Cavada, Benildo S
Nagano, Celso S
Sampaio, Alexandre H
Nascimento, Kyria S
Toyama, Marcos H
author_sort Oliveira, Simone CB
collection PubMed
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 PLA(2 )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 PLA(2)s. 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 PLA(2 )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 PLA(2 )activity, 23% higher than that of PLA(2 )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). PLA(2 )decreased bacterial growth by 27.3% and 98.5% for Xap and Cmm, respectively, while incubating these two proteins with PLA(2)-BTL-2 inhibited their growths by 36.2% for Xap and 98.5% for Cmm. PLA(2 )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 PLA(2). 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 PLA(2)-BTL-2 complex strongly suggest that the pharmacological activity of this PLA(2 )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.
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spelling pubmed-24431512008-07-04 Modulation of the pharmacological effects of enzymatically-active PLA(2 )by BTL-2, an isolectin isolated from the Bryothamnion triquetrum red alga Oliveira, Simone CB Fonseca, Fabiana V Antunes, Edson Camargo, Enilton A Morganti, Rafael P Aparício, Ricardo Toyama, Daniela O Beriam, Luís OS Nunes, Eudismar V Cavada, Benildo S Nagano, Celso S Sampaio, Alexandre H Nascimento, Kyria S Toyama, Marcos H BMC Biochem Research Article 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 PLA(2 )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 PLA(2)s. 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 PLA(2 )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 PLA(2 )activity, 23% higher than that of PLA(2 )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). PLA(2 )decreased bacterial growth by 27.3% and 98.5% for Xap and Cmm, respectively, while incubating these two proteins with PLA(2)-BTL-2 inhibited their growths by 36.2% for Xap and 98.5% for Cmm. PLA(2 )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 PLA(2). 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 PLA(2)-BTL-2 complex strongly suggest that the pharmacological activity of this PLA(2 )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. BioMed Central 2008-06-06 /pmc/articles/PMC2443151/ /pubmed/18534036 http://dx.doi.org/10.1186/1471-2091-9-16 Text en Copyright © 2008 Oliveira et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Oliveira, Simone CB
Fonseca, Fabiana V
Antunes, Edson
Camargo, Enilton A
Morganti, Rafael P
Aparício, Ricardo
Toyama, Daniela O
Beriam, Luís OS
Nunes, Eudismar V
Cavada, Benildo S
Nagano, Celso S
Sampaio, Alexandre H
Nascimento, Kyria S
Toyama, Marcos H
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
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_short 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
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2443151/
https://www.ncbi.nlm.nih.gov/pubmed/18534036
http://dx.doi.org/10.1186/1471-2091-9-16
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