A C-type lectin from Bothrops jararacussu venom can adhere to extracellular matrix proteins and induce the rolling of leukocytes

Detalhes bibliográficos
Autor(a) principal: Elífio-Esposito,S. L.
Data de Publicação: 2007
Outros Autores: Hess,P. L., Moreno,A. N., Lopes-Ferreira,M., Ricart,C. A. O., Souza,M. V., Hasselman-Zielinski,F., Becker,J. A., Pereira,L. F.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: The Journal of venomous animals and toxins including tropical diseases (Online)
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992007000400009
Resumo: Purification of a lectin from Bothrops jararacussu venom (BjcuL) was carried out using agarose-D-galactose affinity gel. MALDI-TOF gave a major signal at m/z 32028, suggesting the presence of a dimmer composed of two identical subunits. Divalent cations were required for the lectin activity, as complete absence of such ions reduced hemagglutination. BjcuL was more effective at neutral pH and showed total loss of activity at pH values below 4.0 and above 9.0. Its agglutinating activity remained stable at 25°C until 60min, but increased when at 35°C for at least 15min. Adhesion assays to extracellular matrix (ECM) glycoproteins showed that the biotinylated lectin (0.039-5.0µg/100µl) was capable of binding to fibronectin and vitronectin in a dose-dependent manner. The binding was partially inhibited in the presence of D-galactose. BjcuL (1.25-10µg/30µl) potential was investigated for leukocyte rolling and adhesion to endothelial cells in living microvessels using intravital microscopy, which showed that it induced a dose-dependent increase in rolling and adherence of leukocytes, acting directly on endothelial cells of postcapillary venules. The specific association between lectins and their ligands, either on the cell surface or on the ECM, is related to a variety of biological processes. The complementary characterization of BjcuL, shown here, is useful to further understand the venom effects and as a background for future investigation for therapeutic strategies.
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spelling A C-type lectin from Bothrops jararacussu venom can adhere to extracellular matrix proteins and induce the rolling of leukocytesvenomsfibronectinsvitronectinsnakesintravital microscopyleukocytesPurification of a lectin from Bothrops jararacussu venom (BjcuL) was carried out using agarose-D-galactose affinity gel. MALDI-TOF gave a major signal at m/z 32028, suggesting the presence of a dimmer composed of two identical subunits. Divalent cations were required for the lectin activity, as complete absence of such ions reduced hemagglutination. BjcuL was more effective at neutral pH and showed total loss of activity at pH values below 4.0 and above 9.0. Its agglutinating activity remained stable at 25°C until 60min, but increased when at 35°C for at least 15min. Adhesion assays to extracellular matrix (ECM) glycoproteins showed that the biotinylated lectin (0.039-5.0µg/100µl) was capable of binding to fibronectin and vitronectin in a dose-dependent manner. The binding was partially inhibited in the presence of D-galactose. BjcuL (1.25-10µg/30µl) potential was investigated for leukocyte rolling and adhesion to endothelial cells in living microvessels using intravital microscopy, which showed that it induced a dose-dependent increase in rolling and adherence of leukocytes, acting directly on endothelial cells of postcapillary venules. The specific association between lectins and their ligands, either on the cell surface or on the ECM, is related to a variety of biological processes. The complementary characterization of BjcuL, shown here, is useful to further understand the venom effects and as a background for future investigation for therapeutic strategies.Centro de Estudos de Venenos e Animais Peçonhentos (CEVAP/UNESP)2007-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992007000400009Journal of Venomous Animals and Toxins including Tropical Diseases v.13 n.4 2007reponame:The Journal of venomous animals and toxins including tropical diseases (Online)instname:Universidade Estadual Paulista (UNESP)instacron:UNESP10.1590/S1678-91992007000400009info:eu-repo/semantics/openAccessElífio-Esposito,S. L.Hess,P. L.Moreno,A. N.Lopes-Ferreira,M.Ricart,C. A. O.Souza,M. V.Hasselman-Zielinski,F.Becker,J. A.Pereira,L. F.eng2007-12-19T00:00:00Zoai:scielo:S1678-91992007000400009Revistahttp://www.scielo.br/jvatitdPUBhttps://old.scielo.br/oai/scielo-oai.php||editorial@jvat.org.br1678-91991678-9180opendoar:2007-12-19T00:00The Journal of venomous animals and toxins including tropical diseases (Online) - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv A C-type lectin from Bothrops jararacussu venom can adhere to extracellular matrix proteins and induce the rolling of leukocytes
title A C-type lectin from Bothrops jararacussu venom can adhere to extracellular matrix proteins and induce the rolling of leukocytes
spellingShingle A C-type lectin from Bothrops jararacussu venom can adhere to extracellular matrix proteins and induce the rolling of leukocytes
Elífio-Esposito,S. L.
venoms
fibronectins
vitronectin
snakes
intravital microscopy
leukocytes
title_short A C-type lectin from Bothrops jararacussu venom can adhere to extracellular matrix proteins and induce the rolling of leukocytes
title_full A C-type lectin from Bothrops jararacussu venom can adhere to extracellular matrix proteins and induce the rolling of leukocytes
title_fullStr A C-type lectin from Bothrops jararacussu venom can adhere to extracellular matrix proteins and induce the rolling of leukocytes
title_full_unstemmed A C-type lectin from Bothrops jararacussu venom can adhere to extracellular matrix proteins and induce the rolling of leukocytes
title_sort A C-type lectin from Bothrops jararacussu venom can adhere to extracellular matrix proteins and induce the rolling of leukocytes
author Elífio-Esposito,S. L.
author_facet Elífio-Esposito,S. L.
Hess,P. L.
Moreno,A. N.
Lopes-Ferreira,M.
Ricart,C. A. O.
Souza,M. V.
Hasselman-Zielinski,F.
Becker,J. A.
Pereira,L. F.
author_role author
author2 Hess,P. L.
Moreno,A. N.
Lopes-Ferreira,M.
Ricart,C. A. O.
Souza,M. V.
Hasselman-Zielinski,F.
Becker,J. A.
Pereira,L. F.
author2_role author
author
author
author
author
author
author
author
dc.contributor.author.fl_str_mv Elífio-Esposito,S. L.
Hess,P. L.
Moreno,A. N.
Lopes-Ferreira,M.
Ricart,C. A. O.
Souza,M. V.
Hasselman-Zielinski,F.
Becker,J. A.
Pereira,L. F.
dc.subject.por.fl_str_mv venoms
fibronectins
vitronectin
snakes
intravital microscopy
leukocytes
topic venoms
fibronectins
vitronectin
snakes
intravital microscopy
leukocytes
description Purification of a lectin from Bothrops jararacussu venom (BjcuL) was carried out using agarose-D-galactose affinity gel. MALDI-TOF gave a major signal at m/z 32028, suggesting the presence of a dimmer composed of two identical subunits. Divalent cations were required for the lectin activity, as complete absence of such ions reduced hemagglutination. BjcuL was more effective at neutral pH and showed total loss of activity at pH values below 4.0 and above 9.0. Its agglutinating activity remained stable at 25°C until 60min, but increased when at 35°C for at least 15min. Adhesion assays to extracellular matrix (ECM) glycoproteins showed that the biotinylated lectin (0.039-5.0µg/100µl) was capable of binding to fibronectin and vitronectin in a dose-dependent manner. The binding was partially inhibited in the presence of D-galactose. BjcuL (1.25-10µg/30µl) potential was investigated for leukocyte rolling and adhesion to endothelial cells in living microvessels using intravital microscopy, which showed that it induced a dose-dependent increase in rolling and adherence of leukocytes, acting directly on endothelial cells of postcapillary venules. The specific association between lectins and their ligands, either on the cell surface or on the ECM, is related to a variety of biological processes. The complementary characterization of BjcuL, shown here, is useful to further understand the venom effects and as a background for future investigation for therapeutic strategies.
publishDate 2007
dc.date.none.fl_str_mv 2007-01-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992007000400009
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992007000400009
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S1678-91992007000400009
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Centro de Estudos de Venenos e Animais Peçonhentos (CEVAP/UNESP)
publisher.none.fl_str_mv Centro de Estudos de Venenos e Animais Peçonhentos (CEVAP/UNESP)
dc.source.none.fl_str_mv Journal of Venomous Animals and Toxins including Tropical Diseases v.13 n.4 2007
reponame:The Journal of venomous animals and toxins including tropical diseases (Online)
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str The Journal of venomous animals and toxins including tropical diseases (Online)
collection The Journal of venomous animals and toxins including tropical diseases (Online)
repository.name.fl_str_mv The Journal of venomous animals and toxins including tropical diseases (Online) - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv ||editorial@jvat.org.br
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