Purification and biological effects of a C-type lectin isolated from Bothrops moojeni
Autor(a) principal: | |
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Data de Publicação: | 2010 |
Outros Autores: | , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1590/S1678-91992010000300016 http://hdl.handle.net/11449/226101 |
Resumo: | Snake venom proteins from the C-type lectin family have very distinct biological activities despite their highly conserved primary structure, which is homologous to the carbohydrate recognition region of true C-type lectins. We purified a lectin-like protein (BmLec) from Bothrops moojeni venom and investigated its effect on platelet aggregation, insulin secretion, antibacterial activity, and isolated kidney cells. The BmLec was purified using two chromatographic steps: affinity chromatography and reverse phase high performance liquid chromatography (HPLC). BmLec showed a dose-dependent platelet aggregation and significantly decreased the bacterial growth rate in approximately 15%. During scanning electron microscopy, the profile of Xanthomonas axonopodis pv. passiflorae treated with lectin disclosed a high vesiculation and membrane rupture. BmLec induced a strong and significant increase in insulin secretion at 2.8 and 16.7 mM glucose concentrations, and this effect was seen in the presence of EGTA in both experiments. BmLec (10 μg/mL) increased the perfusion pressure, renal vascular resistance and urinary flow. The glomerular filtration rate and percentages of sodium, potassium and chloride tubular transport were reduced at 60 minutes of perfusion. Renal alterations caused by BmLec were completely inhibited by indomethacin in all evaluated parameters. In conclusion, the C-type lectin isolated from Bothrops moojeni affected platelet aggregation, insulin secretion, antibacterial activity and isolated kidney function. © CEVAP 2010. |
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Purification and biological effects of a C-type lectin isolated from Bothrops moojeniAntibacterial activityBothrops moojeniInsulinKidneyPlatelet aggregationSnake venom proteins from the C-type lectin family have very distinct biological activities despite their highly conserved primary structure, which is homologous to the carbohydrate recognition region of true C-type lectins. We purified a lectin-like protein (BmLec) from Bothrops moojeni venom and investigated its effect on platelet aggregation, insulin secretion, antibacterial activity, and isolated kidney cells. The BmLec was purified using two chromatographic steps: affinity chromatography and reverse phase high performance liquid chromatography (HPLC). BmLec showed a dose-dependent platelet aggregation and significantly decreased the bacterial growth rate in approximately 15%. During scanning electron microscopy, the profile of Xanthomonas axonopodis pv. passiflorae treated with lectin disclosed a high vesiculation and membrane rupture. BmLec induced a strong and significant increase in insulin secretion at 2.8 and 16.7 mM glucose concentrations, and this effect was seen in the presence of EGTA in both experiments. BmLec (10 μg/mL) increased the perfusion pressure, renal vascular resistance and urinary flow. The glomerular filtration rate and percentages of sodium, potassium and chloride tubular transport were reduced at 60 minutes of perfusion. Renal alterations caused by BmLec were completely inhibited by indomethacin in all evaluated parameters. In conclusion, the C-type lectin isolated from Bothrops moojeni affected platelet aggregation, insulin secretion, antibacterial activity and isolated kidney function. © CEVAP 2010.Department of Physiology and Pharmacology Federal University of Ceará, Fortaleza, Ceará StateDepartment of Clinical and Toxicological Analyses Federal University of Ceará, Fortaleza, Ceará StateSão Paulo Experimental Coast Campus São Paulo State University (UNESP - Univ Estadual Paulista), São Vicente, São Paulo StateDepartment of Histology Institute of Biology State University of Campinas, Campinas, São Paulo StateLaboratory of Plant Microbiology Experimental Center Biological Institute, Campinas, São Paulo StateSão Paulo Experimental Coast Campus São Paulo State University (UNESP - Univ Estadual Paulista), São Vicente, São Paulo StateFederal University of CearáUniversidade Estadual Paulista (UNESP)Universidade Estadual de Campinas (UNICAMP)Biological InstituteBarbosa, P. S.F.Martins, A. M.C.Toyama, M. H. [UNESP]Joazeiro, P. P.Beriam, L. O.S.Fonteles, M. C.Monteiro, H. A.S.2022-04-28T21:25:28Z2022-04-28T21:25:28Z2010-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article493-504http://dx.doi.org/10.1590/S1678-91992010000300016Journal of Venomous Animals and Toxins Including Tropical Diseases, v. 16, n. 3, p. 493-504, 2010.1678-9199http://hdl.handle.net/11449/22610110.1590/S1678-919920100003000162-s2.0-78049479441Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengJournal of Venomous Animals and Toxins Including Tropical Diseasesinfo:eu-repo/semantics/openAccess2022-04-28T21:25:29Zoai:repositorio.unesp.br:11449/226101Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-06T00:06:57.124597Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Purification and biological effects of a C-type lectin isolated from Bothrops moojeni |
title |
Purification and biological effects of a C-type lectin isolated from Bothrops moojeni |
spellingShingle |
Purification and biological effects of a C-type lectin isolated from Bothrops moojeni Barbosa, P. S.F. Antibacterial activity Bothrops moojeni Insulin Kidney Platelet aggregation |
title_short |
Purification and biological effects of a C-type lectin isolated from Bothrops moojeni |
title_full |
Purification and biological effects of a C-type lectin isolated from Bothrops moojeni |
title_fullStr |
Purification and biological effects of a C-type lectin isolated from Bothrops moojeni |
title_full_unstemmed |
Purification and biological effects of a C-type lectin isolated from Bothrops moojeni |
title_sort |
Purification and biological effects of a C-type lectin isolated from Bothrops moojeni |
author |
Barbosa, P. S.F. |
author_facet |
Barbosa, P. S.F. Martins, A. M.C. Toyama, M. H. [UNESP] Joazeiro, P. P. Beriam, L. O.S. Fonteles, M. C. Monteiro, H. A.S. |
author_role |
author |
author2 |
Martins, A. M.C. Toyama, M. H. [UNESP] Joazeiro, P. P. Beriam, L. O.S. Fonteles, M. C. Monteiro, H. A.S. |
author2_role |
author author author author author author |
dc.contributor.none.fl_str_mv |
Federal University of Ceará Universidade Estadual Paulista (UNESP) Universidade Estadual de Campinas (UNICAMP) Biological Institute |
dc.contributor.author.fl_str_mv |
Barbosa, P. S.F. Martins, A. M.C. Toyama, M. H. [UNESP] Joazeiro, P. P. Beriam, L. O.S. Fonteles, M. C. Monteiro, H. A.S. |
dc.subject.por.fl_str_mv |
Antibacterial activity Bothrops moojeni Insulin Kidney Platelet aggregation |
topic |
Antibacterial activity Bothrops moojeni Insulin Kidney Platelet aggregation |
description |
Snake venom proteins from the C-type lectin family have very distinct biological activities despite their highly conserved primary structure, which is homologous to the carbohydrate recognition region of true C-type lectins. We purified a lectin-like protein (BmLec) from Bothrops moojeni venom and investigated its effect on platelet aggregation, insulin secretion, antibacterial activity, and isolated kidney cells. The BmLec was purified using two chromatographic steps: affinity chromatography and reverse phase high performance liquid chromatography (HPLC). BmLec showed a dose-dependent platelet aggregation and significantly decreased the bacterial growth rate in approximately 15%. During scanning electron microscopy, the profile of Xanthomonas axonopodis pv. passiflorae treated with lectin disclosed a high vesiculation and membrane rupture. BmLec induced a strong and significant increase in insulin secretion at 2.8 and 16.7 mM glucose concentrations, and this effect was seen in the presence of EGTA in both experiments. BmLec (10 μg/mL) increased the perfusion pressure, renal vascular resistance and urinary flow. The glomerular filtration rate and percentages of sodium, potassium and chloride tubular transport were reduced at 60 minutes of perfusion. Renal alterations caused by BmLec were completely inhibited by indomethacin in all evaluated parameters. In conclusion, the C-type lectin isolated from Bothrops moojeni affected platelet aggregation, insulin secretion, antibacterial activity and isolated kidney function. © CEVAP 2010. |
publishDate |
2010 |
dc.date.none.fl_str_mv |
2010-01-01 2022-04-28T21:25:28Z 2022-04-28T21:25:28Z |
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/10.1590/S1678-91992010000300016 Journal of Venomous Animals and Toxins Including Tropical Diseases, v. 16, n. 3, p. 493-504, 2010. 1678-9199 http://hdl.handle.net/11449/226101 10.1590/S1678-91992010000300016 2-s2.0-78049479441 |
url |
http://dx.doi.org/10.1590/S1678-91992010000300016 http://hdl.handle.net/11449/226101 |
identifier_str_mv |
Journal of Venomous Animals and Toxins Including Tropical Diseases, v. 16, n. 3, p. 493-504, 2010. 1678-9199 10.1590/S1678-91992010000300016 2-s2.0-78049479441 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Journal of Venomous Animals and Toxins Including Tropical Diseases |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
493-504 |
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 |
|
_version_ |
1808129585532895232 |