The first serine protease inhibitor from Lasiodora sp (Araneae: Theraphosidae) hemocytes
Autor(a) principal: | |
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Data de Publicação: | 2011 |
Outros Autores: | , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNIFESP |
Texto Completo: | http://dx.doi.org/10.1016/j.procbio.2011.09.012 http://repositorio.unifesp.br/handle/11600/34246 |
Resumo: | This work reports, for the first time, the purification, characterization and antibacterial activity of an elastase inhibitor from Lasiodora sp. hemocytes (ElLaH). the hemocyte extract inhibited chymotrypsin (22%). trypsin (44%), tissue plasminogen activator (52%), urokinase (58%) and human neutrophil elastase (99%). ElLaH was purified by Trypsin-Sepharose column and RP-HPLC. SDS-PAGE of ElLaH revealed a molecular mass of 8 kDa and MALDI-TOF mass spectrometry revealed a single molecular mass of 8274 Da. the amino terminal sequence determined was LPC(PF)PYQQELTC. the dissociation constant (K) for human neutrophil elastase was 0.32 nM. Hemocyte extract exerted antibacterial effect on Bacillus subtilis and Enterococcus faecalis, while ElLaH was only active against E. faecalis. Currently, Lasiodora sp. is undergoing a systematic review and this study contributes to molecular characterization of the genus. in addition, the results suggest that serine protease inhibitors expressed in Lasiodora sp. hemocytes may be involved in the defense against bacterial infection. (C) 2011 Elsevier B.V. All rights reserved. |
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The first serine protease inhibitor from Lasiodora sp (Araneae: Theraphosidae) hemocytesSerine protease inhibitorAntibacterial activityHemocytesLasiodora sp.SpiderThis work reports, for the first time, the purification, characterization and antibacterial activity of an elastase inhibitor from Lasiodora sp. hemocytes (ElLaH). the hemocyte extract inhibited chymotrypsin (22%). trypsin (44%), tissue plasminogen activator (52%), urokinase (58%) and human neutrophil elastase (99%). ElLaH was purified by Trypsin-Sepharose column and RP-HPLC. SDS-PAGE of ElLaH revealed a molecular mass of 8 kDa and MALDI-TOF mass spectrometry revealed a single molecular mass of 8274 Da. the amino terminal sequence determined was LPC(PF)PYQQELTC. the dissociation constant (K) for human neutrophil elastase was 0.32 nM. Hemocyte extract exerted antibacterial effect on Bacillus subtilis and Enterococcus faecalis, while ElLaH was only active against E. faecalis. Currently, Lasiodora sp. is undergoing a systematic review and this study contributes to molecular characterization of the genus. in addition, the results suggest that serine protease inhibitors expressed in Lasiodora sp. hemocytes may be involved in the defense against bacterial infection. (C) 2011 Elsevier B.V. All rights reserved.Univ Fed Pernambuco, Dept Bioquim, Recife, PE, BrazilUniversidade Federal de São Paulo, Dept Bioquim, São Paulo, BrazilUniv Pernambuco, Dept Ciencias Fisiol, Recife, PE, BrazilUniversidade Federal de São Paulo, Dept Bioquim, São Paulo, BrazilWeb of ScienceConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Fundacao de Amparo a Ciencia e Tecnologia do Estado de Pernambuco (FACEPE)Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Elsevier B.V.Universidade Federal de Pernambuco (UFPE)Universidade Federal de São Paulo (UNIFESP)Univ PernambucoSoares, TatianaFerreira, Felipe Roberto BorbaGomes, Francis SoaresCoelho, Luana Cassandra Breitenbach BarrosoTorquato, Ricardo José Soares [UNIFESP]Napoleão, Thiago HenriqueCavalcanti, Maria do Socorro de MendonçaTanaka, Aparecida Sadae [UNIFESP]Paiva, Patricia Maria Guedes2016-01-24T14:17:28Z2016-01-24T14:17:28Z2011-12-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion2317-2321application/pdfhttp://dx.doi.org/10.1016/j.procbio.2011.09.012Process Biochemistry. Oxford: Elsevier B.V., v. 46, n. 12, p. 2317-2321, 2011.10.1016/j.procbio.2011.09.012WOS000297832000014.pdf1359-5113http://repositorio.unifesp.br/handle/11600/34246WOS:000297832000014engProcess Biochemistryinfo:eu-repo/semantics/openAccesshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policyreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP2024-07-31T22:51:52Zoai:repositorio.unifesp.br/:11600/34246Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestbiblioteca.csp@unifesp.bropendoar:34652024-07-31T22:51:52Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.none.fl_str_mv |
The first serine protease inhibitor from Lasiodora sp (Araneae: Theraphosidae) hemocytes |
title |
The first serine protease inhibitor from Lasiodora sp (Araneae: Theraphosidae) hemocytes |
spellingShingle |
The first serine protease inhibitor from Lasiodora sp (Araneae: Theraphosidae) hemocytes Soares, Tatiana Serine protease inhibitor Antibacterial activity Hemocytes Lasiodora sp. Spider |
title_short |
The first serine protease inhibitor from Lasiodora sp (Araneae: Theraphosidae) hemocytes |
title_full |
The first serine protease inhibitor from Lasiodora sp (Araneae: Theraphosidae) hemocytes |
title_fullStr |
The first serine protease inhibitor from Lasiodora sp (Araneae: Theraphosidae) hemocytes |
title_full_unstemmed |
The first serine protease inhibitor from Lasiodora sp (Araneae: Theraphosidae) hemocytes |
title_sort |
The first serine protease inhibitor from Lasiodora sp (Araneae: Theraphosidae) hemocytes |
author |
Soares, Tatiana |
author_facet |
Soares, Tatiana Ferreira, Felipe Roberto Borba Gomes, Francis Soares Coelho, Luana Cassandra Breitenbach Barroso Torquato, Ricardo José Soares [UNIFESP] Napoleão, Thiago Henrique Cavalcanti, Maria do Socorro de Mendonça Tanaka, Aparecida Sadae [UNIFESP] Paiva, Patricia Maria Guedes |
author_role |
author |
author2 |
Ferreira, Felipe Roberto Borba Gomes, Francis Soares Coelho, Luana Cassandra Breitenbach Barroso Torquato, Ricardo José Soares [UNIFESP] Napoleão, Thiago Henrique Cavalcanti, Maria do Socorro de Mendonça Tanaka, Aparecida Sadae [UNIFESP] Paiva, Patricia Maria Guedes |
author2_role |
author author author author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Federal de Pernambuco (UFPE) Universidade Federal de São Paulo (UNIFESP) Univ Pernambuco |
dc.contributor.author.fl_str_mv |
Soares, Tatiana Ferreira, Felipe Roberto Borba Gomes, Francis Soares Coelho, Luana Cassandra Breitenbach Barroso Torquato, Ricardo José Soares [UNIFESP] Napoleão, Thiago Henrique Cavalcanti, Maria do Socorro de Mendonça Tanaka, Aparecida Sadae [UNIFESP] Paiva, Patricia Maria Guedes |
dc.subject.por.fl_str_mv |
Serine protease inhibitor Antibacterial activity Hemocytes Lasiodora sp. Spider |
topic |
Serine protease inhibitor Antibacterial activity Hemocytes Lasiodora sp. Spider |
description |
This work reports, for the first time, the purification, characterization and antibacterial activity of an elastase inhibitor from Lasiodora sp. hemocytes (ElLaH). the hemocyte extract inhibited chymotrypsin (22%). trypsin (44%), tissue plasminogen activator (52%), urokinase (58%) and human neutrophil elastase (99%). ElLaH was purified by Trypsin-Sepharose column and RP-HPLC. SDS-PAGE of ElLaH revealed a molecular mass of 8 kDa and MALDI-TOF mass spectrometry revealed a single molecular mass of 8274 Da. the amino terminal sequence determined was LPC(PF)PYQQELTC. the dissociation constant (K) for human neutrophil elastase was 0.32 nM. Hemocyte extract exerted antibacterial effect on Bacillus subtilis and Enterococcus faecalis, while ElLaH was only active against E. faecalis. Currently, Lasiodora sp. is undergoing a systematic review and this study contributes to molecular characterization of the genus. in addition, the results suggest that serine protease inhibitors expressed in Lasiodora sp. hemocytes may be involved in the defense against bacterial infection. (C) 2011 Elsevier B.V. All rights reserved. |
publishDate |
2011 |
dc.date.none.fl_str_mv |
2011-12-01 2016-01-24T14:17:28Z 2016-01-24T14:17:28Z |
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://dx.doi.org/10.1016/j.procbio.2011.09.012 Process Biochemistry. Oxford: Elsevier B.V., v. 46, n. 12, p. 2317-2321, 2011. 10.1016/j.procbio.2011.09.012 WOS000297832000014.pdf 1359-5113 http://repositorio.unifesp.br/handle/11600/34246 WOS:000297832000014 |
url |
http://dx.doi.org/10.1016/j.procbio.2011.09.012 http://repositorio.unifesp.br/handle/11600/34246 |
identifier_str_mv |
Process Biochemistry. Oxford: Elsevier B.V., v. 46, n. 12, p. 2317-2321, 2011. 10.1016/j.procbio.2011.09.012 WOS000297832000014.pdf 1359-5113 WOS:000297832000014 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Process Biochemistry |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy |
dc.format.none.fl_str_mv |
2317-2321 application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier B.V. |
publisher.none.fl_str_mv |
Elsevier B.V. |
dc.source.none.fl_str_mv |
reponame:Repositório Institucional da UNIFESP instname:Universidade Federal de São Paulo (UNIFESP) instacron:UNIFESP |
instname_str |
Universidade Federal de São Paulo (UNIFESP) |
instacron_str |
UNIFESP |
institution |
UNIFESP |
reponame_str |
Repositório Institucional da UNIFESP |
collection |
Repositório Institucional da UNIFESP |
repository.name.fl_str_mv |
Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP) |
repository.mail.fl_str_mv |
biblioteca.csp@unifesp.br |
_version_ |
1814268369505878016 |