The first serine protease inhibitor from Lasiodora sp (Araneae: Theraphosidae) hemocytes

Detalhes bibliográficos
Autor(a) principal: Soares, Tatiana
Data de Publicação: 2011
Outros Autores: 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
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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spelling 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
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