Proteomic analysis of total cellular proteins of human neutrophils
Autor(a) principal: | |
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Data de Publicação: | 2009 |
Outros Autores: | , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNIFESP |
Texto Completo: | http://repositorio.unifesp.br/handle/11600/31749 http://dx.doi.org/10.1186/1477-5956-7-32 |
Resumo: | Background: Neutrophils are the most abundant leukocytes in peripheral blood and represent one of the most important elements of innate immunity. Recent subcellular proteomic studies have focused on the identification of human neutrophil proteins in various subcellular membrane and granular fractions. Although there are relatively few studies dealing with the analysis of the total extract of human neutrophils, many biological problems such as the role of chemokines, adhesion molecules, and other activating inputs involved in neutrophil responses and signaling can be approached on the basis of the identification of the total cellular proteins.Results: Using gel-LC-MS/MS, 251 total cellular proteins were identified from resting human neutrophils. This is more than ten times the number of proteins identified by an initial proteome analysis of human neutrophils and almost five times the number of proteins identified by the first 2-DE map of extracts of rat polymorphonuclear leukocytes. Most of the proteins identified in the present study are well-known, but some of them, such as neutrophil-secreted proteins and centaurin beta-1, a cytoplasmic protein involved in the regulation of NF-kappa B activity, are described here for the first-time.Conclusion: the present report provides new information about the protein content of human neutrophils. Importantly, our study resulted in the discovery of a series of proteins not previously reported to be associated with human neutrophils. These data are relevant to the investigation of comparative pathological states and models for novel classes of pharmaceutical drugs that could be useful in the treatment of inflammatory disorders in which neutrophils participate. |
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Tomazella, Gisele G. [UNIFESP]Silva, Idalete daLaure, Helen J.Rosa, Jose C.Chammas, RogerWiker, Harald G.Souza, Gustavo A. deGreene, Lewis J. [UNIFESP]Universidade de São Paulo (USP)Universidade Federal de São Paulo (UNIFESP)Univ Bergen2016-01-24T13:58:38Z2016-01-24T13:58:38Z2009-08-31Proteome Science. London: Biomed Central Ltd, v. 7, 9 p., 2009.1477-5956http://repositorio.unifesp.br/handle/11600/31749http://dx.doi.org/10.1186/1477-5956-7-32WOS000270069600001.pdf10.1186/1477-5956-7-32WOS:000270069600001Background: Neutrophils are the most abundant leukocytes in peripheral blood and represent one of the most important elements of innate immunity. Recent subcellular proteomic studies have focused on the identification of human neutrophil proteins in various subcellular membrane and granular fractions. Although there are relatively few studies dealing with the analysis of the total extract of human neutrophils, many biological problems such as the role of chemokines, adhesion molecules, and other activating inputs involved in neutrophil responses and signaling can be approached on the basis of the identification of the total cellular proteins.Results: Using gel-LC-MS/MS, 251 total cellular proteins were identified from resting human neutrophils. This is more than ten times the number of proteins identified by an initial proteome analysis of human neutrophils and almost five times the number of proteins identified by the first 2-DE map of extracts of rat polymorphonuclear leukocytes. Most of the proteins identified in the present study are well-known, but some of them, such as neutrophil-secreted proteins and centaurin beta-1, a cytoplasmic protein involved in the regulation of NF-kappa B activity, are described here for the first-time.Conclusion: the present report provides new information about the protein content of human neutrophils. Importantly, our study resulted in the discovery of a series of proteins not previously reported to be associated with human neutrophils. These data are relevant to the investigation of comparative pathological states and models for novel classes of pharmaceutical drugs that could be useful in the treatment of inflammatory disorders in which neutrophils participate.Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Norwegian Research CouncilUniv São Paulo, Ctr Quim Prot, Ctr Reg Hemoterapia, BR-14049900 Ribeirao Preto, BrazilUniv São Paulo, Fac Med Ribeirao Preto, BR-14049900 Ribeirao Preto, BrazilUniversidade Federal de São Paulo, Dept Bioquim, Disciplina Biol Mol, São Paulo, BrazilUniv São Paulo, Fac Med, Lab Oncol Expt LIM 24, São Paulo, BrazilUniv Bergen, Gade Inst, Microbiol & Immunol Sect, Bergen, NorwayUniversidade Federal de São Paulo, Dept Bioquim, Disciplina Biol Mol, São Paulo, BrazilNorwegian Research Council: 175141Web of Science9engBiomed Central LtdProteome ScienceProteomic analysis of total cellular proteins of human neutrophilsinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP11600/317492022-02-18 10:14:11.882metadata only accessoai:repositorio.unifesp.br:11600/31749Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestopendoar:34652023-05-25T12:08:10.213007Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.en.fl_str_mv |
Proteomic analysis of total cellular proteins of human neutrophils |
title |
Proteomic analysis of total cellular proteins of human neutrophils |
spellingShingle |
Proteomic analysis of total cellular proteins of human neutrophils Tomazella, Gisele G. [UNIFESP] |
title_short |
Proteomic analysis of total cellular proteins of human neutrophils |
title_full |
Proteomic analysis of total cellular proteins of human neutrophils |
title_fullStr |
Proteomic analysis of total cellular proteins of human neutrophils |
title_full_unstemmed |
Proteomic analysis of total cellular proteins of human neutrophils |
title_sort |
Proteomic analysis of total cellular proteins of human neutrophils |
author |
Tomazella, Gisele G. [UNIFESP] |
author_facet |
Tomazella, Gisele G. [UNIFESP] Silva, Idalete da Laure, Helen J. Rosa, Jose C. Chammas, Roger Wiker, Harald G. Souza, Gustavo A. de Greene, Lewis J. [UNIFESP] |
author_role |
author |
author2 |
Silva, Idalete da Laure, Helen J. Rosa, Jose C. Chammas, Roger Wiker, Harald G. Souza, Gustavo A. de Greene, Lewis J. [UNIFESP] |
author2_role |
author author author author author author author |
dc.contributor.institution.none.fl_str_mv |
Universidade de São Paulo (USP) Universidade Federal de São Paulo (UNIFESP) Univ Bergen |
dc.contributor.author.fl_str_mv |
Tomazella, Gisele G. [UNIFESP] Silva, Idalete da Laure, Helen J. Rosa, Jose C. Chammas, Roger Wiker, Harald G. Souza, Gustavo A. de Greene, Lewis J. [UNIFESP] |
description |
Background: Neutrophils are the most abundant leukocytes in peripheral blood and represent one of the most important elements of innate immunity. Recent subcellular proteomic studies have focused on the identification of human neutrophil proteins in various subcellular membrane and granular fractions. Although there are relatively few studies dealing with the analysis of the total extract of human neutrophils, many biological problems such as the role of chemokines, adhesion molecules, and other activating inputs involved in neutrophil responses and signaling can be approached on the basis of the identification of the total cellular proteins.Results: Using gel-LC-MS/MS, 251 total cellular proteins were identified from resting human neutrophils. This is more than ten times the number of proteins identified by an initial proteome analysis of human neutrophils and almost five times the number of proteins identified by the first 2-DE map of extracts of rat polymorphonuclear leukocytes. Most of the proteins identified in the present study are well-known, but some of them, such as neutrophil-secreted proteins and centaurin beta-1, a cytoplasmic protein involved in the regulation of NF-kappa B activity, are described here for the first-time.Conclusion: the present report provides new information about the protein content of human neutrophils. Importantly, our study resulted in the discovery of a series of proteins not previously reported to be associated with human neutrophils. These data are relevant to the investigation of comparative pathological states and models for novel classes of pharmaceutical drugs that could be useful in the treatment of inflammatory disorders in which neutrophils participate. |
publishDate |
2009 |
dc.date.issued.fl_str_mv |
2009-08-31 |
dc.date.accessioned.fl_str_mv |
2016-01-24T13:58:38Z |
dc.date.available.fl_str_mv |
2016-01-24T13:58:38Z |
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.citation.fl_str_mv |
Proteome Science. London: Biomed Central Ltd, v. 7, 9 p., 2009. |
dc.identifier.uri.fl_str_mv |
http://repositorio.unifesp.br/handle/11600/31749 http://dx.doi.org/10.1186/1477-5956-7-32 |
dc.identifier.issn.none.fl_str_mv |
1477-5956 |
dc.identifier.file.none.fl_str_mv |
WOS000270069600001.pdf |
dc.identifier.doi.none.fl_str_mv |
10.1186/1477-5956-7-32 |
dc.identifier.wos.none.fl_str_mv |
WOS:000270069600001 |
identifier_str_mv |
Proteome Science. London: Biomed Central Ltd, v. 7, 9 p., 2009. 1477-5956 WOS000270069600001.pdf 10.1186/1477-5956-7-32 WOS:000270069600001 |
url |
http://repositorio.unifesp.br/handle/11600/31749 http://dx.doi.org/10.1186/1477-5956-7-32 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartof.none.fl_str_mv |
Proteome Science |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
9 |
dc.publisher.none.fl_str_mv |
Biomed Central Ltd |
publisher.none.fl_str_mv |
Biomed Central Ltd |
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 |
|
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1783460254145576960 |