Proteomic analysis of total cellular proteins of human neutrophils

Detalhes bibliográficos
Autor(a) principal: Tomazella, Gisele G. [UNIFESP]
Data de Publicação: 2009
Outros Autores: Silva, Idalete da, Laure, Helen J., Rosa, Jose C., Chammas, Roger, Wiker, Harald G., Souza, Gustavo A. de, Greene, Lewis J. [UNIFESP]
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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spelling 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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