Heparin affects the interaction of kininogen on endothelial cells
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 |
dARK ID: | ark:/48912/0013000014fjq |
DOI: | 10.1016/j.biochi.2011.07.003 |
Texto Completo: | http://dx.doi.org/10.1016/j.biochi.2011.07.003 http://repositorio.unifesp.br/handle/11600/34067 |
Resumo: | In the plasma kallikrein-kinin system, it has been shown that when plasma prekallikrein (PM) and high molecular weight kininogen (HK) assemble on endothelial cells, plasma kallikrein (huPK) becomes available to cleave HK, releasing bradykinin, a potent mediator of the inflammatory response. Because the formation of soluble glycosaminoglycans occurs concomitantly during the inflammatory processes, the effect of these polysaccharides on the interaction of HK on the cell surface or extracellular matrix (ECM) of two endothelial cell lines (ECV304 and RAEC) was investigated. in the presence of Zn(+2), HK binding to the surface or ECM of RAEC was abolished by heparin; reduced by heparan sulfate, keratan sulfate, chondroitin 4-sulfate or dermatan sulfate; and not affected by chondroitin 6-sulfate. By contrast, only heparin reduced HK binding to the ECV304 cell surface or ECM. Using heparin-correlated molecules such as low molecular weight dextran sulfate, low molecular weight heparin and N-desulfated heparin, we suggest that these effects were mainly dependent on the charge density and on the N-sulfated glucosamine present in heparin. Surprisingly, PM binding to cell- or ECM-bound-HK and PM activation was not modified by heparin. However, the hydrolysis of HK by huPK, releasing BK in the fluid phase, was augmented by this glycosaminoglycan in the presence of Zn(2+). Thus, a functional dichotomy exists in which soluble glycosaminoglycans may possibly either increase or decrease the formation of BK. in conclusion, glycosaminoglycans that accumulated in inflammatory fluids or used as a therapeutic drug (e.g., heparin) could act as pro- or anti-inflammatory mediators depending on different factors within the cell environment. (C) 2011 Elsevier Masson SAS. All rights reserved. |
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Heparin affects the interaction of kininogen on endothelial cellsEndothelial cellsGlycosaminoglycansKininogenPrekallikreinZinc ionsIn the plasma kallikrein-kinin system, it has been shown that when plasma prekallikrein (PM) and high molecular weight kininogen (HK) assemble on endothelial cells, plasma kallikrein (huPK) becomes available to cleave HK, releasing bradykinin, a potent mediator of the inflammatory response. Because the formation of soluble glycosaminoglycans occurs concomitantly during the inflammatory processes, the effect of these polysaccharides on the interaction of HK on the cell surface or extracellular matrix (ECM) of two endothelial cell lines (ECV304 and RAEC) was investigated. in the presence of Zn(+2), HK binding to the surface or ECM of RAEC was abolished by heparin; reduced by heparan sulfate, keratan sulfate, chondroitin 4-sulfate or dermatan sulfate; and not affected by chondroitin 6-sulfate. By contrast, only heparin reduced HK binding to the ECV304 cell surface or ECM. Using heparin-correlated molecules such as low molecular weight dextran sulfate, low molecular weight heparin and N-desulfated heparin, we suggest that these effects were mainly dependent on the charge density and on the N-sulfated glucosamine present in heparin. Surprisingly, PM binding to cell- or ECM-bound-HK and PM activation was not modified by heparin. However, the hydrolysis of HK by huPK, releasing BK in the fluid phase, was augmented by this glycosaminoglycan in the presence of Zn(2+). Thus, a functional dichotomy exists in which soluble glycosaminoglycans may possibly either increase or decrease the formation of BK. in conclusion, glycosaminoglycans that accumulated in inflammatory fluids or used as a therapeutic drug (e.g., heparin) could act as pro- or anti-inflammatory mediators depending on different factors within the cell environment. (C) 2011 Elsevier Masson SAS. All rights reserved.Universidade Federal de São Paulo, Dept Biochem, BR-04044020 São Paulo, SP, BrazilUniv São Paulo, Sch Arts Sci & Humanities, BR-03828000 São Paulo, SP, BrazilUniversidade Federal de São Paulo, Dept Biophys, BR-04044020 São Paulo, SP, BrazilSapporo Med Univ, Dept Internal Med 2, Sapporo, Hokkaido 0600061, JapanUniversidade Federal de São Paulo, Dept Biochem, BR-04044020 São Paulo, SP, BrazilUniversidade Federal de São Paulo, Dept Biophys, BR-04044020 São Paulo, SP, BrazilWeb of ScienceFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Elsevier B.V.Universidade Federal de São Paulo (UNIFESP)Universidade de São Paulo (USP)Sapporo Med UnivGozzo, Andrezza Justino [UNIFESP]Motta, Guacyara da [UNIFESP]Cruz-Silva, Ilana [UNIFESP]Nunes, Viviane Abreu [UNIFESP]Barros, Nilana Meza Tenório de [UNIFESP]Carmona, Adriana Karaoglanovic [UNIFESP]Sampaio, Misako Uemura [UNIFESP]Michelacci, Yara Maria [UNIFESP]Shimamoto, KazuakiNader, Helena Bonciani [UNIFESP]Araujo, Mariana da Silva [UNIFESP]2016-01-24T14:17:14Z2016-01-24T14:17:14Z2011-10-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion1839-1845application/pdfhttp://dx.doi.org/10.1016/j.biochi.2011.07.003Biochimie. Paris: Elsevier France-editions Scientifiques Medicales Elsevier, v. 93, n. 10, p. 1839-1845, 2011.10.1016/j.biochi.2011.07.003WOS000295107700025.pdf0300-9084http://repositorio.unifesp.br/handle/11600/34067WOS:000295107700025ark:/48912/0013000014fjqengBiochimieinfo: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:UNIFESP2024-07-31T21:30:59Zoai:repositorio.unifesp.br/:11600/34067Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestbiblioteca.csp@unifesp.bropendoar:34652024-12-11T20:55:29.679825Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.none.fl_str_mv |
Heparin affects the interaction of kininogen on endothelial cells |
title |
Heparin affects the interaction of kininogen on endothelial cells |
spellingShingle |
Heparin affects the interaction of kininogen on endothelial cells Heparin affects the interaction of kininogen on endothelial cells Gozzo, Andrezza Justino [UNIFESP] Endothelial cells Glycosaminoglycans Kininogen Prekallikrein Zinc ions Gozzo, Andrezza Justino [UNIFESP] Endothelial cells Glycosaminoglycans Kininogen Prekallikrein Zinc ions |
title_short |
Heparin affects the interaction of kininogen on endothelial cells |
title_full |
Heparin affects the interaction of kininogen on endothelial cells |
title_fullStr |
Heparin affects the interaction of kininogen on endothelial cells Heparin affects the interaction of kininogen on endothelial cells |
title_full_unstemmed |
Heparin affects the interaction of kininogen on endothelial cells Heparin affects the interaction of kininogen on endothelial cells |
title_sort |
Heparin affects the interaction of kininogen on endothelial cells |
author |
Gozzo, Andrezza Justino [UNIFESP] |
author_facet |
Gozzo, Andrezza Justino [UNIFESP] Gozzo, Andrezza Justino [UNIFESP] Motta, Guacyara da [UNIFESP] Cruz-Silva, Ilana [UNIFESP] Nunes, Viviane Abreu [UNIFESP] Barros, Nilana Meza Tenório de [UNIFESP] Carmona, Adriana Karaoglanovic [UNIFESP] Sampaio, Misako Uemura [UNIFESP] Michelacci, Yara Maria [UNIFESP] Shimamoto, Kazuaki Nader, Helena Bonciani [UNIFESP] Araujo, Mariana da Silva [UNIFESP] Motta, Guacyara da [UNIFESP] Cruz-Silva, Ilana [UNIFESP] Nunes, Viviane Abreu [UNIFESP] Barros, Nilana Meza Tenório de [UNIFESP] Carmona, Adriana Karaoglanovic [UNIFESP] Sampaio, Misako Uemura [UNIFESP] Michelacci, Yara Maria [UNIFESP] Shimamoto, Kazuaki Nader, Helena Bonciani [UNIFESP] Araujo, Mariana da Silva [UNIFESP] |
author_role |
author |
author2 |
Motta, Guacyara da [UNIFESP] Cruz-Silva, Ilana [UNIFESP] Nunes, Viviane Abreu [UNIFESP] Barros, Nilana Meza Tenório de [UNIFESP] Carmona, Adriana Karaoglanovic [UNIFESP] Sampaio, Misako Uemura [UNIFESP] Michelacci, Yara Maria [UNIFESP] Shimamoto, Kazuaki Nader, Helena Bonciani [UNIFESP] Araujo, Mariana da Silva [UNIFESP] |
author2_role |
author author author author author author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Federal de São Paulo (UNIFESP) Universidade de São Paulo (USP) Sapporo Med Univ |
dc.contributor.author.fl_str_mv |
Gozzo, Andrezza Justino [UNIFESP] Motta, Guacyara da [UNIFESP] Cruz-Silva, Ilana [UNIFESP] Nunes, Viviane Abreu [UNIFESP] Barros, Nilana Meza Tenório de [UNIFESP] Carmona, Adriana Karaoglanovic [UNIFESP] Sampaio, Misako Uemura [UNIFESP] Michelacci, Yara Maria [UNIFESP] Shimamoto, Kazuaki Nader, Helena Bonciani [UNIFESP] Araujo, Mariana da Silva [UNIFESP] |
dc.subject.por.fl_str_mv |
Endothelial cells Glycosaminoglycans Kininogen Prekallikrein Zinc ions |
topic |
Endothelial cells Glycosaminoglycans Kininogen Prekallikrein Zinc ions |
description |
In the plasma kallikrein-kinin system, it has been shown that when plasma prekallikrein (PM) and high molecular weight kininogen (HK) assemble on endothelial cells, plasma kallikrein (huPK) becomes available to cleave HK, releasing bradykinin, a potent mediator of the inflammatory response. Because the formation of soluble glycosaminoglycans occurs concomitantly during the inflammatory processes, the effect of these polysaccharides on the interaction of HK on the cell surface or extracellular matrix (ECM) of two endothelial cell lines (ECV304 and RAEC) was investigated. in the presence of Zn(+2), HK binding to the surface or ECM of RAEC was abolished by heparin; reduced by heparan sulfate, keratan sulfate, chondroitin 4-sulfate or dermatan sulfate; and not affected by chondroitin 6-sulfate. By contrast, only heparin reduced HK binding to the ECV304 cell surface or ECM. Using heparin-correlated molecules such as low molecular weight dextran sulfate, low molecular weight heparin and N-desulfated heparin, we suggest that these effects were mainly dependent on the charge density and on the N-sulfated glucosamine present in heparin. Surprisingly, PM binding to cell- or ECM-bound-HK and PM activation was not modified by heparin. However, the hydrolysis of HK by huPK, releasing BK in the fluid phase, was augmented by this glycosaminoglycan in the presence of Zn(2+). Thus, a functional dichotomy exists in which soluble glycosaminoglycans may possibly either increase or decrease the formation of BK. in conclusion, glycosaminoglycans that accumulated in inflammatory fluids or used as a therapeutic drug (e.g., heparin) could act as pro- or anti-inflammatory mediators depending on different factors within the cell environment. (C) 2011 Elsevier Masson SAS. All rights reserved. |
publishDate |
2011 |
dc.date.none.fl_str_mv |
2011-10-01 2016-01-24T14:17:14Z 2016-01-24T14:17:14Z |
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.biochi.2011.07.003 Biochimie. Paris: Elsevier France-editions Scientifiques Medicales Elsevier, v. 93, n. 10, p. 1839-1845, 2011. 10.1016/j.biochi.2011.07.003 WOS000295107700025.pdf 0300-9084 http://repositorio.unifesp.br/handle/11600/34067 WOS:000295107700025 |
dc.identifier.dark.fl_str_mv |
ark:/48912/0013000014fjq |
url |
http://dx.doi.org/10.1016/j.biochi.2011.07.003 http://repositorio.unifesp.br/handle/11600/34067 |
identifier_str_mv |
Biochimie. Paris: Elsevier France-editions Scientifiques Medicales Elsevier, v. 93, n. 10, p. 1839-1845, 2011. 10.1016/j.biochi.2011.07.003 WOS000295107700025.pdf 0300-9084 WOS:000295107700025 ark:/48912/0013000014fjq |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Biochimie |
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 |
1839-1845 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_ |
1822183987389399040 |
dc.identifier.doi.none.fl_str_mv |
10.1016/j.biochi.2011.07.003 |