Heparin affects the interaction of kininogen on endothelial cells

Detalhes bibliográficos
Autor(a) principal: Gozzo, Andrezza Justino [UNIFESP]
Data de Publicação: 2011
Outros Autores: 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]
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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spelling 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