Glycosaminoglycans affect the interaction of human plasma kallikrein with plasminogen, factor XII and inhibitors
Autor(a) principal: | |
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Data de Publicação: | 2003 |
Outros Autores: | , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNIFESP |
Texto Completo: | http://repositorio.unifesp.br/handle/11600/1794 http://dx.doi.org/10.1590/S0100-879X2003000800011 |
Resumo: | Human plasma kallikrein, a serine proteinase, plays a key role in intrinsic blood clotting, in the kallikrein-kinin system, and in fibrinolysis. The proteolytic enzymes involved in these processes are usually controlled by specific inhibitors and may be influenced by several factors including glycosaminoglycans, as recently demonstrated by our group. The aim of the present study was to investigate the effect of glycosaminoglycans (30 to 250 µg/ml) on kallikrein activity on plasminogen and factor XII and on the inhibition of kallikrein by the plasma proteins C1-inhibitor and antithrombin. Almost all available glycosaminoglycans (heparin, heparan sulfate, bovine and tuna dermatan sulfate, chondroitin 4- and 6-sulfates) reduced (1.2 to 3.0 times) the catalytic efficiency of kallikrein (in a nanomolar range) on the hydrolysis of plasminogen (0.3 to 1.8 µM) and increased (1.9 to 7.7 times) the enzyme efficiency in factor XII (0.1 to 10 µM) activation. On the other hand, heparin, heparan sulfate, and bovine and tuna dermatan sulfate improved (1.2 to 3.4 times) kallikrein inhibition by antithrombin (1.4 µM), while chondroitin 4- and 6-sulfates reduced it (1.3 times). Heparin and heparan sulfate increased (1.4 times) the enzyme inhibition by the C1-inhibitor (150 nM). |
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Gozzo, Andrezza Justino [UNIFESP]Nunes, V.a. [UNIFESP]Nader, Helena Bonciani [UNIFESP]Dietrich, Carl Peter [UNIFESP]Carmona, Adriana Karaoglanovic [UNIFESP]Sampaio, Misako Uemura [UNIFESP]Sampaio, C.a.m. [UNIFESP]Araujo, Mariana da Silva [UNIFESP]Universidade Federal de São Paulo (UNIFESP)2015-06-14T13:30:05Z2015-06-14T13:30:05Z2003-08-01Brazilian Journal of Medical and Biological Research. Associação Brasileira de Divulgação Científica, v. 36, n. 8, p. 1055-1059, 2003.0100-879Xhttp://repositorio.unifesp.br/handle/11600/1794http://dx.doi.org/10.1590/S0100-879X2003000800011S0100-879X2003000800011.pdfS0100-879X200300080001110.1590/S0100-879X2003000800011WOS:000185012900012Human plasma kallikrein, a serine proteinase, plays a key role in intrinsic blood clotting, in the kallikrein-kinin system, and in fibrinolysis. The proteolytic enzymes involved in these processes are usually controlled by specific inhibitors and may be influenced by several factors including glycosaminoglycans, as recently demonstrated by our group. The aim of the present study was to investigate the effect of glycosaminoglycans (30 to 250 µg/ml) on kallikrein activity on plasminogen and factor XII and on the inhibition of kallikrein by the plasma proteins C1-inhibitor and antithrombin. Almost all available glycosaminoglycans (heparin, heparan sulfate, bovine and tuna dermatan sulfate, chondroitin 4- and 6-sulfates) reduced (1.2 to 3.0 times) the catalytic efficiency of kallikrein (in a nanomolar range) on the hydrolysis of plasminogen (0.3 to 1.8 µM) and increased (1.9 to 7.7 times) the enzyme efficiency in factor XII (0.1 to 10 µM) activation. On the other hand, heparin, heparan sulfate, and bovine and tuna dermatan sulfate improved (1.2 to 3.4 times) kallikrein inhibition by antithrombin (1.4 µM), while chondroitin 4- and 6-sulfates reduced it (1.3 times). Heparin and heparan sulfate increased (1.4 times) the enzyme inhibition by the C1-inhibitor (150 nM).Universidade Federal de São Paulo (UNIFESP) Escola Paulista de Medicina Departamento de BioquímicaUniversidade Federal de São Paulo (UNIFESP) Escola Paulista de Medicina Departamento de BiofísicaUNIFESP, EPM, Depto. de BioquímicaUNIFESP, EPM, Depto. de BiofísicaSciELO1055-1059engAssociação Brasileira de Divulgação CientíficaBrazilian Journal of Medical and Biological ResearchGlycosaminoglycansHuman plasma kallikreinPlasminogenFactor XIIC1-inhibitorAntithrombinGlycosaminoglycans affect the interaction of human plasma kallikrein with plasminogen, factor XII and inhibitorsinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESPORIGINALS0100-879X2003000800011.pdfapplication/pdf451798${dspace.ui.url}/bitstream/11600/1794/1/S0100-879X2003000800011.pdf1dc22b793f592923a629eedf8969b294MD51open accessTEXTS0100-879X2003000800011.pdf.txtS0100-879X2003000800011.pdf.txtExtracted texttext/plain16986${dspace.ui.url}/bitstream/11600/1794/2/S0100-879X2003000800011.pdf.txt7fa39ae0f631b68cd738ce412bc6c48aMD52open access11600/17942021-09-29 11:23:43.187open accessoai:repositorio.unifesp.br:11600/1794Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestopendoar:34652021-09-29T14:23:43Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.en.fl_str_mv |
Glycosaminoglycans affect the interaction of human plasma kallikrein with plasminogen, factor XII and inhibitors |
title |
Glycosaminoglycans affect the interaction of human plasma kallikrein with plasminogen, factor XII and inhibitors |
spellingShingle |
Glycosaminoglycans affect the interaction of human plasma kallikrein with plasminogen, factor XII and inhibitors Gozzo, Andrezza Justino [UNIFESP] Glycosaminoglycans Human plasma kallikrein Plasminogen Factor XII C1-inhibitor Antithrombin |
title_short |
Glycosaminoglycans affect the interaction of human plasma kallikrein with plasminogen, factor XII and inhibitors |
title_full |
Glycosaminoglycans affect the interaction of human plasma kallikrein with plasminogen, factor XII and inhibitors |
title_fullStr |
Glycosaminoglycans affect the interaction of human plasma kallikrein with plasminogen, factor XII and inhibitors |
title_full_unstemmed |
Glycosaminoglycans affect the interaction of human plasma kallikrein with plasminogen, factor XII and inhibitors |
title_sort |
Glycosaminoglycans affect the interaction of human plasma kallikrein with plasminogen, factor XII and inhibitors |
author |
Gozzo, Andrezza Justino [UNIFESP] |
author_facet |
Gozzo, Andrezza Justino [UNIFESP] Nunes, V.a. [UNIFESP] Nader, Helena Bonciani [UNIFESP] Dietrich, Carl Peter [UNIFESP] Carmona, Adriana Karaoglanovic [UNIFESP] Sampaio, Misako Uemura [UNIFESP] Sampaio, C.a.m. [UNIFESP] Araujo, Mariana da Silva [UNIFESP] |
author_role |
author |
author2 |
Nunes, V.a. [UNIFESP] Nader, Helena Bonciani [UNIFESP] Dietrich, Carl Peter [UNIFESP] Carmona, Adriana Karaoglanovic [UNIFESP] Sampaio, Misako Uemura [UNIFESP] Sampaio, C.a.m. [UNIFESP] Araujo, Mariana da Silva [UNIFESP] |
author2_role |
author author author author author author author |
dc.contributor.institution.none.fl_str_mv |
Universidade Federal de São Paulo (UNIFESP) |
dc.contributor.author.fl_str_mv |
Gozzo, Andrezza Justino [UNIFESP] Nunes, V.a. [UNIFESP] Nader, Helena Bonciani [UNIFESP] Dietrich, Carl Peter [UNIFESP] Carmona, Adriana Karaoglanovic [UNIFESP] Sampaio, Misako Uemura [UNIFESP] Sampaio, C.a.m. [UNIFESP] Araujo, Mariana da Silva [UNIFESP] |
dc.subject.eng.fl_str_mv |
Glycosaminoglycans Human plasma kallikrein Plasminogen Factor XII C1-inhibitor Antithrombin |
topic |
Glycosaminoglycans Human plasma kallikrein Plasminogen Factor XII C1-inhibitor Antithrombin |
description |
Human plasma kallikrein, a serine proteinase, plays a key role in intrinsic blood clotting, in the kallikrein-kinin system, and in fibrinolysis. The proteolytic enzymes involved in these processes are usually controlled by specific inhibitors and may be influenced by several factors including glycosaminoglycans, as recently demonstrated by our group. The aim of the present study was to investigate the effect of glycosaminoglycans (30 to 250 µg/ml) on kallikrein activity on plasminogen and factor XII and on the inhibition of kallikrein by the plasma proteins C1-inhibitor and antithrombin. Almost all available glycosaminoglycans (heparin, heparan sulfate, bovine and tuna dermatan sulfate, chondroitin 4- and 6-sulfates) reduced (1.2 to 3.0 times) the catalytic efficiency of kallikrein (in a nanomolar range) on the hydrolysis of plasminogen (0.3 to 1.8 µM) and increased (1.9 to 7.7 times) the enzyme efficiency in factor XII (0.1 to 10 µM) activation. On the other hand, heparin, heparan sulfate, and bovine and tuna dermatan sulfate improved (1.2 to 3.4 times) kallikrein inhibition by antithrombin (1.4 µM), while chondroitin 4- and 6-sulfates reduced it (1.3 times). Heparin and heparan sulfate increased (1.4 times) the enzyme inhibition by the C1-inhibitor (150 nM). |
publishDate |
2003 |
dc.date.issued.fl_str_mv |
2003-08-01 |
dc.date.accessioned.fl_str_mv |
2015-06-14T13:30:05Z |
dc.date.available.fl_str_mv |
2015-06-14T13:30:05Z |
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 |
Brazilian Journal of Medical and Biological Research. Associação Brasileira de Divulgação Científica, v. 36, n. 8, p. 1055-1059, 2003. |
dc.identifier.uri.fl_str_mv |
http://repositorio.unifesp.br/handle/11600/1794 http://dx.doi.org/10.1590/S0100-879X2003000800011 |
dc.identifier.issn.none.fl_str_mv |
0100-879X |
dc.identifier.file.none.fl_str_mv |
S0100-879X2003000800011.pdf |
dc.identifier.scielo.none.fl_str_mv |
S0100-879X2003000800011 |
dc.identifier.doi.none.fl_str_mv |
10.1590/S0100-879X2003000800011 |
dc.identifier.wos.none.fl_str_mv |
WOS:000185012900012 |
identifier_str_mv |
Brazilian Journal of Medical and Biological Research. Associação Brasileira de Divulgação Científica, v. 36, n. 8, p. 1055-1059, 2003. 0100-879X S0100-879X2003000800011.pdf S0100-879X2003000800011 10.1590/S0100-879X2003000800011 WOS:000185012900012 |
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http://repositorio.unifesp.br/handle/11600/1794 http://dx.doi.org/10.1590/S0100-879X2003000800011 |
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eng |
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Brazilian Journal of Medical and Biological Research |
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1055-1059 |
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Associação Brasileira de Divulgação Científica |
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Associação Brasileira de Divulgação Científica |
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