A study of the interaction between Helicobacter pylori and components of the human fibrinolytic system
The interaction of plasminogen, tissue plasminogen activator (t-PA) and urokinase with a clinical strain of Helicobacter pylori was studied. Plasminogen bound to the surface of H. pylori cells in a concentration-dependent manner and could be activated to the enzymatic form, plasmin, by t-PA. Affinity chromatography assays revealed a plasminogen-binding protein of 58.9 kDa in water extracts of surface proteins. Surface-associated plasmin activity, detected with the chromogenic substrate CBS 00.65, was observed only when plasminogen and an exogenous activator were added to the cell suspension. The two physiologic plasminogen activators, t-PA and urokinase, were also shown to bind to and remain active on the surface of bacterial cells. epsilon-Aminocaproic acid caused partial inhibition of t-PA binding, suggesting that the kringle 2 structure of this activator is involved in the interaction with surface receptors. The activation of plasminogen by t-PA, but not urokinase, strongly depended on the presence of cells and a 25-fold enhancer effect on the initial velocity of activation by t-PA compared to urokinase was established. Furthermore, a relationship between cell concentration and the initial velocity of activation was demonstrated. These findings support the concept that plasminogen activation by t-PA on the bacterial surface is a surface-dependent reaction which offers catalytic advantages.
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Associação Brasileira de Divulgação Científica
2000
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oai:scielo:S0100-879X20000009000042000-09-01A study of the interaction between Helicobacter pylori and components of the human fibrinolytic systemYarzábal,A.Avilán,L.Hoelzl,K.Muñoz,M. dePuig,J.Kansau,I. Helicobacter pylori plasminogen t-PA urokinase plasminogen activation The interaction of plasminogen, tissue plasminogen activator (t-PA) and urokinase with a clinical strain of Helicobacter pylori was studied. Plasminogen bound to the surface of H. pylori cells in a concentration-dependent manner and could be activated to the enzymatic form, plasmin, by t-PA. Affinity chromatography assays revealed a plasminogen-binding protein of 58.9 kDa in water extracts of surface proteins. Surface-associated plasmin activity, detected with the chromogenic substrate CBS 00.65, was observed only when plasminogen and an exogenous activator were added to the cell suspension. The two physiologic plasminogen activators, t-PA and urokinase, were also shown to bind to and remain active on the surface of bacterial cells. epsilon-Aminocaproic acid caused partial inhibition of t-PA binding, suggesting that the kringle 2 structure of this activator is involved in the interaction with surface receptors. The activation of plasminogen by t-PA, but not urokinase, strongly depended on the presence of cells and a 25-fold enhancer effect on the initial velocity of activation by t-PA compared to urokinase was established. Furthermore, a relationship between cell concentration and the initial velocity of activation was demonstrated. These findings support the concept that plasminogen activation by t-PA on the bacterial surface is a surface-dependent reaction which offers catalytic advantages.info:eu-repo/semantics/openAccessAssociação Brasileira de Divulgação CientíficaBrazilian Journal of Medical and Biological Research v.33 n.9 20002000-09-01info:eu-repo/semantics/articletext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2000000900004en10.1590/S0100-879X2000000900004 |
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Yarzábal,A. Avilán,L. Hoelzl,K. Muñoz,M. de Puig,J. Kansau,I. |
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Yarzábal,A. Avilán,L. Hoelzl,K. Muñoz,M. de Puig,J. Kansau,I. A study of the interaction between Helicobacter pylori and components of the human fibrinolytic system |
author_facet |
Yarzábal,A. Avilán,L. Hoelzl,K. Muñoz,M. de Puig,J. Kansau,I. |
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Yarzábal,A. |
title |
A study of the interaction between Helicobacter pylori and components of the human fibrinolytic system |
title_short |
A study of the interaction between Helicobacter pylori and components of the human fibrinolytic system |
title_full |
A study of the interaction between Helicobacter pylori and components of the human fibrinolytic system |
title_fullStr |
A study of the interaction between Helicobacter pylori and components of the human fibrinolytic system |
title_full_unstemmed |
A study of the interaction between Helicobacter pylori and components of the human fibrinolytic system |
title_sort |
study of the interaction between helicobacter pylori and components of the human fibrinolytic system |
description |
The interaction of plasminogen, tissue plasminogen activator (t-PA) and urokinase with a clinical strain of Helicobacter pylori was studied. Plasminogen bound to the surface of H. pylori cells in a concentration-dependent manner and could be activated to the enzymatic form, plasmin, by t-PA. Affinity chromatography assays revealed a plasminogen-binding protein of 58.9 kDa in water extracts of surface proteins. Surface-associated plasmin activity, detected with the chromogenic substrate CBS 00.65, was observed only when plasminogen and an exogenous activator were added to the cell suspension. The two physiologic plasminogen activators, t-PA and urokinase, were also shown to bind to and remain active on the surface of bacterial cells. epsilon-Aminocaproic acid caused partial inhibition of t-PA binding, suggesting that the kringle 2 structure of this activator is involved in the interaction with surface receptors. The activation of plasminogen by t-PA, but not urokinase, strongly depended on the presence of cells and a 25-fold enhancer effect on the initial velocity of activation by t-PA compared to urokinase was established. Furthermore, a relationship between cell concentration and the initial velocity of activation was demonstrated. These findings support the concept that plasminogen activation by t-PA on the bacterial surface is a surface-dependent reaction which offers catalytic advantages. |
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Associação Brasileira de Divulgação Científica |
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2000 |
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http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2000000900004 |
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