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A study of the interaction between Helicobacter pylori and components of the human fibrinolytic system

Research output: Contribution to journalArticlepeer-review

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A study of the interaction between Helicobacter pylori and components of the human fibrinolytic system. / Yarzábal, A.; Avilán, L.; Hoelzl, K.; de Muñoz, M.; Puig, J.; Kansau, I.

In: Brazilian Journal of Medical and Biological Research, Vol. 33, No. 9, 09.2000, p. 1015-1021.

Research output: Contribution to journalArticlepeer-review

Harvard

Yarzábal, A, Avilán, L, Hoelzl, K, de Muñoz, M, Puig, J & Kansau, I 2000, 'A study of the interaction between Helicobacter pylori and components of the human fibrinolytic system', Brazilian Journal of Medical and Biological Research, vol. 33, no. 9, pp. 1015-1021. https://doi.org/10.1590/s0100-879x2000000900004

APA

Yarzábal, A., Avilán, L., Hoelzl, K., de Muñoz, M., Puig, J., & Kansau, I. (2000). A study of the interaction between Helicobacter pylori and components of the human fibrinolytic system. Brazilian Journal of Medical and Biological Research, 33(9), 1015-1021. https://doi.org/10.1590/s0100-879x2000000900004

Vancouver

Yarzábal A, Avilán L, Hoelzl K, de Muñoz M, Puig J, Kansau I. A study of the interaction between Helicobacter pylori and components of the human fibrinolytic system. Brazilian Journal of Medical and Biological Research. 2000 Sep;33(9):1015-1021. https://doi.org/10.1590/s0100-879x2000000900004

Author

Yarzábal, A. ; Avilán, L. ; Hoelzl, K. ; de Muñoz, M. ; Puig, J. ; Kansau, I. / A study of the interaction between Helicobacter pylori and components of the human fibrinolytic system. In: Brazilian Journal of Medical and Biological Research. 2000 ; Vol. 33, No. 9. pp. 1015-1021.

Bibtex

@article{136ee0e9ccbf4cd58ebe692c83302df4,
title = "A study of the interaction between Helicobacter pylori and components of the human fibrinolytic system",
abstract = "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.",
keywords = "Aminocaproates/metabolism, Chromatography, Electrophoresis, Polyacrylamide Gel, Fibrinolytic Agents/metabolism, Helicobacter pylori/metabolism, Humans, Indicators and Reagents, Plasminogen Activators/metabolism, Receptors, Cell Surface/metabolism, Tissue Plasminogen Activator/metabolism, Urokinase-Type Plasminogen Activator/metabolism",
author = "A. Yarz{\'a}bal and L. Avil{\'a}n and K. Hoelzl and {de Mu{\~n}oz}, M. and J. Puig and I. Kansau",
year = "2000",
month = sep,
doi = "10.1590/s0100-879x2000000900004",
language = "English",
volume = "33",
pages = "1015--1021",
journal = "Brazilian Journal of Medical and Biological Research",
issn = "0100-879X",
publisher = "Associacao Brasileira de Divulgacao Cientifica",
number = "9",

}

RIS

TY - JOUR

T1 - A study of the interaction between Helicobacter pylori and components of the human fibrinolytic system

AU - Yarzábal, A.

AU - Avilán, L.

AU - Hoelzl, K.

AU - de Muñoz, M.

AU - Puig, J.

AU - Kansau, I.

PY - 2000/9

Y1 - 2000/9

N2 - 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.

AB - 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.

KW - Aminocaproates/metabolism

KW - Chromatography

KW - Electrophoresis, Polyacrylamide Gel

KW - Fibrinolytic Agents/metabolism

KW - Helicobacter pylori/metabolism

KW - Humans

KW - Indicators and Reagents

KW - Plasminogen Activators/metabolism

KW - Receptors, Cell Surface/metabolism

KW - Tissue Plasminogen Activator/metabolism

KW - Urokinase-Type Plasminogen Activator/metabolism

UR - http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2000000900004&lng=en&tlng=en

U2 - 10.1590/s0100-879x2000000900004

DO - 10.1590/s0100-879x2000000900004

M3 - Article

C2 - 10973131

VL - 33

SP - 1015

EP - 1021

JO - Brazilian Journal of Medical and Biological Research

JF - Brazilian Journal of Medical and Biological Research

SN - 0100-879X

IS - 9

ER -

ID: 24736944