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Effect of fibrinogen degradation products on various stages of the fibrinolytic process

100%

Yatsenko T., Rybachuk V. N., Kharchenko S. M., Grinenko T. V., Yusova E. I.

Journal of Pre-Clinical and Clinical Research

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2015

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tom 09

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nr 1

Over-activation of the fibrinolytic system may result in proteolytic destruction of fibrinogen. However, the effect of the degradation products formed during fibrinogenolysis on fibrinolytic process and plasminogen/plasmin properties remains unclear. To investigate this effect and its mechanism, the ability of fibrinogen fragments E and D to act on plasminogen and tPA binding, proenzyme activation, fibrin clot lysis and plasmin inhibition by plasma α2-antiplasmin, were studied. It was found that early product fragment EE binds to plasminogen and tissue-type plasminogen activator and enhances plasminogen conversion into plasmin. C-terminal lysine residues of all 3 chains pair and 16 or 23 amino acid residues of Aα- chain are essential for this process. C-terminal lysines of fragment E Aα- and γ-chains and lysine-binding site of tPA kringle 2 are responsible for the interaction between these proteins. Binding of fragment E to plasminogen is provided by N-terminal Aα1–19 and C-terminal Bβ120–122 regions. Late plasmic fibrinogen degradation product fragment EL loses the ability to potentiate plasmin generation but can bind proenzyme and its activator. Fragment D has no binding properties towards plasminogen and tPA. None of fibrinogen fragments protects plasmin from α2-antiplasmin inhibition. It is concluded that at over-activation of the fibrinolytic system and subsequent fibrinogenolysis, the products of fibrinogen degradation, can bind plasminogen and tPA and potentiate generation of plasmin, which will be neutralized under the normal level of the plasmin inhibitor.

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The role of plasminogen activation system in cancer cell biology

86%

Zekanowska E. B.

Acta Biochimica Polonica

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2007

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tom 54

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nr Supplement 4

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Plasminogen tissue activator [tPA] and inhibitor of plasminogen tissue activator [PAI-1] as potential markers in the study of malignant melanoma metastases

86%

Szemraj J., Pietrucha T., Pytel J., Greger J.

Bulletin of the Polish Academy of Sciences. Biological Sciences

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1994

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tom 42

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nr 2

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Plasma and plasma cell surface measurements of urokinase plasminogen activator system in multiple myeloma patients

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Dmoszynska A., Cioch M., Walter-Croneck A., Jawniak D., Hus I., Rolinski J.

Bulletin of the Veterinary Institute in Puławy. Supplement

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2002

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The importance of selected markers of inflammation and blood-brain barrier damage for short-term ischemic stroke prognosis

58%

Lasek-Bal A., Jedrzejowska-Szypulka H., Student S., Warsz-Wianecka A., Zareba K., Puz P., Bal W., Pawletko K., Lewin-Kowalik J.

Journal of Physiology and Pharmacology

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2019

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tom 70

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nr 2

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The effect of nitric oxide donors on the release of plasminogen activator inhibitor [PAI] from rabbit platelets in vitro

58%

Korbut R., Marcinkiewicz E., Cieslik K., Gryglewski R. J.