Specific fibrinolytic properties of different molecular forms of pro-urokinase from a monkey kidney cell culture

D C Rijken, D J Binnema, P Los

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

The specific fibrinolytic properties of both high molecular weight (55 kd) and low molecular weight (30 kd) pro-urokinase from a monkey kidney cell culture were evaluated in a plasma clot lysis system and compared with those of human urokinase. The system was composed of a radiolabelled plasma clot immersed in plasma containing the fibrinolytic agent. On unit base, 55 kd pro-urokinase was approximately 1.5 times more effective in lysing the clot than 30 kd pro-urokinase and equally effective as urokinase. In contrast to urokinase, both pro-urokinase forms induced clot lysis without degrading fibrinogen in the surrounding plasma. However, a considerable activation of the fibrinolytic system in the plasma occurred as a large amount of alpha 2-antiplasmin was consumed, indicating that pro-urokinase was not fully fibrin-specific. Quenching antibodies against tissue-type plasminogen activator (t-PA) added to the plasma clot lysis system retarded but did not prevent pro-urokinase-induced clot lysis. This indicated that not only was t-PA in plasma involved in the activation of pro-urokinase (probably via plasmin), but that an additional mechanism also existed.

Original languageEnglish
Pages (from-to)761-768
JournalThrombosis and haemostasis
Volume42
Issue number6
Publication statusPublished - 15 Jun 1986

Keywords

  • Animals
  • Enzyme Activation
  • Enzyme Precursors
  • Fibrinogen
  • Fibrinolysin
  • Fibrinolysis
  • In Vitro Techniques
  • Kidney
  • Macaca fascicularis
  • Molecular Weight
  • Plasminogen Activators
  • Substrate Specificity
  • Tissue Plasminogen Activator
  • Urokinase-Type Plasminogen Activator
  • alpha-2-Antiplasmin
  • Journal Article
  • Research Support, Non-U.S. Gov't

Cite this

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title = "Specific fibrinolytic properties of different molecular forms of pro-urokinase from a monkey kidney cell culture",
abstract = "The specific fibrinolytic properties of both high molecular weight (55 kd) and low molecular weight (30 kd) pro-urokinase from a monkey kidney cell culture were evaluated in a plasma clot lysis system and compared with those of human urokinase. The system was composed of a radiolabelled plasma clot immersed in plasma containing the fibrinolytic agent. On unit base, 55 kd pro-urokinase was approximately 1.5 times more effective in lysing the clot than 30 kd pro-urokinase and equally effective as urokinase. In contrast to urokinase, both pro-urokinase forms induced clot lysis without degrading fibrinogen in the surrounding plasma. However, a considerable activation of the fibrinolytic system in the plasma occurred as a large amount of alpha 2-antiplasmin was consumed, indicating that pro-urokinase was not fully fibrin-specific. Quenching antibodies against tissue-type plasminogen activator (t-PA) added to the plasma clot lysis system retarded but did not prevent pro-urokinase-induced clot lysis. This indicated that not only was t-PA in plasma involved in the activation of pro-urokinase (probably via plasmin), but that an additional mechanism also existed.",
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author = "Rijken, {D C} and Binnema, {D J} and P Los",
year = "1986",
month = "6",
day = "15",
language = "English",
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pages = "761--768",
journal = "Thrombosis and haemostasis",
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Specific fibrinolytic properties of different molecular forms of pro-urokinase from a monkey kidney cell culture. / Rijken, D C; Binnema, D J; Los, P.

In: Thrombosis and haemostasis, Vol. 42, No. 6, 15.06.1986, p. 761-768.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Specific fibrinolytic properties of different molecular forms of pro-urokinase from a monkey kidney cell culture

AU - Rijken, D C

AU - Binnema, D J

AU - Los, P

PY - 1986/6/15

Y1 - 1986/6/15

N2 - The specific fibrinolytic properties of both high molecular weight (55 kd) and low molecular weight (30 kd) pro-urokinase from a monkey kidney cell culture were evaluated in a plasma clot lysis system and compared with those of human urokinase. The system was composed of a radiolabelled plasma clot immersed in plasma containing the fibrinolytic agent. On unit base, 55 kd pro-urokinase was approximately 1.5 times more effective in lysing the clot than 30 kd pro-urokinase and equally effective as urokinase. In contrast to urokinase, both pro-urokinase forms induced clot lysis without degrading fibrinogen in the surrounding plasma. However, a considerable activation of the fibrinolytic system in the plasma occurred as a large amount of alpha 2-antiplasmin was consumed, indicating that pro-urokinase was not fully fibrin-specific. Quenching antibodies against tissue-type plasminogen activator (t-PA) added to the plasma clot lysis system retarded but did not prevent pro-urokinase-induced clot lysis. This indicated that not only was t-PA in plasma involved in the activation of pro-urokinase (probably via plasmin), but that an additional mechanism also existed.

AB - The specific fibrinolytic properties of both high molecular weight (55 kd) and low molecular weight (30 kd) pro-urokinase from a monkey kidney cell culture were evaluated in a plasma clot lysis system and compared with those of human urokinase. The system was composed of a radiolabelled plasma clot immersed in plasma containing the fibrinolytic agent. On unit base, 55 kd pro-urokinase was approximately 1.5 times more effective in lysing the clot than 30 kd pro-urokinase and equally effective as urokinase. In contrast to urokinase, both pro-urokinase forms induced clot lysis without degrading fibrinogen in the surrounding plasma. However, a considerable activation of the fibrinolytic system in the plasma occurred as a large amount of alpha 2-antiplasmin was consumed, indicating that pro-urokinase was not fully fibrin-specific. Quenching antibodies against tissue-type plasminogen activator (t-PA) added to the plasma clot lysis system retarded but did not prevent pro-urokinase-induced clot lysis. This indicated that not only was t-PA in plasma involved in the activation of pro-urokinase (probably via plasmin), but that an additional mechanism also existed.

KW - Animals

KW - Enzyme Activation

KW - Enzyme Precursors

KW - Fibrinogen

KW - Fibrinolysin

KW - Fibrinolysis

KW - In Vitro Techniques

KW - Kidney

KW - Macaca fascicularis

KW - Molecular Weight

KW - Plasminogen Activators

KW - Substrate Specificity

KW - Tissue Plasminogen Activator

KW - Urokinase-Type Plasminogen Activator

KW - alpha-2-Antiplasmin

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

M3 - Article

VL - 42

SP - 761

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JO - Thrombosis and haemostasis

JF - Thrombosis and haemostasis

SN - 0340-6245

IS - 6

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