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Related Experiment Videos

Mini-plasminogen like molecule in septic patients.

L C Kordich1, V P Porterie, O Lago

  • 1Departament of Biological Chemistry, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Argentina.

Thrombosis Research
|September 1, 1987
PubMed
Summary

High leukocyte elastase in sepsis patients alters plasminogen, creating forms that do not bind to lysine-Sepharose. This suggests elastase may modify key proteins in sepsis, impacting coagulation and fibrinolysis pathways.

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Area of Science:

  • Biochemistry
  • Hematology
  • Clinical Medicine

Background:

  • Sepsis is a life-threatening condition characterized by a dysregulated host response to infection.
  • Disseminated Intravascular Coagulation (DIC) is a common complication of sepsis, but its absence does not preclude other hemostatic abnormalities.
  • Leukocyte elastase is a serine protease released by neutrophils, known to degrade various proteins, including components of the fibrinolytic system.

Purpose of the Study:

  • To investigate the impact of sepsis on plasminogen and alpha 2-antiplasmin functionality in patients without DIC.
  • To explore the potential role of leukocyte elastase in modifying these proteins during sepsis.
  • To assess the binding behavior of patient plasminogen to lysine-Sepharose 4B as an indicator of functional alteration.

Main Methods:

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  • Plasma samples were collected from 7 septic patients with positive blood cultures and no clinical or laboratory evidence of DIC.
  • Functional plasminogen and alpha 2-antiplasmin levels were measured.
  • Leukocyte elastase levels were quantified.
  • Plasminogen binding capacity to lysine-Sepharose 4B was assessed.
  • Crossed immunoelectrophoresis with plasminogen was used to detect free alpha 2-antiplasmin.

Main Results:

  • Septic patients without DIC exhibited reduced functional plasminogen levels (25-45%) with normal alpha 2-antiplasmin (80-105%).
  • Elevated leukocyte elastase levels (250-750 µg/ml) were observed.
  • Plasminogen from 3 patients did not bind to lysine-Sepharose 4B, while plasma from the other 4 contained both binding and non-binding plasminogen components.
  • A non-plasminogen binding form of alpha 2-antiplasmin was detected in patient plasma.

Conclusions:

  • Elevated leukocyte elastase in sepsis may lead to the formation of modified plasminogen, characterized by a lack of lysine binding sites.
  • Leukocyte elastase may also modify alpha 2-antiplasmin, rendering it unable to bind plasminogen.
  • These findings suggest that leukocyte elastase plays a significant role in the hemostatic abnormalities observed in sepsis, even in the absence of DIC.