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Plasminogen and plasmin activity in patients with coronary artery disease

M C Drinane1, J A Sherman, A E Hall

  • 1Department of Surgery, Vascular Section, Dartmouth Medical School, Lebanon, NH 03756, USA.

Journal of Thrombosis and Haemostasis : JTH
|May 19, 2006
PubMed

Insights

Patients with coronary artery disease (CAD) show altered plasminogen (Plg) structures, leading to increased plasmin activity. This suggests a conformational change in Plg complexed with tissue plasminogen activator (tPA) contributes to CAD-related fibrinolytic disturbances.

Area of Science:

  • Cardiovascular Biology
  • Hemostasis and Thrombosis
  • Molecular Medicine

Background:

  • Coronary artery disease (CAD) is linked to the plasma fibrinolytic system, but the exact mechanisms are unclear.
  • Plasminogen (Plg) activation to plasmin is central to fibrinolysis, modulated by factors like tissue plasminogen activator (tPA) and plasminogen activator inhibitor-1 (PAI-1).
  • Kringle domains of Plg are crucial for regulating plasmin production and fibrinolysis.

Purpose of the Study:

  • To investigate the role of tissue plasminogen activator (tPA) interactions with plasminogen (Plg) kringle domains in regulating plasmin levels in stable CAD patients.
  • To elucidate the nature of fibrinolytic system disturbances in coronary artery disease.

Main Methods:

  • Collected plasma from 33 patients with significant CAD and 18 controls with normal arteries.
  • Measured plasmin activity, tPA activity, and plasma levels of Plg, PAI-1, urokinase plasminogen activator (uPA), and tPA.
  • Utilized epitope mapping to analyze differences in Plg domain exposure between groups.

Main Results:

  • CAD patients exhibited 1.7-fold higher plasmin activity and 1.5-fold higher tPA activity compared to controls.
  • Significant differences in Plg epitope exposure were observed, with CAD patients showing reduced detectable kringle 4 (50% less) and kringles 1-3 (48% less).

Conclusions:

  • Stable CAD patients display altered plasminogen conformations when complexed with tPA.
  • These conformational changes facilitate increased tPA activity and plasminogen conversion, contributing to elevated plasmin levels in CAD.
Abstract

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