What is the clinical evidence from this study?

Population: Atherosclerosis. Intervention: Plasmin treatment vs. Untreated immobilized fibrinogen. Primary outcome: Binding of Lipoprotein (a) to immobilized fibrinogen (3.7-fold increase).

May 1, 1989Proceedings of the National Academy of SciencesOpen Access

Plasmin catalyzes binding of lipoprotein (a) to immobilized fibrinogen and fibrin.

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Key result

Plasmin treatment of immobilized fibrinogen induced a 3.7-fold increase in Lipoprotein (a) binding, demonstrating an affinity between Lp(a) and protease-modified fibrinogen.

Key Points

To examine whether plasmin promotes the binding of lipoprotein (a) to immobilized fibrinogen and fibrin and to define the underlying molecular mechanism.
Measured the binding of lipoprotein (a) and low-density lipoprotein to immobilized fibrinogen, fibrin, and plasmin-digested fibrinogen fragments.
Assessed the sensitivity of binding to enzymatic digestion by trypsin and neutrophil elastase, as well as inhibition by the lysine analogue epsilon-aminocaproic acid.
Tested competitive displacement between lipoprotein (a) and plasminogen for shared binding domains on plasmin-modified fibrinogen.
Plasmin treatment of immobilized fibrinogen produced a 3.7-fold increase in lipoprotein (a) binding, whereas low-density lipoprotein showed low basal binding that was unaffected by plasmin.
Binding of lipoprotein (a) increased proportionally with the duration of plasmin-induced fibrinogen degradation and was lysine-dependent, showing complete inhibition by epsilon-aminocaproic acid.
Lipoprotein (a) competitively inhibited plasminogen binding to plasmin-modified fibrinogen, confirming that both molecules compete for homologous lysine-binding sites.

Structured PICO

Population

In vitro biochemical model using immobilized fibrinogen and fibrin, Lipoprotein (a), and plasmin

Intervention

Plasmin treatment

Comparator

Untreated immobilized fibrinogen/fibrin or treatment with other enzymes (neutrophil elastase)

Outcome

Binding of Lipoprotein (a) to immobilized fibrinogen and fibrinsurrogate

Main Result

Effect estimate: 3.7-fold increase

Plasmin increases the affinity of Lp(a) for fibrinogen and fibrin, suggesting a biochemical mechanism for the atherothrombotic risk associated with elevated Lp(a).

Authors

PHP C HarpelHospital for Special Surgery BGBruce R. GordonNorthwestern University TPThomas S. ParkerCornell University

Discussion

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Implication

May link Lp(a) to fibrin interactions; leaves open in vivo role in atherosclerosis.

Cite This Study

Harpel et al. (1989) studied Atherosclerosis. Plasmin treatment vs. Untreated immobilized fibrinogen was evaluated on Binding of Lipoprotein (a) to immobilized fibrinogen (3.7-fold increase). Plasmin treatment of immobilized fibrinogen induced a 3.7-fold increase in Lipoprotein (a) binding, demonstrating an affinity between Lp(a) and protease-modified fibrinogen.

synapsesocial.com/papers/6a6f179f439bab0cabc2ae39 https://doi.org/10.1073/pnas.86.10.3847

View Full Paper

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Plasmin catalyzes binding of lipoprotein (a) to immobilized fibrinogen and fibrin.

Key Points

Structured PICO

Main Result

Discussion

Implication

Cite This Study

Plasmin catalyzes binding of lipoprotein (a) to immobilized fibrinogen and fibrin.

Key Points

Structured PICO

Main Result

Discussion

Implication

Cite This Study

Also Consider

Also Consider