Discriminating neoantigenic differences between fibrinogen and fibrin derivatives

Area of Science:

• Biochemistry
• Immunology
• Hematology

Background:

• Distinguishing between fibrinogenolysis and fibrinolysis is crucial for understanding coagulation disorders.
• Fibrinogen and fibrin share structural similarities, making differentiation challenging.
• Cleavage fragments of fibrinogen and fibrin possess distinct molecular markers.

Purpose of the Study:

• To develop a molecular marker for differentiating fibrinogenolytic and fibrinolytic processes.
• To investigate the immunochemical properties of fibrinogen cleavage-associated neoantigen (fg-D(neo)).
• To establish a method for distinguishing fibrinogen and fibrin derivatives.

Main Methods:

• Utilized the cleavage-associated neoantigen of fibrinogen (fg-D(neo)) as a molecular marker.
• Employed quantitative competitive inhibition assays to analyze antibody binding affinity.
• Compared immunochemical expressions of fg-D(neo) in vitro and in vivo.

Main Results:

• Demonstrated characteristic differences in the D regions of fibrinogen and fibrin derivatives using fg-D(neo).
• Showed that fg-D(neo) expression is quantitative and unitary across various fibrinogen/fibrin fragments.
• Identified differential binding affinities of anti-fg-D(neo) antibodies, correlating with fragment type.
• Observed identical immunochemical expressions in vitro and in vivo, supporting plasmin as the in vivo cleavage agent.

Conclusions:

• The differential immunochemical features of fg-D(neo) expression reflect conformational/structural changes during the fibrin transition.
• This marker provides new insights into fibrinogen molecular immunology and structure.
• Offers a novel molecular approach to discriminate between fibrinogenolysis and fibrinolysis secondary to coagulation.