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Fibrin--recombinant human factor XIII a-subunit association
R Procyk1, P D Bishop, B Kudryk
1New York Blood Center, NY 10021.
Thrombosis Research
|July 15, 1993
Summary
Factor XIII (FXIII) a-subunits bind to fibrin clots after thrombin activation. This binding is partially reversible and can be blocked by antibodies targeting specific fibrinogen regions.
Area of Science:
- Biochemistry
- Molecular Biology
- Hemostasis Research
Background:
- Factor XIII (FXIII) is a transglutaminase crucial for blood clot stabilization.
- Understanding FXIII's interaction with fibrin is essential for hemostasis and thrombosis research.
Purpose of the Study:
- To characterize the binding of factor XIII a-subunits to fibrin clots.
- To investigate the role of thrombin activation in FXIII-fibrin association.
- To identify specific regions of fibrin involved in FXIII binding.
Main Methods:
- Utilized recombinant human placental factor XIII (rFXIII) and purified fibrinogen.
- Employed radioiodinated rFXIII to assess binding to fibrin clots immobilized on small columns.
- Investigated binding reversibility by buffer perfusion.
- Used specific antibodies and peptide fragments to block binding.
Main Results:
- Thrombin activation of rFXIII significantly enhanced its binding to fibrin clots.
- The association of rFXIII with fibrin was partially reversible.
- Binding was inhibited by antibodies against the COOH-terminal fibrinogen A alpha-chain (A alpha 389-402).
- Binding was also blocked by the A alpha 241-476 peptide fragment (Hi2-DSK).
Conclusions:
- Thrombin-activated rFXIII specifically associates with fibrin clots.
- The COOH-terminal region of the fibrinogen A alpha-chain is involved in FXIII binding.
- This interaction is partially reversible, suggesting dynamic binding mechanisms in clot stabilization.