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Angiogenic activity of fibrin degradation products is located in fibrin fragment E
Author(s) -
Thompson W. D.,
Smith E. B.,
Stirk C. M.,
Marshall F. I.,
Stout A. J.,
Kocchar A
Publication year - 1992
Publication title -
the journal of pathology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.964
H-Index - 184
eISSN - 1096-9896
pISSN - 0022-3417
DOI - 10.1002/path.1711680109
Subject(s) - fibrin , fibrinogen , chemistry , thrombin , antiserum , biochemistry , fibronectin , cleavage (geology) , platelet , biology , immunology , antigen , paleontology , fracture (geology) , extracellular matrix
The source of angiogenic activity of fibrin degradation products has been sought in a series of experiments, applying degradation products from different types of fibrin and fibrinogen to the chick chorioallantoic membrane. The presence of platelets or fibronectin during clotting was not essential for activity, and neither was crosslinking. Fibrinogen degradation products were non‐stimulatory, as was serum. Molecular sieve column chromatography indicated a range of active fragments. Admixture of active fibrin degradation products with antifibrin fragment E, but not D, antiserum neutralized activity. Preparations containing only fibrin fragment E retained activity. A commercial preparation of fibrinogen fragment E was inactive until treated with thrombin. These experiments point to fibrin fragment E being the source of angiogenic activity, with thrombin cleavage being the essential step in generating activity.