Abstract
Fibrinolysis, which represents the end stage of coagulation, was defined by Dastre in 1893 as the dissolution of polymerized fibrin. Todd (1959) reported the presence of fibrinolytic activity in serosal cells derived from human peritoneum and pleura. Astrup and Allbrechtsen (1957) demonstrated plasminogen activator in extracts of serosa from the human fallopian tube and parietal peritoneum of the rat uterus. These studies were confirmed by others who demonstrated fibrinolytic activity and plasminogen activator in parietal pleura, pericardium, and peritoneum (Myhre-Jensen, Larsen, & Astrup, 1969; Porter, McGregor, Mullen, & Silver, 1969; Porter, Ball, & Silver, 1971; Raftery, 1979; Merlo, Fausone, Barbero, & Castagna, 1980). Pugatch and Poole (1969) subsequently reported the presence of fibrinolysis-inhibiting agents in bovine parietal peritoneum. Plasmin, the major enzyme involved in fibrinolysis, is formed from the inactive precursor, plasminogen, by the action of plasminogen activators (PA). PAs are found in urine, tissues, and blood. Normally, coagulation and fibrinolysis are in balance such that no net fibrin deposition occurs.
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diZerega, G.S., Rodgers, K.E. (1992). Fibrinolysis. In: The Peritoneum. Springer, New York, NY. https://doi.org/10.1007/978-1-4613-9235-4_7
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DOI: https://doi.org/10.1007/978-1-4613-9235-4_7
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