{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,1]],"date-time":"2026-07-01T16:38:02Z","timestamp":1782923882900,"version":"3.54.5"},"reference-count":69,"publisher":"Georg Thieme Verlag KG","issue":"02","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Semin Thromb Hemost"],"published-print":{"date-parts":[[2025,3]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Fibrinolysis is initiated by the activation of plasminogen to plasmin via tissue-plasminogen activator (tPA) and urokinase-plasminogen activator (uPA); plasmin then converts fibrin to fibrin degradation products (FDPs). The antifibrinolytics counterbalancing this system include plasminogen activator inhibitor-1 (PAI-1), which inhibits tPA and uPA, \u03b1-2 antiplasmin (\u03b12AP), which inhibits plasmin, and thrombin activatable fibrinolysis inhibitor, which inhibits the conversion of fibrin to FDP. Inherited disorders of the fibrinolytic pathway are rare and primarily have hemorrhagic phenotypes in humans: PAI-1 deficiency, \u03b12AP deficiency, and Quebec platelet disorder. Patients with these disorders are usually treated for bleeds or receive prophylaxis to prevent bleeds in the surgical setting, with pharmacological antifibrinolytics such as aminocaproic acid and tranexamic acid. Disorders of the fibrinolytic pathway with fibrin deposition are extremely rare, mostly noted in patients with plasminogen deficiency, who have more recently benefited from advances in human plasma-derived plasminogen concentrates administered intravenously or locally. These disorders can be very difficult to diagnose using conventional or even specialized coagulation testing, as testing can be nonspecific or have low sensitivity. Testing of the corresponding protein's activity and antigen (where applicable) can be obtained in specialized centres, and routine laboratory measures are not diagnostic. Genetic testing of the pathogenic mutations is recommended in patients with a high suspicion of an inherited disorder of the fibrinolytic pathway.<\/jats:p>","DOI":"10.1055\/s-0044-1789596","type":"journal-article","created":{"date-parts":[[2024,9,19]],"date-time":"2024-09-19T22:51:01Z","timestamp":1726786261000},"page":"227-235","source":"Crossref","is-referenced-by-count":10,"title":["Inherited Disorders of the Fibrinolytic Pathway: Pathogenic Phenotypes and Diagnostic Considerations of Extremely Rare Disorders"],"prefix":"10.1055","volume":"51","author":[{"given":"Maha","family":"Al-Ghafry","sequence":"additional","affiliation":[{"name":"Division of Hematology, Department of Pediatrics, Johns Hopkins University School of Medicine, Baltimore, Maryland"},{"name":"Cancer and Blood Disorders Institute, Johns Hopkins All Children's Hospital, St Petersburg, Florida"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mouhamed Yazan","family":"Abou-Ismail","sequence":"additional","affiliation":[{"name":"Division of Hematology and Hematologic Malignancies, Department of Internal Medicine, University of Utah Health Sciences Center, Salt Lake City, Utah"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Suchitra S.","family":"Acharya","sequence":"additional","affiliation":[{"name":"Division of Pediatric Hematology, Oncology and Stem Cell Transplant - Cohen Children's Medical Center, New Hyde Park, New York"},{"name":"Donald and Barbara Zucker School of Medicine at Hofstra\/Northwell, Hempstead, New York"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"194","published-online":{"date-parts":[[2024,9,19]]},"reference":[{"issue":"12","key":"ref1","doi-asserted-by":"crossref","first-page":"3304","DOI":"10.1016\/j.jtha.2023.09.012","article-title":"The fibrinolysis renaissance","volume":"21","author":"N J Mutch","year":"2023","journal-title":"J Thromb Haemost"},{"key":"ref2","doi-asserted-by":"crossref","first-page":"1036","DOI":"10.1126\/science.6990488","article-title":"Synthesis of human plasminogen by the liver","volume":"208","author":"D Raum","year":"1980","journal-title":"Science"},{"key":"ref3","first-page":"2958","volume-title":"Plasmin","author":"F Castellino","year":"2012","edition":"3rd ed."},{"key":"ref4","first-page":"287","volume-title":"Disorders of coagulation","author":"S N Sarangi","year":"2022","edition":"7th ed."},{"issue":"04","key":"ref5","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1016\/0049-3848(75)90099-7","article-title":"Human plasminogen: in vitro and in vivo evidence for the biological integrity of NH2-terminal glutamic acid plasminogen","volume":"7","author":"D Collen","year":"1975","journal-title":"Thromb Res"},{"issue":"21","key":"ref6","doi-asserted-by":"crossref","first-page":"2881","DOI":"10.1182\/blood.2020008951","article-title":"Plasminogen: an enigmatic zymogen","volume":"137","author":"C B Keragala","year":"2021","journal-title":"Blood"},{"issue":"19","key":"ref7","doi-asserted-by":"crossref","first-page":"12862","DOI":"10.1074\/jbc.M805123200","article-title":"The serine protease plasmin cleaves the amino-terminal domain of the NR2A subunit to relieve zinc inhibition of the N-methyl-D-aspartate receptors","volume":"284","author":"H Yuan","year":"2009","journal-title":"J Biol Chem"},{"issue":"01","key":"ref8","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1172\/JCI110253","article-title":"Alpha2-plasmin inhibitor and alpha2-macroglobulin-plasmin complexes in plasma. 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