منابع مشابه
Dynamic changes of fibrin architecture during fibrin formation and intrinsic fibrinolysis of fibrin-rich clots.
Clotting and fibrinolysis are initiated simultaneously in vivo, and fibrinolysis usually occurs without any individualized lysis front (intrinsic fibrinolysis). We have developed a novel model to assess whether morphological changes resulting from intrinsic fibrinolysis are similar to those previously reported at the lysis front using externally applied lytic agents. Fibrin assembly and fibrino...
متن کاملAβ delays fibrin clot lysis by altering fibrin structure and attenuating plasminogen binding to fibrin.
Alzheimer disease is characterized by the presence of increased levels of the β-amyloid peptide (Aβ) in the brain parenchyma and cerebral blood vessels. This accumulated Aβ can bind to fibrin(ogen) and render fibrin clots more resistant to degradation. Here, we demonstrate that Aβ(42) specifically binds to fibrin and induces a tighter fibrin network characterized by thinner fibers and increased...
متن کاملFibrin stabilization (factor XIII), fibrin structure and thrombosis.
Factor XIII (FXIII) is a zymogen that is converted into an active transglutaminase (FXIIIa) by the concerted action of thrombin and Ca2+. Its main task is to crosslink alpha-, and gamma-chains of fibrin and alpha2-plasmin inhibitor to fibrin. By this way FXIIIa strengthens fibrin and protects it from the prompt elimination by fibrinolytic system.The changes of FXIII level in thrombotic diseases...
متن کاملFibrin sheath following pleurodesis.
To cite: Yamane H, Ochi N, Yamagishi T, et al. BMJ Case Rep Published online: [please include Day Month Year] doi:10.1136/bcr-2013203047 DESCRIPTION A 63-year-old man was admitted to our hospital with drug-induced interstitial pneumonia. He was treated with corticosteroid and showed a partial decrease in the interstitial shadow. However, secondary pneumothorax was detected on day 28 of the trea...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1915
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)88277-1