Digestion of125I‐labelled plasmin‐derived fibrin degradation products by neutrophil lysosomal enzymes
作者:
S. Adams,
S. Kelly,
R. Kirsch,
E. Shephard,
期刊:
Blood Coagulation and Fibrinolysis
(OVID Available online 1998)
卷期:
Volume 9,
issue 4
页码: 307-314
ISSN:0957-5235
年代: 1998
出版商: OVID
关键词: fibrin;plasmin;neutrophil lysosomal enzymes;D-dimer;factor XIII
数据来源: OVID
摘要:
The cellular components of the blood, which become associated with fibrin through specific cellular adhesive processes, play a significant role in the breakdown of fibrin. Fibrinolysis by neutrophil elastase and cathepsin G occurs in a manner distinct from that produced by plasmin. This study demonstrates that neutrophil lysosomal enzyme activity further degrades the end products of plasmic fibrin degradation into low-molecular-weight material, followed by reassembly of higher-molecular-weight products in a process dependent on calcium and factor XIII. Although one of the reformed products has a similar molecular weight to D-dimer and is recognized by a monoclonal antibody raised against D-dimer, its isoelectric point indicates it to be distinctly different from plasmin-derived D-dimer. Processing of the end products of plasmic fibrin degradation by neutrophils may have the potential for modulating the immune response as well as compromising the predictive value of tests measuring D-dimer. Blood Coag Fibrinol 9:307–313 © 1998 Lippincott-Raven Publishers.
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