Digestion of 125I-labelled plasmin-derived fibrin degradation products by neutrophil lysosomal enzymes

被引：3

作者：

Adams, SA ^{[1
]}

Kelly, SL ^{[1
]}

Kirsch, RE ^{[1
]}

Shephard, EG ^{[1
]}

机构：

[1] Univ Cape Town, Dept Med, MRC UCT Liver Res Ctr, ZA-7925 Cape Town, South Africa

来源：

BLOOD COAGULATION & FIBRINOLYSIS | 1998年 / 9卷 / 04期

关键词：

fibrin; plasmin; neutrophil lysosomal enzymes; D-dimer; factor XIII;

D O I：

10.1097/00001721-199806000-00002

中图分类号：

R5 [内科学];

学科分类号：

1002 ; 100201 ;

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 Gong Fibrinol 9:307-313 (C) 1998 Lippincott-Raven Publishers.

引用

页码：307 / 313

页数：7

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