Adams S A, Kelly S L, Kirsch R E, Shephard E G
MRC/UCT Liver Research Centre, Department of Medicine, University of Cape Town, South Africa.
Blood Coagul Fibrinolysis. 1998 Jun;9(4):307-13. doi: 10.1097/00001721-199806000-00002.
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.
血液中的细胞成分通过特定的细胞黏附过程与纤维蛋白结合，在纤维蛋白的分解中起重要作用。中性粒细胞弹性蛋白酶和组织蛋白酶G引起的纤维蛋白溶解，其发生方式与纤溶酶产生的方式不同。本研究表明，中性粒细胞溶酶体酶活性进一步将血浆纤维蛋白降解的终产物降解为低分子量物质，随后在依赖于钙和因子XIII的过程中重新组装成高分子量产物。虽然其中一种重组产物的分子量与D-二聚体相似，并且能被针对D-二聚体产生的单克隆抗体识别，但其等电点表明它与纤溶酶衍生的D-二聚体明显不同。中性粒细胞对血浆纤维蛋白降解终产物的处理可能具有调节免疫反应的潜力，同时也会影响检测D-二聚体试验的预测价值。
