Digestion of 125I-labelled plasmin-derived fibrin degradation products by neutrophil lysosomal enzymes
| Autor: | S. L. Kelly, R. E. Kirsch, Enid G. Shephard, S.A. Adams |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
Time Factors
Neutrophils Spermidine Plasmin medicine.medical_treatment Cathepsin G Fibrin Fibrin Fibrinogen Degradation Products Iodine Radioisotopes chemistry.chemical_compound Lysosome D-dimer Fibrinolysis medicine Humans Electrophoresis Gel Two-Dimensional Fibrinolysin Isoelectric Point Enzyme Inhibitors biology Antibodies Monoclonal Sodium Dodecyl Sulfate Hematology General Medicine Factor XIII Molecular Weight medicine.anatomical_structure chemistry Biochemistry Reducing Agents Neutrophil elastase biology.protein Electrophoresis Polyacrylamide Gel Spermine Lysosomes medicine.drug |
| Zdroj: | BLOOD COAGULATION & FIBRINOLYSIS. 9:307-314 |
| ISSN: | 0957-5235 |
| DOI: | 10.1097/00001721-199806000-00002 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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