Specific binding of soluble fibrin to macrophages
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Updated: Sep 30, 2026

Culture of Macrophage Colony-stimulating Factor Differentiated Human Monocyte-derived Macrophages
Published on: June 30, 2016
Abstract:
Guinea pig peritoneal macrophages were demonstrated to bind selectively soluble 125I-fibrin and fibrin/fibrinogen complexes as compared with fibrinogen, fibrinogen degradation products, and fibrin degradation products. Cellular uptake was considered to be surface receptor binding on the basis of removal of bound 125I-fibrin by trypsin and because uptake occurred in the presence of metabolic inhibitors. 125I-fibrin uptake could be blocked by nonradioactive fibrin but not by IgG or immune complexes. Binding was uneffected by prior treatment with plasmin or trypsin but was calcium dependent. Only limited reversibility of binding could be demonstrated after prolonged incubation. Scatchard plots permitted an estimate of the number of bound molecules. At saturation 6.92 X 10(6) 125I-fibrin molecules were bound per cell. Similar binding of fibrin was noted in polymorphonuclear leukocytes, but not lymphocytes or fibroblasts. Soluble fibrin binding may be a host defense mechanism whereby the reticuloendothelial system can remove fibrin from the blood before the development of microthrombi.
Insights
Guinea pig macrophages bind soluble fibrin, a process crucial for removing fibrin from the bloodstream. This binding mechanism may help prevent microthrombi formation.
Area of Science:
- Immunology
- Hematology
- Cell Biology
Background:
- Fibrin plays a critical role in hemostasis and thrombosis.
- The interaction between immune cells and fibrin is not fully understood.
- Mechanisms for clearing soluble fibrin from circulation are important for preventing pathological thrombus formation.
Purpose of the Study:
- To investigate the binding of soluble fibrin to guinea pig peritoneal macrophages.
- To characterize the nature of the fibrin-macrophage interaction.
- To explore the potential role of this interaction in host defense.
Main Methods:
- Macrophages were incubated with radiolabeled (125I) soluble fibrin.
- Binding assays were performed under various conditions, including the presence of metabolic inhibitors, trypsin, plasmin, calcium, and competing ligands.
- Scatchard analysis was used to quantify binding.
- Fibrin binding was assessed in other cell types, including polymorphonuclear leukocytes, lymphocytes, and fibroblasts.
Main Results:
- Macrophages selectively bind soluble 125I-fibrin and fibrin/fibrinogen complexes, but not fibrinogen or its degradation products.
- Binding is mediated by surface receptors, as evidenced by trypsin sensitivity and occurrence in the presence of metabolic inhibitors.
- Fibrin binding is specific, blocked by nonradioactive fibrin but not by IgG or immune complexes.
- Binding is calcium-dependent and unaffected by plasmin or trypsin pretreatment.
- Approximately 6.92 x 10^6 fibrin molecules bind per macrophage at saturation.
- Similar binding was observed in polymorphonuclear leukocytes but not in lymphocytes or fibroblasts.
Conclusions:
- Guinea pig macrophages possess specific receptors for soluble fibrin.
- This binding is likely a receptor-mediated process, calcium-dependent, and specific for fibrin.
- Soluble fibrin binding by macrophages and polymorphonuclear leukocytes may represent a host defense mechanism to clear fibrin from the blood, preventing microthrombi.
- This interaction highlights a potential pathway for the reticuloendothelial system in managing fibrin clearance.
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