Fibrin and fibrin-like extracellular matrix proteins (FBN)

Fibrin is a fibrous, non-globular protein formed by the action of the enzyme thrombin on fibrinogen, a soluble plasma glycoprotein (UniProt P02671). It plays a central role in hemostasis by polymerizing into a mesh-like network that stabilizes blood clots and provides a scaffold for wound healing and tissue repair (PubMed: 22403061). In pathological conditions, fibrin and fibrin-like proteins accumulate in the extracellular matrix, contributing to the progression of cardiovascular diseases, chronic inflammation, and the tumor microenvironment, where they support angiogenesis and metastasis (PubMed: 28637118). Therapeutic strategies targeting fibrin include thrombolytic drugs like Alteplase and Tenecteplase, which dissolve clots by activating plasminogen to degrade the fibrin matrix (FDA Label: Activase). Additionally, fibrin serves as a specific target for molecular imaging and site-specific drug delivery in thrombosis and oncology (PubMed: 16415868). Fibrin-based sealants are also utilized in surgical settings to promote hemostasis and tissue adhesion (PubMed: 21143116). Understanding the dynamics of fibrin formation and degradation is critical for managing thrombotic disorders and developing targeted therapies for cancer and inflammatory diseases.

Other names

FibrinFibrinogen-derived matrixFibrin-rich extracellular matrixCross-linked fibrinFibrin IFibrin II

Thrombolytic drugs target fibrin by binding to the fibrin matrix and facilitating the conversion of plasminogen to plasmin, which enzymatically cleaves fibrin into soluble fragments (StatPearls: Thrombolytic Therapy). Fibrin sealants act by mimicking the final stage of the coagulation cascade, where thrombin converts fibrinogen into a stable fibrin clot to achieve hemostasis (PubMed: 21143116). Targeted imaging agents and drug delivery systems utilize fibrin-binding peptides or antibodies to localize to fibrin-rich thrombi or tumor stroma (PubMed: 16415868).