Fibrinogen and Fibrin in Human Diseases

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: 30 September 2026 | Viewed by 2041

Special Issue Editor

Department of Pathology, University of Texas Medical Branch at Galveston, Galveston, TX, USA
Interests: fibrinogen; fibrin; growth factors; angiogenesis; tumor growth; metastasis; signaling pathways; infection; inflammation
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Special Issue Information

Dear Colleagues,

Fibrinogen and fibrin (collectively referred to as fibrin(ogen)) are well known for their key physiological roles in regulating bleeding following vascular injury, as well as in wound healing and tissue regeneration. Growing evidence highlights their involvement in a wide range of human diseases, including cardiovascular conditions, inflammation, infections, tumor growth and metastasis, and neurological disorders. Fibrin(ogen) interacts with various plasma proteins and receptors on platelets, leukocytes, endothelial cells, and other cell types, influencing numerous signaling pathways and their downstream effects. Genetic and pharmacological studies have further elucidated the significant contributions of fibrinogen in both local and systemic inflammation. Cellular and molecular research also underscores fibrin(ogen)’s role as a signaling molecule that helps balance hemostasis and thrombosis, coagulation and fibrosis, and, ultimately, life and death. Continued research into the roles of fibrinogen and fibrin in these processes holds the potential to improve treatment strategies and prevention for a range of human diseases.

This Special Issue on “Fibrinogen and Fibrin in Human Diseases” welcomes original research, mini- and full reviews, and perspectives that explore the diverse roles of fibrinogen and fibrin in human health. The aim is to offer a thorough overview of current biomedical research on how fibrin(ogen) contributes to various pathological processes associated with different human diseases.

Dr. Abha Sahni
Guest Editor

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Keywords

  • fibrinogen
  • fibrin
  • inflammation
  • cardiovascular
  • neurological
  • endothelium
  • thrombosis
  • hemostasis
  • fibrosis

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Published Papers (2 papers)

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Research

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16 pages, 2583 KB  
Article
Functional Aspects of Fibrin Structure Alterations by Tranexamic Acid in the Inhibition of Fibrinolysis
by Kata Balog Virag, Barbara Baráth, Kristóf Molnár, Petra Csikós, Alexandra Raska, László Szabó, Natalia Nikolova, Kiril Tenekedjiev, Krasimir Kolev and Nikolett Wohner
Biomolecules 2026, 16(5), 696; https://doi.org/10.3390/biom16050696 - 8 May 2026
Viewed by 566
Abstract
Background: Tranexamic acid (TXA) is a synthetic lysine analog widely used as an antifibrinolytic agent. Large randomized trials have demonstrated life-saving benefits when TXA is administered early in acute hemorrhage, but results regarding prophylactic administration have been conflicting, and several trials have not [...] Read more.
Background: Tranexamic acid (TXA) is a synthetic lysine analog widely used as an antifibrinolytic agent. Large randomized trials have demonstrated life-saving benefits when TXA is administered early in acute hemorrhage, but results regarding prophylactic administration have been conflicting, and several trials have not shown improved clinical outcomes. The mechanisms underlying this discrepancy remain incompletely understood. Objectives: To investigate the molecular and structural mechanisms that determine TXA efficacy in purified fibrin clots under conditions mimicking therapeutic versus prophylactic administration. Methods: We examined fibrinolysis induced by tissue plasminogen activator (tPA) in vitro using confocal microscopy, viscoelastic testing (ClotPro), turbidimetry, and plasmin generation assays at physiologically and therapeutically relevant concentrations of plasminogen and TXA. Scanning electron microscopy (SEM) was employed to assess fibrin structure. Results: When TXA was incorporated into fibrin clots before the addition of tPA, physiological plasminogen concentrations (2.5 µM) reversed the antifibrinolytic effect, resulting in paradoxical acceleration of lysis. By contrast, when clotting and fibrinolysis occurred simultaneously in the presence of TXA and tPA, TXA consistently prolonged lysis time irrespective of plasminogen concentration. SEM demonstrated that TXA, even at concentrations as low as 16 µM, doubled the top-quartile values of the fibrin fiber diameter, altering susceptibility to plasmin-mediated degradation without accelerating plasminogen activation. Conclusions: TXA efficacy is determined not only by dose but also by timing and the plasminogen availability in the clot microenvironment. These findings provide mechanistic insight into the failure of prophylactic TXA administration and highlight the importance of context in optimizing its clinical use. Full article
(This article belongs to the Special Issue Fibrinogen and Fibrin in Human Diseases)
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Review

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15 pages, 1168 KB  
Review
Fibrinogen and Fibrin as Growth Factor Regulators: Pathological Implications, and Translational Opportunities
by Abha Sahni and Sanjeev K. Sahni
Biomolecules 2026, 16(2), 335; https://doi.org/10.3390/biom16020335 - 23 Feb 2026
Cited by 2 | Viewed by 961
Abstract
Fibrinogen and fibrin are multifunctional plasma proteins that play central roles in hemostasis, tissue repair, and extracellular matrix organization. Their complex molecular architecture enables specific interactions with key growth factors, including fibroblast growth factor-2 (FGF-2), vascular endothelial growth factor (VEGF), platelet-derived growth factor [...] Read more.
Fibrinogen and fibrin are multifunctional plasma proteins that play central roles in hemostasis, tissue repair, and extracellular matrix organization. Their complex molecular architecture enables specific interactions with key growth factors, including fibroblast growth factor-2 (FGF-2), vascular endothelial growth factor (VEGF), platelet-derived growth factor (PDGF), transforming growth factor-β (TGF-β), and others, promoting growth factor localization, protection from proteolysis, and enhanced signaling. These interactions regulate essential biological processes such as angiogenesis, cell proliferation, and wound healing. Dysregulation of fibrinogen–fibrin contributes to pathological conditions, including thrombosis, chronic inflammation, cancer progression, neurological complications, and impaired tissue regeneration. Recent advances in fibrin-based biomaterials leverage these molecular interactions for controlled therapeutic delivery and regenerative medicine applications. Emerging recombinant fibrinogen technologies and precision biomaterial engineering further expand the translational potential of targeting fibrinogen–fibrin growth factor interactions to improve clinical outcomes. This review offers an integrated overview of fibrinogen and fibrin biology, detailing their molecular interactions with growth factors, their pathological implications, clinical significance, and future research directions, emphasizing the translational potential of leveraging these interactions to advance human health. Full article
(This article belongs to the Special Issue Fibrinogen and Fibrin in Human Diseases)
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