# Fibrinogen and Fibrin as Growth Factor Regulators: Pathological Implications, and Translational Opportunities

**Authors:** Abha Sahni, Sanjeev K. Sahni

PMC · DOI: 10.3390/biom16020335 · Biomolecules · 2026-02-23

## TL;DR

Fibrinogen and fibrin regulate growth factors, influencing tissue repair and disease, with potential for new therapies in regenerative medicine.

## Contribution

This review integrates the biology and clinical implications of fibrinogen–fibrin interactions with growth factors, highlighting translational opportunities.

## Key findings

- Fibrinogen and fibrin interact with growth factors like FGF-2, VEGF, and TGF-β to regulate biological processes.
- Dysregulation of these interactions contributes to diseases such as cancer and chronic inflammation.
- Advances in fibrin-based biomaterials offer therapeutic delivery and regenerative medicine applications.

## 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 (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.

## Linked entities

- **Proteins:** FGB (fibrinogen beta chain)
- **Diseases:** thrombosis (MONDO:0000831), cancer (MONDO:0004992)

## Full-text entities

- **Genes:** MMRN1 (multimerin 1) [NCBI Gene 22915] {aka ECM, EMILIN4, GPIa*, MMRN}, FGF2 (fibroblast growth factor 2) [NCBI Gene 396413] {aka BFGF, FGF-2, HBGF-2}, F2 (coagulation factor II, thrombin) [NCBI Gene 2147] {aka PT, RPRGL2, THPH1}, FGB (fibrinogen beta chain) [NCBI Gene 373926] {aka fibrinogen}, FN1 (fibronectin 1) [NCBI Gene 2335] {aka CIG, ED-B, FINC, FN, FNZ, GFND}, FGFR1 (fibroblast growth factor receptor 1) [NCBI Gene 2260] {aka BFGFR, CD331, CEK, ECCL, FGFBR, FGFR-1}, ITGAV (integrin subunit alpha V) [NCBI Gene 3685] {aka CD51, IDNDC, MSK8, VNRA, VTNR}, TGFB1 (transforming growth factor beta 1) [NCBI Gene 7040] {aka CAEND1, CED, DPD1, IBDIMDE, LAP, TGF-beta1}, FGF2 (fibroblast growth factor 2) [NCBI Gene 2247] {aka BFGF, FGF-2, FGFB, HBGF-2}, VEGFA (vascular endothelial growth factor A) [NCBI Gene 7422] {aka L-VEGF, MVCD1, VEGF, VPF}, EGF (epidermal growth factor) [NCBI Gene 1950] {aka HOMG4, URG}, F13A1 (coagulation factor XIII A chain) [NCBI Gene 2162] {aka F13A}, FGB (fibrinogen beta chain) [NCBI Gene 2244] {aka HEL-S-78p}, KDR (kinase insert domain receptor) [NCBI Gene 3791] {aka CD309, FLK1, VEGFR, VEGFR2}, IL1A (interleukin 1 alpha) [NCBI Gene 3552] {aka IL-1 alpha, IL-1A, IL1, IL1-ALPHA, IL1F1}, PGF (placental growth factor) [NCBI Gene 5228] {aka D12S1900, PGFL, PIGF, PLGF, PlGF-2, SHGC-10760}, IL1B (interleukin 1, beta) [NCBI Gene 395196] {aka IL-1BETA, IL1beta}, VTN (vitronectin) [NCBI Gene 7448] {aka V75, VN, VNT}
- **Diseases:** inflammatory cytokines (MESH:D000080424), neuronal injury (MESH:D009410), musculoskeletal injury (MESH:D009140), rotator cuff tears (MESH:D000070636), breast cancer (MESH:D001943), sickle cell disease (MESH:D000755), multiple sclerosis (MESH:D009103), tissue damage (MESH:D017695), chronic (MESH:D002908), sepsis (MESH:D018805), diabetic ulcers (MESH:D017719), rheumatoid arthritis (MESH:D001172), thrombosis (MESH:D013927), metastasis (MESH:D009362), atherosclerosis (MESH:D050197), myocardial infarction (MESH:D009203), coagulation (MESH:D001778), infection (MESH:D007239), ischemic stroke (MESH:D002544), vascular injury (MESH:D057772), bleeding disorders (MESH:D006470), obesity (MESH:D009765), hypoxic (MESH:D002534), Fibrotic disorders (MESH:D009358), chronic wounds (MESH:D014947), Inflammatory (MESH:D007249), fibrosis (MESH:D005355), platelet aggregation (MESH:D001791), vascular occlusion (MESH:D008641), Alzheimer's disease (MESH:D000544), lung diseases (MESH:D008171), vascular disease (MESH:D014652), diabetes (MESH:D003920), Cancer (MESH:D009369), neurological complications (MESH:D002493), neuroinflammation (MESH:D000090862)
- **Chemicals:** heparin (MESH:D006493), reactive oxygen species (MESH:D017382), fibrinopeptides A and B (-), disulfide (MESH:D004220), ogen (MESH:C009927)
- **Species:** Gallus gallus (bantam, species) [taxon 9031], Homo sapiens (human, species) [taxon 9606], Mus musculus (house mouse, species) [taxon 10090]

## Full text

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## Figures

2 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12938480/full.md

## References

93 references — full list in the complete paper: https://tomesphere.com/paper/PMC12938480/full.md

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Source: https://tomesphere.com/paper/PMC12938480