Regulation of Fibrinogen Synthesis

Authors

Dre'Von A Dobson
Richard J Fish
Paul S de Vries
Alanna C Morrison
Marguerite Neerman-Arbez
Alisa S Wolberg

Language

English

Publication Date

10-1-2024

Journal

Thrombosis Research

DOI

10.1016/j.thromres.2024.109134

PMID

39216273

PMCID

PMC11381137

PubMedCentral® Posted Date

10-1-2025

PubMedCentral® Full Text Version

Author MSS

Abstract

The plasma protein fibrinogen is encoded by 3 structural genes (FGA, FGB, and FGG) that are transcribed to mRNA, spliced, and translated to 3 polypeptide chains (Aα, Bβ, and γ, respectively). These chains are targeted for secretion, decorated with post-translational modifications, and assembled into a hexameric “dimer of trimers” (AαBβγ)2. Fully assembled fibrinogen is secreted into the blood as a 340 kDa glycoprotein. Fibrinogen is one of the most prevalent coagulation proteins in blood, and its expression is induced by inflammatory cytokines, wherein circulating fibrinogen levels may increase up to 3-fold during acute inflammatory events. Abnormal levels of circulating fibrinogen are associated with bleeding and thrombotic disorders, as well as several inflammatory diseases. Notably, therapeutic strategies to modulate fibrinogen levels have shown promise in experimental models of disease. Herein, we review pathways mediating fibrinogen synthesis, from gene expression to secretion. Knowledge of these mechanisms may lead to the identification of biomarkers and new therapeutic targets to modulate fibrinogen in health and disease.

Keywords

Fibrinogen, Humans, Animals, Fibrinogen, gene expression, mRNA, post-translational modification, acute phase response, cytokines

Published Open-Access

yes

Recommended Citation

Dobson, Dre'Von A; Fish, Richard J; de Vries, Paul S; et al., "Regulation of Fibrinogen Synthesis" (2024). Faculty, Staff and Student Publications. 1273.
https://digitalcommons.library.tmc.edu/uthsph_docs/1273