Oxidative stress–induced fibrinogen modifications in liver transplant recipients: unraveling a novel potential mechanism for cardiovascular risk

Gitto, Stefano; Fiorillo, Claudia; Argento, Flavia Rita; Fini, Eleonora; Borghi, Serena; Falcini, Margherita; Roccarina, Davide; La Delfa, Rosario; Lillo, Ludovica; Zurli, Tommaso; Forte, Paolo; Ghinolfi, Davide; De Simone, Paolo; Chiesi, Francesca; Ingravallo, Angelica; Vizzutti, Francesco; Aspite, Silvia; Laffi, Giacomo; Lynch, Erica; Petruccelli, Stefania; Carrai, Paola; Palladino, Simona; Sofi, Francesco; Stefani, Laura; Amedei, Amedeo; Baldi, Simone; Toscano, Arianna; Lau, Chloe; Marra, Fabio; Becatti, Matteo

doi:10.1016/j.rpth.2024.102555

Research and Practice in Thrombosis and Haemostasis

2024

DOI: 10.1016/j.rpth.2024.102555

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Oxidative stress–induced fibrinogen modifications in liver transplant recipients: unraveling a novel potential mechanism for cardiovascular risk

Stefano Gitto,

Claudia Fiorillo,

Flavia Rita Argento

et al.

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2024

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Cited by 2 publications

References 81 publications

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Post-translational modifications of fibrinogen: implications for clotting, fibrin structure and degradation

Nencini,

Bettiol,

Argento

et al. 2024

Mol Biomed

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Fibrinogen, a blood plasma protein with a key role in hemostasis and thrombosis, is highly susceptible to post-translational modifications (PTMs), that significantly influence clot formation, structure, and stability. These PTMs, which include acetylation, amidation, carbamylation, citrullination, dichlorination, glycation, glycosylation, guanidinylation, hydroxylation, homocysteinylation, malonylation, methylation, nitration, oxidation, phosphorylation and sulphation, can alter fibrinogen biochemical properties and affect its functional behavior in coagulation and fibrinolysis. Oxidation and nitration are notably associated with oxidative stress, impacting fibrin fiber formation and promoting the development of more compact and resistant fibrin networks. Glycosylation and glycation contribute to altered fibrinogen structural properties, often resulting in changes in fibrin clot density and susceptibility to lysis, particularly in metabolic disorders like diabetes. Acetylation and phosphorylation, influenced by medications such as aspirin, modulate clot architecture by affecting fiber thickness and clot permeability. Citrullination and homocysteinylation, although less studied, are linked to autoimmune conditions and cardiovascular diseases, respectively, affecting fibrin formation and stability. Understanding these modifications provides insights into the pathophysiology of thrombotic disorders and highlights potential therapeutic targets. This review comprehensively examines the current literature on fibrinogen PTMs, their specific sites, biochemical pathways, and their consequences on fibrin clot architecture, clot formation and clot lysis.

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Post-translational modifications of fibrinogen: implications for clotting, fibrin structure and degradation

Nencini,

Bettiol,

Argento

et al. 2024

Mol Biomed

View full text Add to dashboard Cite

show abstract

Fibrinogen Structural Changes and Their Potential Role in Endometriosis-Related Thrombosis

Fini,

Argento,

Borghi

et al. 2024

Antioxidants

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Endometriosis (EM), a chronic inflammatory condition predominantly affecting women of reproductive age, has been linked to an elevated risk of thrombosis, though its underlying molecular mechanisms remain incompletely understood. In this case-control study, involving 71 EM patients and 71 matched controls, we explored the structural and functional changes in fibrinogen and their potential role in thrombosis. Key oxidative stress markers, such as reactive oxygen species (ROS) levels in blood lymphocytes, monocytes, and granulocytes, along with plasma lipid peroxidation markers and total antioxidant capacity, were measured. Fibrinogen structure was examined using circular dichroism spectroscopy and intrinsic fluorescence, while functional properties were evaluated by analyzing thrombin-mediated polymerization and plasmin-induced lysis. Compared to controls, EM patients exhibited elevated ROS production and systemic oxidative stress, leading to notable fibrinogen oxidation and structural alterations. These changes were associated with impaired fibrin polymerization and enhanced resistance to plasmin-induced lysis, which are indicative of a pro-thrombotic state. These findings suggest that oxidative stress-driven fibrinogen modifications may contribute to the heightened thrombotic risk in women with EM, highlighting a potential therapeutic target to mitigate cardiovascular complications.

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Oxidative stress–induced fibrinogen modifications in liver transplant recipients: unraveling a novel potential mechanism for cardiovascular risk

Cited by 2 publications

References 81 publications

Post-translational modifications of fibrinogen: implications for clotting, fibrin structure and degradation

Post-translational modifications of fibrinogen: implications for clotting, fibrin structure and degradation

Fibrinogen Structural Changes and Their Potential Role in Endometriosis-Related Thrombosis

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