Fibrinogen post-translational modifications are biochemical determinants of fibrin clot properties and interactions.

Margarita Tenopoulou
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Abstract

The structure of fibrinogen and resulting fibrin formed during the coagulation process have important biological functions in human physiology and pathology. Fibrinogen post-translational modifications (PTMs) increase the complexity of the protein structure and many studies have emphasized the potential associations of post-translationally altered fibrinogen with the formation of a fibrin clot with a prothrombotic phenotype. However, the mechanisms by which PTMs exert their action on fibrinogen, and their causal association with disease pathogenesis are relatively unexplored. Moreover, the significance of fibrinogen PTMs in health has yet to be appreciated. In this review, the impact of fibrinogen PTMs on fibrinogen functionality is discussed from a biochemical perspective, emphasizing the potential mechanisms by which PTMs mediate the acquisition of altered fibrinogen properties. A brief discussion on dysfibrinogenemias of genetic origin, attributed to single point variations of the fibrinogen molecule is also provided, highlighting the influence that amino acid properties have on fibrinogen structure, properties, and molecular interactions that arise during thrombus formation.

纤维蛋白原翻译后修饰是纤维蛋白凝块特性和相互作用的生化决定因素。
纤维蛋白原的结构和凝血过程中形成的纤维蛋白在人体生理和病理中具有重要的生物学功能。纤维蛋白原翻译后修饰(PTMs)增加了蛋白质结构的复杂性,许多研究强调翻译后改变的纤维蛋白原可能与纤维蛋白凝块的形成有关,并具有促血栓形成的表型。然而,PTMs 对纤维蛋白原产生作用的机制及其与疾病发病机制的因果关系还相对缺乏研究。此外,纤维蛋白原 PTMs 对健康的重要意义也有待进一步认识。本综述从生化角度讨论了纤维蛋白原 PTM 对纤维蛋白原功能的影响,强调了 PTM 介导纤维蛋白原特性改变的潜在机制。本综述还简要讨论了由纤维蛋白原分子单点变异引起的遗传性纤维蛋白原血症,强调了氨基酸特性对纤维蛋白原结构、特性以及血栓形成过程中分子相互作用的影响。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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