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首页> 外文会议>ASMS Conference on Mass Spectrometry and Allied Topics >Homocysteine Thiolactone Modification of Fibrinogen Analyzed by Mass Spectrometry and its Implication to Impaired Fibrinolysis
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Homocysteine Thiolactone Modification of Fibrinogen Analyzed by Mass Spectrometry and its Implication to Impaired Fibrinolysis

机译：通过质谱分析的纤维蛋白原的同型半胱氨酸硫灭绝改性及其对纤维蛋白溶解的影响

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摘要

Fibrinogen is a plasma glycoprotein involved in coagulation in response to vascular or tissue injury. Altered fibrinogen function and increased resistance to fibrinolysis has implications in wound healing, atherosclerosis and thrombosis. This alteration has recently been observed in vivo in rabbits containing elevated levels of homocysteine (Hcys). We postulate that fibrinogen is covalently modified in the presence of Hcys. One mechanism by which Hcys is thought to modify plasma proteins is via a chemical reaction in which homocysteine thiolactone (HcysTL), a homocysteine metabolite, reacts with the protein's lysl residues. In this work we use a combination of biochemical and mass spectrometric techniques to study homocysteine thiolactone modification of fibrinogen in vitro and consider its importance in the altered fibrinogen function.
机译：纤维蛋白原是响应血管或组织损伤而参与凝血的血浆糖蛋白。改变的纤维蛋白原功能和增加对纤维蛋白质的抗性具有伤口愈合，动脉粥样硬化和血栓形成的影响。最近在含有升高的同型半胱氨酸（HCYS）的兔子中的体内观察到这种改变。我们假设在HCYS存在下共价修饰纤维蛋白原。通过该方法被认为修饰血浆蛋白质的一种机制是通过化学反应，其中同型硫虫蛋氨酸（HcySt1），同型半胱氨酸代谢物与蛋白质的Lysl残基反应。在这项工作中，我们使用生物化学和质谱技术的组合来研究体外纤维蛋白原的同型硫内酯修饰，并考虑其在改变的纤维蛋白原功能中的重要性。

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