Pathogen inactivation technologies are known to alter in vitro phenotype and functional properties of platelets. Because pathogen inactivation generates reactive oxygen species, oxidative stress is considered as one of the plausible cause at the origin of the platelet storage lesion acceleration after treatment. To date proteomics has been used to document the protein variations to picture out the impact. Here, platelet concentrates were prepared from buffy-coats in Intersol additive solution, leukoreduced and pathogen inactivated using a riboflavin/UVB treatment. At day 2 of storage the platelet proteomes of control (untreated) and treated platelet concentrates were investigated against the site specific oxidation by liquid chromatography coupled to tandem mass spectrometry in a shotgun experiment. The shotgun approach detected 9350 peptides (and 2534 proteins) of which 1714 were oxidized. Eighteen peptides were found exclusively oxidized in treated platelets whereas 3 peptides were only found oxidized in control. The present data evidenced an interference with several proteins involved in platelet aggregation and platelet shape change (such as talin and vinculin).

已知病原体灭活技术会改变血小板的体外表型和功能特性。由于病原体失活会产生活性氧，因此氧化应激被认为是治疗后血小板存储病变加速起源的合理原因之一。迄今为止，蛋白质组学已被用于记录蛋白质的变化，以阐明其影响。在这里，血小板浓缩物是由在Intersol添加剂溶液中的血沉棕黄层制备的，通过核黄素/ UVB处理可白细胞减少和病原体灭活。在储存的第2天，在a弹枪实验中，通过液相色谱-串联质谱联用研究了对照（未处理的）和处理过的血小板浓缩液的血小板蛋白质组抗位点特异性氧化。弹枪方法检测到9350个肽（和2534个蛋白质），其中1714个被氧化。发现在处理的血小板中仅氧化了18种肽，而在对照中仅发现了3种肽。本数据证明干扰了参与血小板聚集和血小板形状改变的几种蛋白质（例如塔林和纽蛋白）。