Center for the Study of Atherosclerosis, E. Bassini Hospital, via M. Gorki 50, 20092 Cinisello Balsamo, Milan, Italy.
IRCCS MultiMedica, via Milanese 300, 20099 Sesto S. Giovanni, Milan, Italy.
Cardiovasc Res. 2021 Mar 21;117(4):1033-1045. doi: 10.1093/cvr/cvaa252.
Protein glycosylation is a post-translational modification consisting in the enzymatic attachment of carbohydrate chains to specific residues of the protein sequence. Several types of glycosylation have been described, with N-glycosylation and O-glycosylation being the most common types impacting on crucial biological processes, such as protein synthesis, trafficking, localization, and function. Genetic defects in genes involved in protein glycosylation may result in altered production and activity of several proteins, with a broad range of clinical manifestations, including dyslipidaemia and atherosclerosis. A large number of apolipoproteins, lipoprotein receptors, and other proteins involved in lipoprotein metabolism are glycosylated, and alterations in their glycosylation profile are associated with changes in their expression and/or function. Rare genetic diseases and population genetics have provided additional information linking protein glycosylation to the regulation of lipoprotein metabolism.
蛋白质糖基化是一种翻译后修饰，包括酶将碳水化合物链连接到蛋白质序列的特定残基上。已经描述了几种类型的糖基化，其中 N-糖基化和 O-糖基化是最常见的类型，影响着关键的生物过程，如蛋白质合成、运输、定位和功能。涉及蛋白质糖基化的基因的遗传缺陷可能导致多种蛋白质的产生和活性改变，临床表现广泛，包括血脂异常和动脉粥样硬化。大量载脂蛋白、脂蛋白受体和其他参与脂蛋白代谢的蛋白质都发生了糖基化，其糖基化谱的改变与它们的表达和/或功能的改变有关。罕见的遗传疾病和群体遗传学提供了更多的信息，将蛋白质糖基化与脂蛋白代谢的调节联系起来。
