Proteomic characterization of novel serum amyloid P component variants from human plasma and urine
Proteomic characterization of novel serum amyloid P component variants from human plasma and urine
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DOI：
10.1002/pmic.200300690
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发表时间：
2004-06-01
期刊：
影响因子：
3.4
通讯作者：
Nelson, RW
中科院分区：
文献类型：
--
作者：
Kiernan, UA;Nedelkov, D;Nelson, RW
血清淀粉样蛋白P组分（SAP）是一种人血浆蛋白，因其对淀粉样斑块形成和稳定的影响而被广泛研究。SAP的特点是直接从人血浆和尿液样本通过新的亲和质谱为基础的蛋白质组学技术，能够很容易地区分质量改变的蛋白质变体。这些分析能够识别先前未报告的SAP的几种变体。这些变体包括聚糖结构的微观异质性，来自一个或两个末端唾液酸残基的丢失以及C-末端缬氨酸残基的丢失。此外，尿液分析允许一致的血清淀粉样蛋白P组分作为尿液蛋白质组的正常成分的鉴定。
Serum amyloid P component (SAP) is a human plasma protein that has been widely studied for its influence on amyloid plaque formation and stabilization. SAP was characterized directly from human plasma and urine samples via novel affinity mass spectrometry-based proteomic technology that is able to readily discriminate between mass-altered protein variants. These analyses were able to identify several variants of SAP that have not been previously reported. These variants include microheterogeneity of the glycan structure, from the loss of one or both terminal sialic acid residues, as well as the loss of the C-terminal valine residue. Moreover, the analysis of urine allowed for the consistent identification of serum amyloid P component as a normal constituent of the urine proteome.