An initial characterization of the serum phosphoproteome.

An initial characterization of the serum phosphoproteome.
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DOI:
10.1021/pr900603n
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发表时间:
2009-12
影响因子:
4.4
通讯作者:
Petricoin, Emanuel F., III
Petricoin, Emanuel F., III
中科院分区:
生物学2区
文献类型:
--
作者:
Zhou, Weidong;Ross, Mark M.;Tessitore, Alessandra;Ornstein, David;VanMeter, Amy;Liotta, Lance A.;Petricoin, Emanuel F., III

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Phosphorylation is a dynamic post-translational protein modification that is the basis of a general mechanism for maintaining and regulating protein structure and function, and of course underpins key cellular processes through signal transduction. In the last several years, many studies of large-scale profiling of phosphoproteins and mapping phosphorylation sites from cultured human cells or tissues by mass spectrometry technique have been published; however, there is little information on general (or global) phosphoproteomic characterization and description of the content of phosphoprotein analytes within the circulation. Circulating phosphoproteins and phosphopeptides could represent important disease biomarkers because of their well-known importance in cellular function, and these analytes frequently are mutated and activated in human diseases such as cancer. Here we report an initial attempt to characterize the phosphoprotein content of serum. To accomplish this, we developed a method in which phosphopeptides are enriched from digested serum proteins and analyzed by LC-MS/MS using LTQ-Orbitrap (CID) and LTQ-ETD mass spectrometers. Using this approach we identified ~100 unique phosphopeptides with stringent filtering criteria and a lower than 1% false discovery rate.
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作者:
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通讯作者: Antunes, E.
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通讯作者: Aebersold, R
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发表时间: 2008-02-01
影响因子: 7
作者:
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