Serum protein profiling by solid phase extraction and mass spectrometry: A future diagnostics tool?

Abstract

Serum protein profiling by MS is a promising method for early detection of disease. Important characteristics for serum protein profiling are preanalytical factors, analytical reproducibility and high throughput. Problems related to preanalytical factors can be overcome by using standardized and rigorous sample collection and sample handling protocols. The sensitivity of the MS analysis relies on the quality of the sample; consequently, the blood sample preparation step is crucial to obtain pure and concentrated samples and enrichment of the proteins and peptides of interest. This review focuses on the serum sample preparation step prior to protein profiling by MALDI MS analysis, with particular focus on various SPE methods. The application of SPE techniques with different chromatographic properties such as RP, ion exchange, or affinity binding to isolate specific subsets of molecules (subproteomes) is advantageous for increasing resolution and sensitivity in the subsequent MS analysis. In addition, several of the SPE sample preparation methods are simple and scalable and have proven easy to automate for higher reproducibility and throughput, which is important in a clinical proteomics setting.

A comprehensive glycome profiling of Huntington's disease transgenic mice

“…Glycomics is the system-level study of the glycan repertoires (glycomes), which comprise the entire set of glycans produced in a single organism [22]. It has been an attractive area of research in the postgenome era emerging as a new paradigm for biomarker discovery [23][24][25][26][27]. However, the stereochemical and structural diversity of monosaccharides, the heterogeneous or highly complicated glycan structures of glycoproteins (microheterogeneity), the multivalent nature of glycan-protein interactions [27,28], and the lack of a direct genetic code for glycan complex modification (the non-template dependent biosynthesis of glycans) [29][30][31] are the challenges that scientists are faced with.…”

Targeted metabolomics and mass spectrometry

“…The peak at 1755 is seen to discriminate between the two groups. phase options for sample fractionation (Tiss et al, 2007;Callesen et al, 2009). An alternative fractionation method utilizes magnetic beads (usually with reverse phase C8 coating) to produce reliable peptide profiles and this has been applied to many biological samples, including serum and CSF (Bruegel et al, 2009;Taurines et al, 2010).…”

Diabetic retinopathy: Proteomic approaches to help the differential diagnosis and to understand the underlying molecular mechanisms

“…The gel-free approaches include usually liquid chromatographic (LC) separation of proteins preceded in many cases by other off-line separation techniques such as solid-phase extraction or strong cation exchange [35,36]. In typical conditions the LC is coupled on-line with mass spectrometer and the proteins/peptides eluted from an analytical column are directly injected into the mass spectrometer for identification and/or quantification [37].…”