Proteomic analysis of microvesicles from plasma of healthy donors reveals high individual variability

Bastos-Amador, Patricia; Royo, Félix; González, Esperanza; Conde‐Vancells, Javier; Palomo-Diez, Laura; Borràs, Francesc E.; Falcón‐Pérez, Juan Manuel

doi:10.1016/j.jprot.2012.03.054

Cited by 83 publications

(83 citation statements)

References 37 publications

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“…On the example of blood plasma: depending on the personal variations in metabolism, diet, possible diseases, e.g. the composition (first of all but not limited to the content of proteins, phospholipids and polyunsaturated fatty acids [124][125][126]) of blood plasma can vary significantly, even though formally the matrix is the same -blood plasma [127]. The sample preparation procedure that is suitable for blood plasma of low protein or phospholipid content may give different results for blood plasma with high protein or phospholipid content.…”

Section: Selectivity Specificity Confirmation Of Identity Selectivimentioning

confidence: 99%

Tutorial review on validation of liquid chromatography–mass spectrometry methods: Part I

Kruve

Rebane

Kipper

et al. 2015

Analytica Chimica Acta

243

145

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This is the part I of a tutorial review intending to give an overview of the state of the art of method validation in liquid chromatography mass spectrometry (LC-MS) and discuss specific issues that arise with MS (and MS/MS) detection in LC (as opposed to the "conventional" detectors). The Part I briefly introduces the principles of operation of LC-MS (emphasizing the aspects important from the validation point of view, in particular the ionization process and ionization suppression/enhancement); reviews the main validation guideline documents and discusses in detail the following performance parameters: selectivity/specificity/identity, ruggedness/robustness, limit of detection, limit of quantification, decision limit and detection capability. With every method performance characteristic its essence and terminology are addressed, the current status of treating it is reviewed and recommendations are given, how to determine it, specifically in the case of LC-MS methods.

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Section: Selectivity Specificity Confirmation Of Identity Selectivimentioning

confidence: 99%

Tutorial review on validation of liquid chromatography–mass spectrometry methods: Part I

Kruve

Rebane

Kipper

et al. 2015

Analytica Chimica Acta

243

145

View full text Add to dashboard Cite

show abstract

“…Ubiquitin has been identified in proteomics studies analysing the composition of EVs [94] and by now it is well known that ubiquitination plays a crucial role in the sorting of molecules into EVs. A recent paper analysed the ubiquitination pattern associated with EVs secreted by myeloid-derived suppressor cells and identified fifty ubiquitinated proteins [95].…”

Section: Ubiquitination and Evsmentioning

confidence: 99%

Oxidative and other posttranslational modifications in extracellular vesicle biology

Szabó-Taylor

Ryan

Osteikoetxea

et al. 2015

Seminars in Cell & Developmental Biology

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“…The proteins like alpha-1-acid glycoprotein, coagulation factor XII, apolipoprotein D (APOD) and many more enriched in this study were recently shown to be associated with circulating extracellular vesicles (EVs). 48 Alpha-1-acid glycoprotein that has been treated as a potential cancer biomarker proteins in human plasma 38 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60 glycoprotein, alpha-1-antichymotrypsin 2, clusterin, vitronectin, serotransferrin and many more were identified with high protein score in this study. Earlier studies 38,48,49 , that have reported these proteins associated with EVs followed extensive ultracentrifugation coupled sucrose gradient or immunoprecipitation technique for their isolation and mostly focused on identification and their concentrations in plasma samples.…”

Section: Glycoproteomic Analysis By Lc-ms/msmentioning

confidence: 99%

“…48 Alpha-1-acid glycoprotein that has been treated as a potential cancer biomarker proteins in human plasma 38 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60 glycoprotein, alpha-1-antichymotrypsin 2, clusterin, vitronectin, serotransferrin and many more were identified with high protein score in this study. Earlier studies 38,48,49 , that have reported these proteins associated with EVs followed extensive ultracentrifugation coupled sucrose gradient or immunoprecipitation technique for their isolation and mostly focused on identification and their concentrations in plasma samples. Interestingly, our study found these circulating EVs are glycosylated and this information could be very useful to interpret their role with new insights as well as their role as potential biomarkers for a variety of human cancers, from laryngeal to ovarian, with breast cancer having the highest correlation.…”

Section: Glycoproteomic Analysis By Lc-ms/msmentioning

confidence: 99%

Improving Blood Plasma Glycoproteome Coverage by Coupling Ultracentrifugation Fractionation to Electrostatic Repulsion–Hydrophilic Interaction Chromatography Enrichment

et al. 2015

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Blood plasma is considered to be an excellent source of disease biomarkers because it contains proteins, lipids, metabolites, cell, and cell-derived extracellular vesicles from different cellular origins including diseased tissues. Most secretory and membranous proteins that can be found in plasma are glycoproteins; therefore, the plasma glycoproteome is one of the major subproteomes that is highly enriched with disease biomarkers. As a result, the glycoproteome has attracted much attention in clinical proteomic research. The modification of proteins with glycans regulates a wide range of functions in biology, but profiling plasma glycoproteins on a global scale has been hampered by the presence of low stoichiometry of glycoproteins in a complex high abundance plasma proteome background and lack of effective analytical technique. This study aims to improve plasma glycoproteome coverage using pig plasma as a model sample with a two-step strategy. The first step involves fractionation of the plasma proteins using ultracentrifugation into supernatant and pellet that is believed to contain low abundant glycoproteins. In the second step, further enrichment of glycopeptides was achieved in both fractions by adopting electrostatic repulsion hydrophilic interaction chromatography (ERLIC) coupled to tandem mass spectrometry (LC-MS/MS) analysis. The coverage of enriched glycoproteins in supernatant, pellet, and whole plasma sample as control was compared. Using this simple sample fractionation approach by ultracentrifugation and further ERLIC enrichment technique, sample complexity was reduced and glycoproteome coverage was significantly enhanced in supernatant and pellet fractions (by >50%) compared with whole plasma sample. This study showed that when ultracentrifugation is coupled to ERLIC glycopeptides enrichment and glycoproteome identification are significantly improved. This study demonstrates the combination of ultracentrifugation and ERLIC as a useful method for discovering plasma glycoprotein disease biomarkers.

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Proteomic analysis of microvesicles from plasma of healthy donors reveals high individual variability

Cited by 83 publications

References 37 publications

Tutorial review on validation of liquid chromatography–mass spectrometry methods: Part I

Tutorial review on validation of liquid chromatography–mass spectrometry methods: Part I

Oxidative and other posttranslational modifications in extracellular vesicle biology

Improving Blood Plasma Glycoproteome Coverage by Coupling Ultracentrifugation Fractionation to Electrostatic Repulsion–Hydrophilic Interaction Chromatography Enrichment

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