scholarly journals Mass spectrometry–based proteomics in cell biology

2010 ◽  
Vol 190 (4) ◽  
pp. 491-500 ◽  
Author(s):  
Tobias C. Walther ◽  
Matthias Mann
Keyword(s):  
Mass Spectrometry ◽  
Quantitative Analysis ◽  
High Resolution ◽  
Sample Preparation ◽  
Cell Biology ◽  
Computational Analysis ◽  
Global Analysis ◽  
Protein Composition ◽  
Broad Community

The global analysis of protein composition, modifications, and dynamics are important goals in cell biology. Mass spectrometry (MS)–based proteomics has matured into an attractive technology for this purpose. Particularly, high resolution MS methods have been extremely successful for quantitative analysis of cellular and organellar proteomes. Rapid advances in all areas of the proteomic workflow, including sample preparation, MS, and computational analysis, should make the technology more easily available to a broad community and turn it into a staple methodology for cell biologists.

The high-resolution mass spectrometry study of the protein composition of amyloid-like urine aggregates associated with preeclampsia

2019 ◽  
Vol 26 (2) ◽  
pp. 158-161 ◽  
Author(s):  
Victoria A Sergeeva ◽  
Natalia V Zakharova ◽  
Anna E Bugrova ◽  
Natalia L Starodubtseva ◽  
Maria I Indeykina ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
High Resolution ◽  
Pregnant Women ◽  
Congo Red ◽  
Molecular Mechanisms ◽  
High Resolution Mass Spectrometry ◽  
Protein Composition ◽  
High Resolution Mass ◽  
Proteomic Approach ◽  
Resolution Mass

The study of protein misfolding and post-translational processing abnormalities is a promising diagnostic approach for socially significant pathologies associated with the accumulation of abnormal forms of proteins. Recently, it was shown that amyloid-like aggregates can be observed in the urine of pregnant women with preeclampsia, which is the most severe hypertensive complication that can lead to fateful outcomes. The protein composition of urine aggregates may clarify the molecular mechanisms underlying the pathology and has not yet been studied in detail. Using a proteomic approach based on high-resolution mass spectrometry, we studied the protein composition of amyloid-like structures that aggregate in the presence of Congo red azo-dye in the urine of pregnant women with preeclampsia. Fragments of β-sheets of α-1-antitrypsin, complement 3, haptoglobin, ceruloplasmin, and trypstatin were identified as most likely targets for Congo red binding.

scholarly journals A streamlined pipeline for multiplexed quantitative site-specific N-glycoproteomics

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Pan Fang ◽  
Yanlong Ji ◽  
Ivan Silbern ◽  
Carmen Doebele ◽  
Momchil Ninov ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
High Resolution ◽  
Sample Preparation ◽  
Large Scale ◽  
Handling Time ◽  
Database Search ◽  
High Confidence ◽  
Site Specific ◽  
Sample Handling ◽  
Data Processing Tool

Abstract Regulation of protein N-glycosylation is essential in human cells. However, large-scale, accurate, and site-specific quantification of glycosylation is still technically challenging. We here introduce SugarQuant, an integrated mass spectrometry-based pipeline comprising protein aggregation capture (PAC)-based sample preparation, multi-notch MS3 acquisition (Glyco-SPS-MS3) and a data-processing tool (GlycoBinder) that enables confident identification and quantification of intact glycopeptides in complex biological samples. PAC significantly reduces sample-handling time without compromising sensitivity. Glyco-SPS-MS3 combines high-resolution MS2 and MS3 scans, resulting in enhanced reporter signals of isobaric mass tags, improved detection of N-glycopeptide fragments, and lowered interference in multiplexed quantification. GlycoBinder enables streamlined processing of Glyco-SPS-MS3 data, followed by a two-step database search, which increases the identification rates of glycopeptides by 22% compared with conventional strategies. We apply SugarQuant to identify and quantify more than 5,000 unique glycoforms in Burkitt’s lymphoma cells, and determine site-specific glycosylation changes that occurred upon inhibition of fucosylation at high confidence.

Sample preparation approaches for qualitative and quantitative analysis of lipid-derived electrophile modified proteomes by mass spectrometry

2020 ◽  
Vol 16 (6) ◽  
pp. 511-520
Author(s):  
Wenjuan Yuan ◽  
Jun Wang ◽  
Ying Zhang ◽  
Haojie Lu
Keyword(s):  
Mass Spectrometry ◽  
Quantitative Analysis ◽  
Sample Preparation ◽  
Analytical Methods ◽  
Qualitative And Quantitative Analysis ◽  
Qualitative And Quantitative

MS-based analytical methods of lipid-derived electrophile modified proteome are discussed in this review.

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