Analysis of mouse liver membrane proteins using multidimensional separations and tandem mass spectrometry

Wang, Zhuowei; Wang, Min; Tong, Wei

doi:10.1016/j.jchromb.2010.10.005

Cited by 3 publications

(4 citation statements)

References 39 publications

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“…Ionic exchange resins can also be used in the chromatographic column for a multidimensional separation method to increase the coverage of identified membrane proteins [95,96]. Thus, Wang et al tested four different ionic exchange resins (DEAE-Sepharose, Q-Sepharose, CM-Sepharose, and SP-Sepharose) and their binary mixtures to evaluate their protein binding capacity.…”

Section: Sorbents For Liquid Chromatographymentioning

confidence: 99%

“…Thus, this resin was used in combination with Sephacryl S-200HR for the HPLC separation of membrane proteins. Using this procedure as the first step of a tandem-HPLC method, SDS-PAGE and reversed-phase HPLC allowed successful separation and further identification of membrane and membraneassociated proteins from mouse liver tissues [96].…”

Section: Sorbents For Liquid Chromatographymentioning

confidence: 99%

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Sample preparation strategies for improving the identification of membrane proteins by mass spectrometry

2015

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Despite enormous advances in the mass spectrometry and proteomics fields during the last two decades, the analysis of membrane proteins still remains a challenge for the proteomic community. Membrane proteins play a wide number of key roles in several cellular events, making them relevant target molecules to study in a significant variety of investigations (e.g., cellular signaling, immune surveillance, drug targets, vaccine candidates, etc.). Here, we critically review the several attempts that have been carried out on the different steps of the sample preparation procedure to improve and modify existing conventional proteomic strategies in order to make them suitable for the study of membrane proteins. We also revise novel techniques that have been designed to tackle the difficult but relevant task of identifying and characterizing membrane proteins.

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Section: Sorbents For Liquid Chromatographymentioning

confidence: 99%

Section: Sorbents For Liquid Chromatographymentioning

confidence: 99%

Sample preparation strategies for improving the identification of membrane proteins by mass spectrometry

2015

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“…Wang et al. proposed detergent‐free dual anion exchange–SEC for isolating intact MPs after denaturing in 6 M guanidine hydrochloride and resolubilization in 4 M urea (pH 9) in order to decrease sample complexity and increase protein identifications in complex membrane samples .…”

Section: Improving Membrane Proteome Coverage Using Protein and Peptimentioning

confidence: 99%

“…More recently, Whittelegge et al successfully used SEC with acidic aqueous chloroform/methanol mobile phase for the online top-down MS analysis of several intact transmembrane proteins, thus illustrating the promise of detergent-free protein-level fractionations in top-down proteomics [41,44]. Wang et al proposed detergent-free dual anion exchange-SEC for isolating intact MPs after denaturing in 6 M guanidine hydrochloride and resolubilization in 4 M urea (pH 9) in order to decrease sample complexity and increase protein identifications in complex membrane samples [109].…”

Section: Protein-level Fractionationmentioning

confidence: 99%

Membrane proteomics by high performance liquid chromatography–tandem mass spectrometry: Analytical approaches and challenges

et al. 2013

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Membrane proteins (MPs) play diverse biologically important structural and functional roles including molecular transport, cell communication, and signal transduction. The dysfunctions of many are linked to deleterious human diseases and thus are of utmost importance in drug discovery. MPs comprise approximately 20–30% of all open reading frames (ORFs), however they are typically under‐represented in many LC‐MS proteomics experiments due to their low abundance and poor solubility. To address these analytical challenges, various MP enrichment, solubilization, digestion, and fractionation strategies have been employed to further improve the coverage of the membrane systems while maintaining compatibility with MS detection. This review discusses both established and emerging high‐throughput gel‐free analytical workflows in membrane proteomics, and the inherent advantages, disadvantages, and orthogonality of the various approaches. The issues of critical importance for successful LC‐MS/MS detection such as detergent selection and minimizing ion suppression in detergent‐based workflows are discussed in detail. Recent studies comparing the performance of different analytical strategies are highlighted in order to provide practical insight into the choice of the most appropriate method for membrane‐centric applications ranging from cell surface biomarker discovery to MP interaction network mapping.

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Strategies for Membrane Protein Analysis by Mass Spectrometry

Prados-Rosales

Aragoneses-Cazorla

Estévez

et al. 2019

Advances in Experimental Medicine and Biology

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Analysis of mouse liver membrane proteins using multidimensional separations and tandem mass spectrometry

Cited by 3 publications

References 39 publications

Sample preparation strategies for improving the identification of membrane proteins by mass spectrometry

Sample preparation strategies for improving the identification of membrane proteins by mass spectrometry

Membrane proteomics by high performance liquid chromatography–tandem mass spectrometry: Analytical approaches and challenges

Strategies for Membrane Protein Analysis by Mass Spectrometry

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