Comparative proteomics of rat liver and Morris hepatoma 7777 plasma membranes

Clifton, James R; Li, Xuesong; Reutter, Werner; Hixson, Douglas C.; Josić, Djuro

doi:10.1016/j.jchromb.2006.08.047

Cited by 29 publications

(44 citation statements)

References 52 publications

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“…Enrichment for membrane proteins by selective extraction that relies on the use of salt solutions in combination with different ionic and non-ionic detergents and chaotropic reagents [11,13,32] or by biotin/avidin affinity chromatography following cell surface biotinylation gave results similar to those reported by Senis et al [31], indicating a need for better methods to enrich hydrophobic integral membrane proteins. Some improvement has been obtained using a combination of selective extraction; membrane solubilization in methanol-based buffers; enzymatic digestion of the soluble fraction in a buffer containing 60% methanol and analysis by LC-MS/MS [13].…”

Section: Selective Extraction and Proteolytic Digestionsupporting

confidence: 68%

“…It is the reason that several parallel methods should be used, in order to identify both transmembrane and membraneassociated proteins when the goal is the discovery of new biomarkers or drug targets. Thus, to maximize biomarker discovery, a recommended workflow might be selective extraction of membrane proteins by different agents, subsequent identification of solubilized proteins in all isolated fractions [11,32], optimized in-gel digestion and quantitative comparison of different membrane preparations [32,33,37,40] is one of strategies that can be recommended.…”

Section: Choice Of the Experimental Strategymentioning

confidence: 99%

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Mammalian plasma membrane proteins as potential biomarkers and drug targets

2011

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Defining the plasma membrane proteome is crucial to understand the role of plasma membrane in fundamental biological processes. Change in membrane proteins is one of the first events that take place under pathological conditions, making plasma membrane proteins a likely source of potential disease biomarkers with prognostic or diagnostic potential. Membrane proteins are also potential targets for monoclonal antibodies and other drugs that block receptors or inhibit enzymes essential to the disease progress. Despite several advanced methods recently developed for the analysis of hydrophobic proteins and proteins with posttranslational modifications, integral membrane proteins are still under-represented in plasma membrane proteome. Recent advances in proteomic investigation of plasma membrane proteins, defining their roles as diagnostic and prognostic disease biomarkers and as target molecules in disease treatment, are presented.

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Section: Selective Extraction and Proteolytic Digestionsupporting

confidence: 68%

Section: Choice Of the Experimental Strategymentioning

confidence: 99%

Mammalian plasma membrane proteins as potential biomarkers and drug targets

2011

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“…The predominant Ã ProteinPilot scores (S) are related to confidence (C) by C ¼ 100 Â (1-10 ÀS )% (Clifton et al, 2007). y Ratio of normalized volume of droughted plants (D) or recovered plants (R) and control plats (W).…”

Section: Discussionmentioning

confidence: 99%

Changes in the protein profile of Quercus ilex leaves in response to drought stress and recovery

Echevarría-Zomeño

Ariza

Jorge

et al. 2009

Journal of Plant Physiology

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“…During stepwise solubilization, plasma membranes are frozen and thawed, and subsequently treated with salts, usually at higher pH, followed by chaotropic reagents, and then by different ionic or non-ionic detergents, or by combination of these substances [5, 8, 12]. We used this solubilization schema for qualitative and semi-quantitative comparison of proteomes of tissues and for identification of candidate biomarkers for hepatocellular carcinomas [13, 15]. Peng’s group recommended the use of a similar method for enrichment of membranes from the liver microsomal fraction, to be followed by SDS-PAGE, tryptic digestion of excised proteins and identification by LC-MS/MS [15].…”

Section: Introductionmentioning

confidence: 99%

Mass Spectrometry-Based Analysis of Rat Liver and Hepatocellular Carcinoma Morris Hepatoma 7777 Plasma Membrane Proteome

et al. 2013

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The gel-based proteomic analysis of plasma membranes from rat liver and chemically induced, malignant hepatocellular carcinoma Morris hepatoma 7777 was systematically optimized to yield the maximum number of proteins containing transmembrane domains (TMDs). Incorporation of plasma membrane proteins into polyacrylamide “tube gel” followed by in-gel digestion of “tube gel” pieces significantly improved detection by ESI-LC-MS/MS. Removal of less hydrophobic proteins by washing isolated plasma membranes with 0.1 M sodium carbonate enables detection of hydrophobic proteins with one or more TMDs in both tissues. Subsequent treatment of plasma membranes by a proteolytic enzyme (trypsin) causes the loss of some of the proteins that are detected after washing with sodium carbonate, but it enables the detection of other hydrophobic proteins containing TMDs. Introduction of mass spectrometers with higher sensitivity, higher mass resolution and mass accuracy, and a faster scan rate significantly improved detection of membrane proteins, but the improved sample preparation is still useful, and enables detection of additional hydrophobic proteins. Proteolytic pre-digestion of plasma membranes enables detection of additional hydrophobic proteins and better sequence coverage of TMD-containing proteins in plasma membranes from both tissues.

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Comparative proteomics of rat liver and Morris hepatoma 7777 plasma membranes

Cited by 29 publications

References 52 publications

Mammalian plasma membrane proteins as potential biomarkers and drug targets

Mammalian plasma membrane proteins as potential biomarkers and drug targets

Changes in the protein profile of Quercus ilex leaves in response to drought stress and recovery

Mass Spectrometry-Based Analysis of Rat Liver and Hepatocellular Carcinoma Morris Hepatoma 7777 Plasma Membrane Proteome

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