ArticleJournal of proteome research2006
Combined chemical and enzymatic stable isotope labeling for quantitative profiling of detergent-insoluble membrane proteins isolated using Triton X-100 and Brij-96.
Article in Journal of proteome research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 53 citations in OpenAlex.
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- Identification of Proteomic Biomarkers of Acetaminophen-Induced Hepatotoxicity Using Stable Isotope Labeling.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Comparative proteomics of a model MCF10A-KRasG12V cell line reveals a distinct molecular signature of the KRasG12V cell surface.Oncotarget · 2016Article
- Advancement of mass spectrometry-based proteomics technologies to explore triple negative breast cancer.Molecular bioSystems · 2016Review
- The sporulation of the green alga Ulva prolifera is controlled by changes in photosynthetic electron transport chain.Scientific reports · 2016Article
- Analysis of the immune response of human dendritic cells to Mycobacterium tuberculosis by quantitative proteomics.Proteome science · 2016Article
- Stable isotope dilution mass spectrometry for membrane transporter quantitation.The AAPS journal · 2013Review
- Article
- Mapping tissue-specific expression of extracellular proteins using systematic glycoproteomic analysis of different mouse tissues.Journal of proteome research · 2010Article
- Optimized method for computing (18)O/(16)O ratios of differentially stable-isotope labeled peptides in the context of postdigestion (18)O exchange/labeling.Analytical chemistry · 2010Article
- Contributions of quantitative proteomics to understanding membrane microdomains.Journal of lipid research · 2009Review
- 18O stable isotope labeling in MS-based proteomics.Briefings in functional genomics & proteomics · 2009Review
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Effective quantitative profiling of detergent-insoluble membrane proteins using high-throughput mass spectrometry (MS)-based proteomics would allow a better understanding of physiological and pathological processes that take place at the cell surface. To increase the coverage of proteins present in detergent-resistant membrane microdomains (DRMMs), a combination of 16O/18O and isotope coded affinity tags (ICAT) labeling was used in a comparative analysis of detergent-insoluble membrane proteins isolated from rat basophilic leukemia cells (RBL-2H3), with either Triton X-100 or Brij-96. The analysis resulted in the quantification of 738 unique proteins from Triton X-100 and Brij-96 isolated DRMMs, significantly exceeding the number of proteins quantified from either single labeling technique. Twenty-five noncysteine-containing proteins were quantified, as well as 32 cysteine-containing proteins that would have been missed if either 16O/18O or ICAT labeling had been used exclusively, which illustrate better proteome coverage and enhanced ability to quantitate. The comparative analysis revealed that proteins were more readily extracted using Triton X-100 than Brij-96; however, Triton X-100 also extracted larger quantities of non-DRMMs-associated proteins. This result confirms previous, targeted studies suggesting that DRMMs isolated using Triton X-100 and Brij-96 differ in their protein content.
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