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Current Proteome Profiling Methods and Applications Yetrib Hathout, Ph.D. Center for Genetic Medicine Children’s National Medical Center & The George Washington.

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Presentation transcript:

Nat. Rev. Gastroenterol. Hepatol. doi:10.1038/nrgastro.2017.76 Figure 5 Conceptual workflow for proteomic analysis of extracellular matrix proteins Figure 5 | Conceptual workflow for proteomic analysis of extracellular matrix proteins. Healthy or diseased gastrointestinal tissues (such as inflammatory colon sections caused by the progression of IBD) can be excised and the cellular proteins extracted using a chaotropic CHAPS (3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate) buffer and mechanical dissociation. Soluble extracellular matrix (ECM) components (such as growth factors and cytokines) are extracted using 6M urea buffer, and insoluble ECM components (such as collagen and elastin) are extracted using chemical digestion with cyanogen bromide. Extracted ECM proteins can be identified and quantified by liquid chromatography tandem mass spectrometry (LC-MS/MS) analysis. Although an overlap of ECM proteins will probably be detected between healthy and diseased states, this proteomic approach will yield an ECM signature that reflects the pathological state of the tissue. This ECM signature could provide important insights into how the ECM is remodelled during disease progression, and could also elucidate novel biomarkers and molecular targets for therapeutic intervention. Hussey, G. S. et al. (2017) The extracellular matrix of the gastrointestinal tract: a regenerative medicine platform Nat. Rev. Gastroenterol. Hepatol. doi:10.1038/nrgastro.2017.76