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Proteomic analysis of the enterocyte brush border.

ABSTRACT: The brush border domain at the apex of intestinal epithelial cells is the primary site of nutrient absorption in the intestinal tract and the primary surface of interaction with microbes that reside in the lumen. Because the brush border is positioned at such a critical physiological interface, we set out to create a comprehensive list of the proteins that reside in this domain using shotgun mass spectrometry. The resulting proteome contains 646 proteins with diverse functions. In addition to the expected collection of nutrient processing and transport components, we also identified molecules expected to function in the regulation of actin dynamics, membrane bending, and extracellular adhesion. These results provide a foundation for future studies aimed at defining the molecular mechanisms underpinning brush border assembly and function.

SUBMITTER: McConnell RE

PROVIDER: S-EPMC3094140 | biostudies-literature | 2011 May

REPOSITORIES: biostudies-literature

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Proteomic analysis of the enterocyte brush border.

McConnell Russell E RE Benesh Andrew E AE Mao Suli S Tabb David L DL Tyska Matthew J MJ

American journal of physiology. Gastrointestinal and liver physiology 20110217 5

The brush border domain at the apex of intestinal epithelial cells is the primary site of nutrient absorption in the intestinal tract and the primary surface of interaction with microbes that reside in the lumen. Because the brush border is positioned at such a critical physiological interface, we set out to create a comprehensive list of the proteins that reside in this domain using shotgun mass spectrometry. The resulting proteome contains 646 proteins with diverse functions. In addition to th ...[more]

PMID: 21330445

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