Proteomic analysis of the enterocyte brush border.

McConnell RE, Benesh AE, Mao S, Tabb DL, Tyska MJ
Am J Physiol Gastrointest Liver Physiol. 2011 300 (5): G914-26

PMID: 21330445 · PMCID: PMC3094140 · DOI:10.1152/ajpgi.00005.2011

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.

MeSH Terms (20)

Actins Animals Carrier Proteins Cell Adhesion Molecules Cell Separation Chromatography, High Pressure Liquid Computational Biology Cytoskeleton Enterocytes In Vitro Techniques Ion Channels Mass Spectrometry Membrane Proteins Mice Mice, 129 Strain Microvilli Myosins Proteins Proteomics TOR Serine-Threonine Kinases

Connections (3)

This publication is referenced by other Labnodes entities:

Links