title: 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.
authors.affiliation: Dept. of Cell and Developmental Biology, Vanderbilt Univ. Medical Center, Nashville, TN 37232, USA.
authors.forename: Russell E
authors.initials: RE
authors.lastname: McConnell
authors.forename: Andrew E
authors.initials: AE
authors.lastname: Benesh
authors.forename: Suli
authors.initials: S
authors.lastname: Mao
authors.forename: David L
authors.initials: DL
authors.lastname: Tabb
authors.forename: Matthew J
authors.initials: MJ
authors.lastname: Tyska
mesh_terms: D000199:Actins / Q000378:metabolism; D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism; D015815:Cell Adhesion Molecules / Q000378:metabolism; D002469:Cell Separation; D002851:Chromatography, High Pressure Liquid; D019295:Computational Biology; D003599:Cytoskeleton / Q000378:metabolism; D020895:Enterocytes / Q000378:metabolism / Q000502:physiology*; D066298:In Vitro Techniques; D007473:Ion Channels / Q000378:metabolism; D013058:Mass Spectrometry; D008565:Membrane Proteins / Q000378:metabolism; D051379:Mice; D057507:Mice, 129 Strain; D008871:Microvilli / Q000378:metabolism / Q000502:physiology*; D009218:Myosins / Q000378:metabolism; D011506:Proteins / Q000737:chemistry; D040901:Proteomics; D058570:TOR Serine-Threonine Kinases / Q000378:metabolism
chemical_list: D000199:Actins; D002352:Carrier Proteins; D015815:Cell Adhesion Molecules; D007473:Ion Channels; D008565:Membrane Proteins; D011506:Proteins; D058570:TOR Serine-Threonine Kinases; D009218:Myosins