title: The apical membrane of intestinal brush cells possesses a specialised, but species-specific, composition of glycoconjugates--on-section and in vivo lectin labelling in rats, guinea-pigs and mice.
abstract: Brush cells are specialised epithelial cells that are assumed to represent chemoreceptors of the digestive tract. They comprise a small population of the epithelial cells lining the intestine, possess a unique ultrastructure and, in many aspects, resemble the receptor cells of taste buds. To characterise glycoconjugates possibly involved in a sensory function, we investigated brush cells in the small intestine of three species using lectin histochemistry in confocal light and thin-section electron microscopy. Brush cells of rats were selectively labelled by the sialic acid-specific lectin Maackia amurensis agglutinin, those of guinea-pigs by the D-galactose-specific lectin Bandeiraea simplicifolia agglutinin, isolectin B4 and those of mice by the L-fucose-specific lectin Ulex europaeus agglutinin lectin I. Lectin binding sites were consistently located in the glycocalyx of the apical membrane and in that of cytoplasmic vesicles. In vivo lectin labelling revealed that the glycoconjugates of the apical membrane are accessible under physiological conditions, that brush cells do not endocytose and that they probably possess a high membrane turnover rate. The results show that specialisations exist in the composition of glycoconjugates forming the glycocalyx of brush cells in all species investigated. The presence of brush cell-specific glycoconjugates would be in accordance with the current hypothesis of a receptive function of brush cells. Differences in the specific glycosylation patterns among rats, guinea-pigs and mice indicate that species-specific adaptations exist.
authors.affiliation: Abteilung Anatomie 2, Medizinische Hochschule Hannover, Germany. Gebert.Andreas@mh-hannover.de
authors.forename: A
authors.initials: A
authors.lastname: Gebert
authors.forename: K
authors.initials: K
authors.lastname: al-Samir
authors.forename: K
authors.initials: K
authors.lastname: Werner
authors.forename: S
authors.initials: S
authors.lastname: Fassbender
authors.forename: A
authors.initials: A
authors.lastname: Gebhard
mesh_terms: D000818:Animals; D020895:Enterocytes / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D004847:Epithelial Cells / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D005643:Fucose / Q000032:analysis; D005690:Galactose / Q000032:analysis; D019276:Glycocalyx / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D006001:Glycoconjugates / Q000032:analysis*; D006168:Guinea Pigs; D007421:Intestine, Small / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D037102:Lectins / Q000378:metabolism; D051379:Mice; D008807:Mice, Inbred BALB C; D008854:Microscopy, Electron; D008871:Microvilli; D019158:N-Acetylneuraminic Acid / Q000032:analysis; D010835:Phytohemagglutinins / Q000378:metabolism*; D037121:Plant Lectins; D051381:Rats; D017208:Rats, Wistar; D013045:Species Specificity
chemical_list: D006001:Glycoconjugates; C045475:Griffonia simplicifolia lectins; D037102:Lectins; D010835:Phytohemagglutinins; D037121:Plant Lectins; C036850:Ulex europaeus lectins; C100156:leukoagglutinins, plants; D005643:Fucose; D019158:N-Acetylneuraminic Acid; D005690:Galactose