Molecular organization of the intestinal brush border.
The brush border of enterocytes represents one of the more specialized apical poles of epithelial cells. It is formed by particularly well-developed apical plasma membrane microvilli, whose shape is ensured by a highly organized cytoskeleton. The molecular organization of the cytoskeleton is described. Whereas several cytoskeleton proteins are ubiquitous, villin is highly specific for intestinal cells and can be used as a differentiation marker of these cells. The major glycoproteins, in particular hydrolases, of the brush border membrane have been characterized. They have many common structural features, in particular their mode of integration into the membrane by their N-terminal hydrophobic sequences that also plays the role of the 'signal peptide' responsible for their co-translational insertions into the endoplasmic reticulum. Studies on the biosynthesis and intracellular pathway of aminopeptidase N strongly suggest that sorting of apical and basolateral glycoproteins could occur after their integration into the basolateral domain.
Maroux
S
S
CBBM, CNRS, Marseille, France.
Coudrier
E
E
Feracci
H
H
Gorvel
J P
JP
Louvard
D
D
D000626:Aminopeptidases / Q000096:biosynthesis / Q000378:metabolism; D000818:Animals; D002352:Carrier Proteins; D003598:Cytoskeletal Proteins / Q000378:metabolism; D006023:Glycoproteins / Q000096:biosynthesis; D007413:Intestinal Mucosa / Q000378:metabolism*; D007700:Kinetics; D008840:Microfilament Proteins; D008871:Microvilli / Q000378:metabolism; D011817:Rabbits; D013462:Sulfur Radioisotopes
D002352:Carrier Proteins; D003598:Cytoskeletal Proteins; D006023:Glycoproteins; D008840:Microfilament Proteins; D013462:Sulfur Radioisotopes; C026615:villin; D000626:Aminopeptidases