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The filamentous brush border glycocalyx, a mucin-like marker of enterocyte hyper-polarization

, : The filamentous brush border glycocalyx, a mucin-like marker of enterocyte hyper-polarization. European Journal of Biochemistry 228(2): 323-331

The probably sole constituent of the filamentous brush border glycocalyx, which has been defined on the basis of electron microscopic data as a set of filaments radiating from the tip of rabbit intestinal brush border microvilli, has been purified. It consists of a mucin-type glycoprotein that can be solubilized by either Triton extraction or papain treatment of the brush border membrane vesicles but is insensitive to phosphatidylinositol phospholipase C. The detergent- and papain-solubilized forms both have the same apparent molecular mass of 400 kDa (SDS/PAGE). This suggests that the filamentous brush border glycocalyx may be anchored to the membrane by a small hydrophobic peptidic tail. Ser, Thr, Pro and Ala amount to 65 % of the protein core amino acid residues. The glycosidic moiety, which amounts to 73 % of the molecular mass, has high O-acetylated sialic acid contents. A monoclonal antibody (3A4) raised against the purified material was produced which specifically recognized the 400-kDa band by immunoprecipitation and immunoblotting, and the filamentous brush border glycocalyx of villus enterocytes when jejunum sections were immunolabelled. The 3A4 determinant was identified with a filamentous brush border glycocalyx-specific carbohydrate structure containing an O-acetylated sialic acid. The fact that the labeled glycocalyx was anchored entirely in a membrane microdomain at the tip of the microvilli shows that mature enterocytes are hyper-polarized epithelial cells.


PMID: 7535695

DOI: 10.1111/j.1432-1033.1995.0323n.x

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