Histochemical characterization of the equine guttural pouches was performed using lectins combined with sialidase digestion and deglycosylation pre-treatments. The goblet cells contained O- and N-linked oligosaccharides with -Fuc, GlcNAc moieties whereas -GalNAc, -Gal-(1–3)-GalNAc, -Gal-(1–4)-GlcNAc and -Gal residues belonged only to O-linked glycoproteins. The acinar and ductal cells expressed -Man/-Glc in N-linked oligosaccharides, GlcNAc in both O- and N-glycoproteins and -GalNAc, -Gal-(1–3)-GalNAc, -Gal-(1–4)-GlcNAc and -Gal residues included in O-linked glycoproteins. The Golgi area of the epithelial lining expressed -Fuc in O-linked glycoproteins, internal GlcNAc in N-linked glycoproteins and large amounts of sialic acid residues linked to subterminal -GalNAc, Gal1,4GlcNAc and Gal1,3GalNAc. High amounts of sulpho-carbohydrates and of sialic acids (2,3–6), linked to-/-Gal and sialic acids (2–6) linked to -GalNAc, were also demonstrated. Such diversity of the mucin saccharide residues may be implicated in the binding of macromolecules such as those of bacterial or viral etiology, thus playing a role in the organism’s host-defense mechanism in the guttural pouches.

Glycoprofile of the different cell types present in the mucosa of the horse guttural pouches.

PARILLO, Francesco;
2009-01-01

Abstract

Histochemical characterization of the equine guttural pouches was performed using lectins combined with sialidase digestion and deglycosylation pre-treatments. The goblet cells contained O- and N-linked oligosaccharides with -Fuc, GlcNAc moieties whereas -GalNAc, -Gal-(1–3)-GalNAc, -Gal-(1–4)-GlcNAc and -Gal residues belonged only to O-linked glycoproteins. The acinar and ductal cells expressed -Man/-Glc in N-linked oligosaccharides, GlcNAc in both O- and N-glycoproteins and -GalNAc, -Gal-(1–3)-GalNAc, -Gal-(1–4)-GlcNAc and -Gal residues included in O-linked glycoproteins. The Golgi area of the epithelial lining expressed -Fuc in O-linked glycoproteins, internal GlcNAc in N-linked glycoproteins and large amounts of sialic acid residues linked to subterminal -GalNAc, Gal1,4GlcNAc and Gal1,3GalNAc. High amounts of sulpho-carbohydrates and of sialic acids (2,3–6), linked to-/-Gal and sialic acids (2–6) linked to -GalNAc, were also demonstrated. Such diversity of the mucin saccharide residues may be implicated in the binding of macromolecules such as those of bacterial or viral etiology, thus playing a role in the organism’s host-defense mechanism in the guttural pouches.
2009
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11581/115469
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