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Presence of terminal N-acetylgalactosamine residues in subregions of the endoplasmic reticulum is influenced by cell differentiation in culture

Opened Access Presence of terminal N-acetylgalactosamine residues in subregions of the endoplasmic reticulum is influenced by cell differentiation in culture
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Autor: Pérez Vilar, J.
Hidalgo Jiménez, Josefina
Velasco López, Ángel
Departamento: Universidad de Sevilla. Departamento de Biología Celular
Fecha: 1991
Publicado en: The Journal of Biological Chemistry, 266 (35, Issue of December 15),23967-23976
Tipo de documento: Artículo
Resumen: Using Helix pomatia lectin as a specific probe for terminal, nonreducing N-acetylgalactosamine residues, glycoprotein precursors bearing newly initiated O-linked oligosaccharides have been localized in the lumen of the endoplasmic reticulum and cis-Golgi cisternae. This pattern contrasts with the detection of the terminal disaccharide galactose beta-1,3-N-acetylgalactosamine by Arachis hypogaea lectin in middle and trans-Golgi compartments, which are considered elongation sites for O-glycosylation. Distribution of H. pomatia ligands in the endoplasmic reticulum is confined to specialized regions or subcompartments in both human colonic adenocarcinoma cells and cultured chicken chondrocytes. Since in cartilage, chondrocytes contain H. pomatia-binding sites exclusively concentrated in cis-Golgi cisternae, primary cultures of this cell type have been used to study those conditions that promote initiation of O-glycosylation in the endoplasmic reticulum. A correlation has been found betwee...
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URI: http://hdl.handle.net/11441/40672

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