Although F9 cells labelled with [3H]glucosamine synthesize many glycoproteins that bind to Datura stramonium agglutinin-agarose, only a small proportion of these were immunoprecipitated with monoclonal antibodies to lamp-1 and lamp-2 (lamp = lysosomal membrane protein). Differentiation of F9 cells by retinoic acid increased labelling of all Datura stramonium-bound glycoproteins, including lamp-1 and lamp-2. Although the large polylactosaminoglycans excluded from Bio-Gel P-6 that are characteristic of F9 cells were obtained from total glycoproteins, little of these large polylactosaminoglycans was found on lamp-1 and lamp-2. There was no increase in large polylactosaminoglycans of lamp-1 and lamp-2 after retinoic acid treatment, but an increase in the size of small polylactosaminoglycans (included on Bio-Gel P-6) and tri- and tetra-antennary complex oligosaccharides. Therefore, other factors besides the expression of specific glycosyltransferases determine the extent of elongation of polylactosaminoglycans on lysosomal membrane proteins.
Research Article|November 15 1993
Lamp-1 does not acquire the large polylactosaminoglycans characteristic of F9 cells
P A Romero;
Biochem J (1993) 296 (1): 253-257.
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P A Romero, T Way, A Herscovics; Lamp-1 does not acquire the large polylactosaminoglycans characteristic of F9 cells. Biochem J 15 November 1993; 296 (1): 253–257. doi: https://doi.org/10.1042/bj2960253
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