Lamp-1 does not acquire the large polylactosaminoglycans characteristic of F9 cells.
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.[1]References
- Lamp-1 does not acquire the large polylactosaminoglycans characteristic of F9 cells. Romero, P.A., Way, T., Herscovics, A. Biochem. J. (1993) [Pubmed]
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