Uptake of dimannoside clusters and oligomannosides by human dendritic cells.
Biosci Rep
; 21(6): 839-55, 2001 Dec.
Article
in En
| MEDLINE
| ID: mdl-12166831
ABSTRACT
Knowing that human blood monocyte-derived dendritic cells express cell-surface mannose-specific lectins, we prepared various mannoses containing glycoconjugates with the aim of developing highly specific synthetic carriers of oligonucleotides and genes. Conjugates were prepared from oligosaccharides obtained by hydrazinolysis of Saccharomyces cerevisiae invertase glycopeptides. The reducing saccharides were converted into glycosynthons, i.e., into glyco-amino acids. Fluorescein derivatives were obtained by coupling the free carboxyl group of oligosaccharyl-pyroglutamate to the alpha-amino group of epsilon-fluoresceinyl-thiocarbamyl lysine methyl ester. It has been shown by others that glycosylated linear oligolysines containing up to six alpha-D-mannopyranosylphenylthiocarbamyl units have a high affinity for the human mannose receptor. In order to obtain fully biodegradable clusters and to improve both the specificity and the selectivity, disaccharides transformed into glycosynthons were coupled to pentalysine carriers (Lys5-Ala-Cys-NH2). Glycosylated pentalysyl cysteine conjugates were made fluorescent upon substitution of the cysteine thiol group with fluorescein iodoacetamide. As shown by flow cytofluorimetry, both the dimannoside clusters and yeast oligomannosides were very efficiently taken up by DC, conversely lactoside clusters were not.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Dendritic Cells
/
Endocytosis
/
Mannosides
Limits:
Humans
Language:
En
Journal:
Biosci Rep
Year:
2001
Document type:
Article
Affiliation country:
France