L-Fucose-terminated glycoconjugates are recognized by pinocytosis receptors on macrophages

V. L. Shepherd, Y. C. Lee, P. H. Schlesinger, P. D. Stahl

Research output: Contribution to journalArticlepeer-review

126 Scopus citations


125I-Labeled L-fucose-albumin complex and rat preputial β-glucuronidase are rapidly cleared from plasma after intravenous infusion. L-Fucose-albumin retards the plasma clearance of β-glucuronidase whereas D-fucose-albumin is inactive. In vitro, 125I-labeled L-fucose-albumin is taken up into rat or rabbit alveolar macrophages by receptor-mediated pinocytosis. Uptake (37°C) is time-dependent, is saturable with increasing ligand concentration (K(uptake) = 4.4 x 10-8M), and requires Ca2+. 125I-Labeled D-fucose-albumin is poorly taken up. Binding (4°C) is saturable and Ca2+ dependent. Binding and uptake are fully inhibited by yeast mannan. A series of neoglycoproteins, including L-fucose-albumin, were tested as inhibitors of uptake of 125I-labeled β-glucuronidase into macrophages. The following order of potency was observed: L-Fuc= D-Man>GlcNAc nearly equal to D-Glc>D-Xyl >>>D-Gal=L-Ara=D-Fuc. L-Fucose-terminated oligosaccharides coupled to bovine serum albumin also block 125I-labeled β-glucuronidase uptake into macrophages.

Original languageEnglish
Pages (from-to)1019-1022
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number2 II
StatePublished - 1981

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