Receptor-mediated endocytosis of fucosylated neoglycoprotein by macrophages

Sarkar, Kakali ; Sarkar, Himadri Sekhar ; Kole, Labanyamo ; Das, Pijush K. (1996) Receptor-mediated endocytosis of fucosylated neoglycoprotein by macrophages Molecular and Cellular Biochemistry, 156 (2). pp. 109-116. ISSN 0300-8177

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The characteristics of the recognition system involved in the receptor mediated endocytosis of the neoglycoprotein, fucose human serum albumin (HSA) were studied. It was found that (i) fucose-HSA showed strong affinity binding and uptake by various macrophages; (ii) binding was specific for L-fucose and D-mannose; (iii) binding was found to be inhibited by oxidant like H2O2 and swainsonine whereas it was elevated by dexamethasone; (iv) clearance of125I-fucose-HSA was rapid and strongly inhibited by unlabelled fucose-HSA. Greater than 70% of fucose-HSA was found in liver and more than 60% of this was found in liver lysosomes; (v) uptake of fucose-HSA was thirty-fold more efficient in liver macrophages (Kupffer cells) than in hepatocytes; (vi) moreover, mannose-HSA and ovalbumin which are potent inhibitors of mannose/N-acetylglucosamine receptors inhibited clearance and uptake of fucose-HSA by liver as well as by isolated Kupffer cells suggesting the involvement of both fucose and mannose receptors or a single type of receptor having greater affinity for fucose-HSA than for mannose-HSA. These results emphasize the important role of fucose-terminated glycoproteins in site-specific drug targeting.

Item Type:Article
Source:Copyright of this article belongs to Springer-Verlag.
Keywords:Macrophages; Neoglycoproteins; Sugar Receptors; Endocytosis
ID Code:30480
Deposited On:23 Dec 2010 13:32
Last Modified:31 May 2011 06:43

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