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The influence of mannose-containing oligosaccharides on the tissue uptake of glycoproteins has been examined with synthetic glycoconjugates. Oligosaccharides obtained from the acetolysis of bakers' yeast mannan have been coupled to the lysine residues of the cross-linked dimer of bovine pancreatic ribonuclease A and of human serum albumin by reductive amination with cyanoborohydride. 14C-labeled derivatives of the two proteins containing two to four mannopyranose residues per 10,000 mol wt were administered intravenously to rats. There was selective (70-80%) uptake of these derivatives by the liver within 10-15 min after injection. A minor site of uptake was the spleen. The extent of hepatic uptake was a function of the number and size of the mannooligosaccharide residues coupled. With the nonglycosaminated derivatives the liver uptake was less than 5%. Related studies have shown that mannose-containing glycoproteins are taken up by both the endothelial and Kupffer cells of the liver; thus, reductive mannosamination may provide a means of directing to these cells proteins of potential therapeutic interest.

Selective hepatic uptake of synthetic glycoproteins: mannosaminated ribonuclease A dimer and serum albumin.