The Journal of General Physiology, Vol 74, 495-509, Copyright © 1979 by The Rockefeller University Press
Selective hepatic uptake of synthetic glycoproteins: mannosaminated ribonuclease A dimer and serum albumin
G Wilson
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.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Facebook 
Reddit 
Technorati 
Twitter What's this?
