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Transferrin Glycans
Author(s) -
Regoeczi Erwin,
Chindemi Paul A.,
Debanne Maria T.
Publication year - 1984
Publication title -
alcoholism: clinical and experimental research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.267
H-Index - 153
eISSN - 1530-0277
pISSN - 0145-6008
DOI - 10.1111/j.1530-0277.1984.tb05513.x
Subject(s) - transferrin , sialic acid , catabolism , chemistry , biochemistry , carbohydrate deficient transferrin , hepatocyte , glycan , metabolism , biology , glycoprotein , alcohol , in vitro , alcohol consumption
The hepatic uptake of 59Fe from diferrtc rat and rabbit asialotrans‐ferrins and from human transferrin lacking two sialyl residues was investigated in rats in experiments lasting for 1 hr. The 59Fe attached to either of these preparations disappeared from the plasma more rapidly than the 59Fe introduced with the unmodified respective parent proteins. Most of the 59Fe activity that had disappeared from the circulation could be recovered with the liver. Studies with double‐labeled (125I, 58Fe) preparations showed that the enhanced 58Fe clearance was not associated with increased catabolism of the modified transferrins. Prolonged, heavy alcohol consumption, as shown by others, results in the appearance of sialic acid‐deficient transferrin (two residues missing) in human serum. We suggest that the increased capacity of transferrin deficient in sialic acid to selectively deposit iron in the nepatocyte may be of significance for the development of the hepatic siderosis observed in alcoholism.