Diacytosis of asialoglycoprotein in isolated hepatocytes is dependent on the structure of ligand and cellular distribution of the receptors.

Biochimica Et Biophysica Acta
T M Chang, C H Chang

Abstract

Diacytosis, degradation and retention of 125I-labeled asialoorosomucoid (ASOR), its reduced and carboxymethylated N-terminal cyanogen bromide-cleaved fragment (RC-ASCNBr-I) and asialofetuin preloaded into isolated rat or rabbit hepatocytes for various periods of time were compared. In rat hepatocytes preloaded with a saturating concentration (3.10(-8) M) of the ligands, the proportion of the preloaded ligands distributed to degradation and diacytosis was fairly constant during 4 h of preincubation. In addition, a small portion of the preloaded ligands was neither diacytosed nor degraded, but was retained intracellularly. Diacytosis of 125I-ASOR (29%) was greater than that of either 125I-RC-ASCNBr-I (23%) or 125I-asialofetuin (15%). Diacytosis of 125I-ASOR, when preloaded in the presence of 5 microM colchicine, was significantly enhanced by 79% (increasing from 29% to 52%), whereas those of 125I-RC-ASCNBr-I and 125I-asialofetuin were not significantly altered (with average increases of 14% and 19%, respectively). The fraction of the preloaded 125I-asialofetuin (69%) and 125I-RC-ASCNBr-I (68.6%) that was degraded was slightly higher than that of 125I-ASOR (64%) and all was decreased by colchicine. The fraction of all three ligand...Continue Reading

References

Jan 1, 1982·Annual Review of Biochemistry·G Ashwell, J Harford
Nov 17, 2007·Clinical Cancer Research : an Official Journal of the American Association for Cancer Research·Lee S RosenChristopher G Willett

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Citations

Oct 6, 2000·The Journal of Cell Biology·E BananisA W Wolkoff
May 14, 2020·Metallomics : Integrated Biometal Science·Marie MonestierElisabeth Mintz

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