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Two asialoglycoprotein receptor polypeptides in human hepatoma cells
Abstract
Two cDNA clones isolated from a HepG2 lambda gt11 library encode the classical asialoglycoprotein receptor, H1, as well as a homologous membrane glycoprotein, H2 (Spiess, M., and Lodish, H.F. (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 6465-6469). To study the relationship of H2 to H1 and its possible role in receptor-mediated endocytosis of desialyated glycoproteins, we generated anti-peptide antibodies that are specific for each polypeptide. As judged by metabolic labeling of HepG2 cells and specific immunoadsorption, the biosynthesis of H2 is similar to H1 (Schwartz, A.L., and Rup, D. (1983) J. Biol. Chem. 258, 11249-11255); H2 is synthesized as a 43,000-dalton precursor polypeptide containing high mannose-type oligosaccharides, that is processed to a 50,000-dalton mature glycoprotein containing complex-type oligosaccharides. Both H1 and H2 have a half-life of approximately 12 h. Trypsin and neuraminidase digestion of intact cells at 4 and 12 degrees C was used to determine that, at steady state, 50-60 percent of both H1 and H2 are on the cell surface. Furthermore, all of the H2 molecules were digested by extracellular neuraminidase in 1 h at 37 degrees C, indicating that all gain access to the plasma membrane. Both H1 and H2 were purified to homogeneity when Triton X-100-solubilized membrane proteins from [35S]cysteine-labeled cells were subjected to affinity chromatography on galactose-agarose. Since we cannot detect a complex between mature H1 and H2, H2 must be a galactos…
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In humans, the functional ASGR is composed of two subunits, ASGR1 (major, approximately 46 kDa) and ASGR2 (minor, approximately 50 kDa), that exist as homo-oligomers or hetero-oligomers in a molar ratio of approximately 3:1.
“In humans, the functional receptor is composed of two subunits, ASGR1 (major, ∼46 kDa) and ASGR2 (minor, ∼50 kDa), that exist as homo-oligomers or hetero-oligomers in a molar ratio of ∼3:1, respectively (13, 31).”
From Asialoglycoprotein receptor 1 is a novel PCSK9-independent ligand of liver LDLR cleaved by furin (2021) · cites this paper as [13]
Hepatic ASGR is pivotal for the efficient clearance of desialylated glycoproteins from circulation by receptor-mediated endocytosis and lysosomal degradation, whereupon ASGR is recycled back to the cell surface.
“The hepatic ASGR is pivotal for the efficient clearance of desialylated glycoproteins from circulation by receptor-mediated endocytosis and lysosomal degradation, whereupon ASGR is recycled back to the cell surface (13, 31).”
From Asialoglycoprotein receptor 1 is a novel PCSK9-independent ligand of liver LDLR cleaved by furin (2021) · cites this paper as [13]
Both ASGR subunits are type II, single-pass transmembrane proteins.
“Both subunits are type II, single-pass transmembrane proteins.”
From Asialoglycoprotein receptor 1 is a novel PCSK9-independent ligand of liver LDLR cleaved by furin (2021) · cites this paper as [13]
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Carbohydrate-Specific Receptors of the Liver
Ashwell, G., & Harford, J. (1982) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.51.070182.002531 · Cited by 1,914
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Ebenezer, O., Comoglio, P., Wong, G. K.-S., & Tuszynski, J. A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24044019 · Cited by 39
Asialoglycoprotein receptor 1 is a novel PCSK9-independent ligand of liver LDLR cleaved by furin
Susan-Resiga, D., Girard, E., Essalmani, R., Roubtsova, A., Marcinkiewicz, J., Derbali, R. M., Evagelidis, A., Byun, J. H., Lebeau, P. F., Austin, R. C., et al. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101177 · Cited by 34
Metadata
- Authors
- Bischoff, J., & Lodish, H. F.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1987-08
- Volume
- 262
- Issue
- 24
- Pages
- 11825-11832
- ISSN
- 0021-9258
- Cited by
- 78
- References
- 1
- Language
- en
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