The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Glycans as endocytosis signals: the cases of the asialoglycoprotein and hyaluronan/chondroitin sulfate receptors
Abstract
Animal cells internalize specific extracellular macromolecules (ligands) by using specialized cell surface receptors that operate through a complex and highly regulated process known as receptor-mediated endocytosis, which involves the binding, internalization, and transfer of ligands through a series of distinct intracellular compartments. For the uptake of a variety of carbohydrate-containing macromolecules, such as glycoproteins, animal cells use specialized membrane-bound lectins as endocytic receptors that recognize different sugar residues or carbohydrate structures present on various ligands. The hepatic asialoglycoprotein receptor, which recognizes glycoconjugates containing terminal galactose or N-acetylgalactosamine residues, was the first membrane lectin discovered and has been a classical system for studying receptor-mediated endocytosis. Studies of how the asialoglycoprotein receptor functions have led to the discovery of two functionally distinct, parallel pathways of clathrin-mediated endocytosis (called the State 1 and State 2 pathways), which may also be utilized by all the other endocytic recycling receptor systems. Another endocytic membrane lectin, the hyaluronan/chondroitin sulfate receptor, which has recently been purified and cloned, is responsible for the turnover in mammals of these glycosaminoglycans, which are important components of extracellular matrices. We discuss the characteristics and physiological importance of these two proteins as examples…
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Glycoprotein ASGR ligands contain terminal galactose or N-acetylgalactosamine, with the latter being the preferred residue.
“Glycoprotein ASGR ligands contain terminal galactose or N-acetylgalactosamine, with the latter being the preferred residue (31).”
From Asialoglycoprotein receptor 1 is a novel PCSK9-independent ligand of liver LDLR cleaved by furin (2021) · cites this paper as [31]
Oligomerization of the ASGR subunits via their respective stalk regions occurs in the endoplasmic reticulum.
“Oligomerization of the ASGR subunits via their respective stalk regions occurs in the ER (31).”
From Asialoglycoprotein receptor 1 is a novel PCSK9-independent ligand of liver LDLR cleaved by furin (2021) · cites this paper as [31]
At steady state, approximately 40% to 60% of total cellular ASGRs are on the cell surface.
“Thus, at steady state ∼40% to 60% of total cellular ASGRs are on the cell surface (31).”
From Asialoglycoprotein receptor 1 is a novel PCSK9-independent ligand of liver LDLR cleaved by furin (2021) · cites this paper as [31]
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 [31]
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 [31]
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 [31]
ASGRs are primarily known to interact with circulating factors.
“since ASGRs are primarily known to interact with circulating factors (11, 31).”
From Asialoglycoprotein receptor 1 is a novel PCSK9-independent ligand of liver LDLR cleaved by furin (2021) · cites this paper as [31]
Citations
Cites
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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The Ashwell receptor mitigates the lethal coagulopathy of sepsis
Grewal, P. K., Uchiyama, S., Ditto, D., Varki, N., Le, D. T., Nizet, V., & Marth, J. D. (2008) · Nature Medicine · doi:10.1038/nm1760 · Cited by 374
Solís, D., Bovin, N. V., Davis, A. P., Jiménez-Barbero, J., Romero, A., Roy, R., Smetana, K., & Gabius, H.-J. (2015) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.03.016 · Cited by 222
Variant ASGR1 Associated with a Reduced Risk of Coronary Artery Disease
Nioi, P., Sigurdsson, A., Thorleifsson, G., Helgason, H., Agustsdottir, A. B., Norddahl, G. L., Helgadottir, A., Magnusdottir, A., Jonasdottir, A., Gretarsdottir, S., et al. (2016) · New England Journal of Medicine · doi:10.1056/nejmoa1508419 · Cited by 189
Wahrenbrock, M. G., & Varki, A. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-3851 · Cited by 58
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
- Weigel, P.
- Venue
- Biochimica et Biophysica Acta (BBA) - General Subjects
- Publisher
- Elsevier BV
- Published
- 2002-09-19
- Volume
- 1572
- Issue
- 2-3
- Pages
- 341-363
- ISSN
- 0304-4165
- Cited by
- 208
- References
- 1
- Language
- en
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