The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Asialoglycoprotein receptors as important mediators of plasma lipids and atherosclerosis
Abstract
Purpose of review: This review seeks to describe the role of the asialoglycoprotein receptor (ASGR) in modulating non-HDL lipoprotein levels, platelet numbers and atherosclerosis. Recent findings: Genetics studies have revealed that ASGR haplodeficiency provides protection from atherosclerosis. The potential interactions of ASGR with LDL receptor may regulate the rate of LDL uptake and as a result may lower plasma non-HDL cholesterol. ASGR clears senescent platelets and induces the expression of hepatic thrombopoietin. Platelet activity promotes plaque formation and atherosclerosis. Summary: ASGR is a multifunctional receptor specializing in clearance of desialylated glycoproteins and platelets. The impact of ASGR on the levels of plasma non-HDL cholesterol makes it a potential therapeutic target for the treatment of hypercholesterolemia and atherosclerosis.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
ASGRs are internalized from the cell surface via clathrin-coated vesicles into endosomes and are rapidly recycled constitutively even in the absence of a ligand.
“ASGRs are internalized from the cell surface via clathrin-coated vesicles into endosomes and are rapidly recycled constitutively even in the absence of a ligand (11).”
From Asialoglycoprotein receptor 1 is a novel PCSK9-independent ligand of liver LDLR cleaved by furin (2021) · cites this paper as [11]
ASGR consists of two subunits, ASGR1 (major) and ASGR2 (minor).
“It consists of two subunits, ASGR1 (major) and ASGR2 (minor), and plays a critical role in serum glycoprotein homeostasis by mediating the endocytosis and lysosomal degradation of desialylated glycoproteins with exposed terminal galactose or N-acetylgalactosamine residues (11).”
From Asialoglycoprotein receptor 1 is a novel PCSK9-independent ligand of liver LDLR cleaved by furin (2021) · cites this paper as [11]
So far, the known ligands of ASGRs are soluble desialylated proteins, including von Willebrand factor and exogenous proteins such as asialofuetin and asialo-orosomucoid.
“So far, the known ligands of ASGRs are soluble desialylated proteins, including von Willebrand factor (11) and exogenous proteins (e.g., asialofuetin, asialo-orosomucoid) (32).”
From Asialoglycoprotein receptor 1 is a novel PCSK9-independent ligand of liver LDLR cleaved by furin (2021) · cites this paper as [11]
ASGR plays a critical role in serum glycoprotein homeostasis by mediating the endocytosis and lysosomal degradation of desialylated glycoproteins with exposed terminal galactose or N-acetylgalactosamine residues.
“It consists of two subunits, ASGR1 (major) and ASGR2 (minor), and plays a critical role in serum glycoprotein homeostasis by mediating the endocytosis and lysosomal degradation of desialylated glycoproteins with exposed terminal galactose or N-acetylgalactosamine residues (11).”
From Asialoglycoprotein receptor 1 is a novel PCSK9-independent ligand of liver LDLR cleaved by furin (2021) · cites this paper as [11]
Strategies aimed at inhibiting ASGR1 expression or activity are being explored as another approach to lowering plasma LDL cholesterol and cardiovascular disease risk.
“Strategies aimed at inhibiting ASGR1 expression/activity are being explored as another approach to lowering plasma LDLc and CVD risk (11).”
From Asialoglycoprotein receptor 1 is a novel PCSK9-independent ligand of liver LDLR cleaved by furin (2021) · cites this paper as [11]
The present data are the first to identify the secretory membrane-bound LDLR as a physiological target of ASGR1, as opposed to soluble desialylated glycoproteins such as von Willebrand factor.
“The present data are the first to identify the secretory membrane-bound LDLR as a physiological target of ASGR1, as opposed to soluble desialylated glycoproteins, e.g., von Willebrand factor (24), normally thought to be sensitive to hepatocyte-derived ASGR1 regulation (11).”
From Asialoglycoprotein receptor 1 is a novel PCSK9-independent ligand of liver LDLR cleaved by furin (2021) · cites this paper as [11]
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 [11]
Citations
Cites
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
Flagged first, then by citations
Research works printed but not linked: 38
- Ashwell, 1982, Carbohydrate-specific receptors of the liver, Annu Rev Biochem, 51, 531, 10.1146/annurev.bi.51.070182.002531 · DOI · Paper page
- Spiess, 1985, Sequence of a second human asialoglycoprotein receptor: conservation of two receptor genes during evolution, Proc Natl Acad Sci U S A, 82, 6465, 10.1073/pnas.82.19.6465 · DOI
- Weigel, 1994, Galactosyl and N-acetylgalactosaminyl homeostasis: a function for mammalian asialoglycoprotein receptors, Bioessays, 16, 519, 10.1002/bies.950160713 · DOI
- Chiacchia, 1984, Direct evidence for the transmembrane orientation of the hepatic glycoprotein receptors, J Biol Chem, 259, 15440, 10.1016/S0021-9258(17)42568-3 · DOI
- Yik, 2002, The minor subunit splice variants, H2b and H2c, of the human asialoglycoprotein receptor are present with the major subunit H1 in different hetero-oligomeric receptor complexes, J Biol Chem, 277, 23076, 10.1074/jbc.M202748200 · DOI
- Weis, 1992, Structure of a C-type mannose-binding protein complexed with an oligosaccharide, Nature, 360, 127, 10.1038/360127a0 · DOI
- Breitfeld, 1984, Influence of the N-linked oligosaccharides on the biosynthesis, intracellular routing, and function of the human asialoglycoprotein receptor, J Biol Chem, 259, 10414, 10.1016/S0021-9258(18)90980-4 · DOI
- Ishibashi, 1994, Asialoglycoprotein receptor deficiency in mice lacking the minor receptor subunit, J Biol Chem, 269, 27803, 10.1016/S0021-9258(18)46855-X · DOI
- Tozawa, 2001, Asialoglycoprotein receptor deficiency in mice lacking the major receptor subunit. Its obligate requirement for the stable expression of oligomeric receptor, J Biol Chem, 276, 12624, 10.1074/jbc.M011063200 · DOI · Paper page
- Rumjantseva, 2009, Dual roles for hepatic lectin receptors in the clearance of chilled platelets, Nat Med, 15, 1273, 10.1038/nm.2030 · DOI
- Mi, 2016, Functional consequences of mannose and asialoglycoprotein receptor ablation, J Biol Chem, 291, 18700, 10.1074/jbc.M116.738948 · DOI
- Tolleshaug, 1979, Chloroquine reduces the number of asialo-glycoprotein receptors in the hepatocyte plasma membrane, Biochem Pharmacol, 28, 2919, 10.1016/0006-2952(79)90586-0 · DOI
- Ciechanover, 1983, Sorting and recycling of cell surface receptors and endocytosed ligands: the asialoglycoprotein and transferrin receptors, J Cell Biochem, 23, 107, 10.1002/jcb.240230111 · DOI
- Tycko, 1983, Rapid acidification of endocytic vesicles containing asialoglycoprotein in cells of a human hepatoma line, J Cell Biol, 97, 1762, 10.1083/jcb.97.6.1762 · DOI
- Fuhrer, 1991, Endocytosis of the ASGP receptor H1 is reduced by mutation of tyrosine-5 but still occurs via coated pits, J Cell Biol, 114, 423, 10.1083/jcb.114.3.423 · DOI
- Feinberg, 2000, Mechanism of pH-dependent N-acetylgalactosamine binding by a functional mimic of the hepatocyte asialoglycoprotein receptor, J Biol Chem, 275, 35176, 10.1074/jbc.M005557200 · DOI
- Loeb, 1988, Conformational changes in the chicken receptor for endocytosis of glycoproteins. Modulation of ligand-binding activity by Ca2+ and pH, J Biol Chem, 263, 9752, 10.1016/S0021-9258(19)81582-X · DOI
- Bider, 1998, Ligand-induced endocytosis of the asialoglycoprotein receptor: evidence for heterogeneity in subunit oligomerization, FEBS Lett, 434, 37, 10.1016/S0014-5793(98)00947-8 · DOI
- Pshezhetsky, 1997, Cloning, expression and chromosomal mapping of human lysosomal sialidase and characterization of mutations in sialidosis, Nat Genet, 15, 316, 10.1038/ng0397-316 · DOI · Paper page
- Monti, 1999, Cloning and characterization of NEU2, a human gene homologous to rodent soluble sialidases, Genomics, 57, 137, 10.1006/geno.1999.5749 · DOI
- Monti, 2000, Identification and expression of NEU3, a novel human sialidase associated to the plasma membrane, Biochem J, 349, 343, 10.1042/bj3490343 · DOI
- Comelli, 2003, Identification and expression of Neu4, a novel murine sialidase, Gene, 321, 155, 10.1016/j.gene.2003.08.005 · DOI
- Igdoura, 1998, Cloning of the cDNA and gene encoding mouse lysosomal sialidase and correction of sialidase deficiency in human sialidosis and mouse SM/J fibroblasts, Hum Mol Genet, 7, 115, 10.1093/hmg/7.1.115 · DOI
- Bonten, 2009, Heterodimerization of the sialidase NEU1 with the chaperone protective protein/cathepsin A prevents its premature oligomerization, J Biol Chem, 284, 28430, 10.1074/jbc.M109.031419 · DOI · Paper page
- Galjart, 1991, Human lysosomal protective protein has cathepsin A-like activity distinct from its protective function, J Biol Chem, 266, 14754, 10.1016/S0021-9258(18)98751-X · DOI · Paper page
- van der Spoel, 1998, Transport of human lysosomal neuraminidase to mature lysosomes requires protective protein cathepsin A, Embo Journal, 17, 1588, 10.1093/emboj/17.6.1588 · DOI · Paper page
- Bonten, 1995, Lysosomal protective protein/cathepsin A. Role of the ‘linker’ domain in catalytic activation, J Biol Chem, 270, 26441, 10.1074/jbc.270.44.26441 · DOI · Paper page
- Yang, 2012, Hypomorphic sialidase expression decreases serum cholesterol by downregulation of VLDL production in mice, J Lipid Res, 53, 2573, 10.1194/jlr.M027300 · DOI
- Breslow, 1988, Apolipoprotein genetic variation and human disease, Physiol Rev, 68, 85, 10.1152/physrev.1988.68.1.85 · DOI
- Chen, 2003, APOE polymorphism and angiographic coronary artery disease severity in the Women's Ischemia Syndrome Evaluation (WISE) study, Atherosclerosis, 169, 159, 10.1016/S0021-9150(03)00160-6 · DOI
- Luc, 1994, Impact of apolipoprotein E polymorphism on lipoproteins and risk of myocardial infarction. The ECTIM Study, Arterioscler Thromb, 14, 1412, 10.1161/01.ATV.14.9.1412 · DOI
- Semple, 2011, Platelets and the immune continuum, Nat Rev Immunol, 11, 264, 10.1038/nri2956 · DOI
- Broijersen, 1998, Platelet activity in vivo in hyperlipoproteinemia: importance of combined hyperlipidemia, Thromb Haemost, 79, 268, 10.1055/s-0037-1615005 · DOI
- Mestas, 2008, Monocyte-endothelial cell interactions in the development of atherosclerosis, Trends Cardiovasc Med, 18, 228, 10.1016/j.tcm.2008.11.004 · DOI
- Tailor, 2003, Hypercholesterolemia promotes P-selectin-dependent platelet-endothelial cell adhesion in postcapillary venules, Arterioscler Thromb Vasc Biol, 23, 675, 10.1161/01.ATV.0000056742.97580.79 · DOI
- Grozovsky, 2015, The Ashwell-Morell receptor regulates hepatic thrombopoietin production via JAK2-STAT3 signaling, Nat Med, 21, 47, 10.1038/nm.3770 · DOI
- Skripchenko, 2014, Addition of sialidase or p38 MAPK inhibitors does not ameliorate decrements in platelet in vitro storage properties caused by 4 degrees C storage, Vox Sang, 107, 360, 10.1111/vox.12174 · DOI
- Cyrus, 2002, Effect of low-dose aspirin on vascular inflammation, plaque stability, and atherogenesis in low-density lipoprotein receptor-deficient mice, Circulation, 106, 1282, 10.1161/01.CIR.0000027816.54430.96 · DOI
Cited by
Sorted by citations
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
- Igdoura, S. A.
- Venue
- Current Opinion in Lipidology
- Published
- 2017-04
- Volume
- 28
- Issue
- 2
- Pages
- 209-212
- ISSN
- 0957-9672
- 1473-6535
- Cited by
- 22
- References
- 1
- Language
- en
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review