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Journal articles on the topic 'Asialoglycoproteine'

Author: Grafiati

Published: 4 June 2021

Last updated: 6 February 2022

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1

Schiff, J. M., M. M. Fisher, A. L. Jones, and B. J. Underdown. "Human IgA as a heterovalent ligand: switching from the asialoglycoprotein receptor to secretory component during transport across the rat hepatocyte." Journal of Cell Biology 102, no. 3 (March 1, 1986): 920–31. http://dx.doi.org/10.1083/jcb.102.3.920.

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Asialoglycoproteins are taken up by the rat liver for degradation; rat polymeric IgA is taken up via a separate receptor, secretory component (SC), for quantitative delivery to bile. There is negligible uptake of these ligands by the converse receptor, and only a low level of missorting of ligands to opposite destinations. The two pathways are not cross-inhibitable and operate independently (Schiff, J.M., M. M. Fisher, and B. J. Underdown, 1984, J. Cell Biol., 98:79-89). We report here that when human IgA is presented as a ligand in the rat, it is processed using elements of both pathways. To study this in detail, different IgA fractions were prepared using two radiolabeling methods that provide separate probes for degradation or re-secretion. Behavior of intravenously injected human polymeric IgA in the rat depended on its binding properties. If deprived of SC binding activity by affinity adsorption or by reduction and alkylation, greater than 80% of human IgA was degraded in hepatic lysosomes; radioactive catabolites were released into bile by a leupeptin-inhibitable process. If prevented from binding to the asialoglycoprotein receptor by competition or by treatment with galactose oxidase, human IgA was cleared and transported to bile directly via SC, but its uptake was about fivefold slower than rat IgA. Untreated human IgA was taken up rapidly by the asialoglycoprotein receptor, but depended on SC binding to get to bile: the proportion secreted correlated 1:1 with SC binding activity determined in vitro, and the IgA was released into bile with SC still attached. These results demonstrate that human IgA is normally heterovalent: it is first captured from blood by the asialoglycoprotein receptor, but escapes the usual fate of asialoglycoproteins by switching to SC during transport. Since the biliary transit times of native human and rat IgA are the same, it is probable that the receptor switching event occurs en route. This implies that the two receptors briefly share a common intracellular compartment.

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2

Kaufman, S. S., P. L. Blain, J. H. Park, and D. J. Tuma. "Role of microfilaments in asialoglycoprotein processing in adult and developing liver." American Journal of Physiology-Gastrointestinal and Liver Physiology 259, no. 4 (October 1, 1990): G639—G645. http://dx.doi.org/10.1152/ajpgi.1990.259.4.g639.

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To assess the role of microfilaments in receptor-mediated endocytosis of asialoglycoproteins, hepatocytes isolated from adult and 6-day-old rats were treated with the antimicrofilamentous agent cytochalasin D and then incubated with 125I-asialoorosomucoid (ASOR). Cytochalasin D (50 microM) reduced degradation of continuously endocytosed ASOR (7.5 micrograms/ml) equally in adult and neonate to approximately 20% of control. Internalization of surface-bound ASOR suggested at least two discrete sites at which ligand translocation was inhibited by drug at both ages: 1) initial movement of receptor-ligand complex from cell surface to interior and 2) postinternalization ligand transit to lysosomes. Inhibition of plasma membrane translocation was confirmed by calculation of endocytotic rate constant (Ke) values, which were decreased to approximately 20-30% of control after cytochalasin D treatment. In contrast, the antimicrotubular drug colchicine did not reduce Ke values significantly nor did colchicine in combination with cytochalasin D impede lysosome-directed transport more than cytochalasin D alone. These results indicate that internalization of occupied asialoglycoprotein surface receptor is microfilament dependent irrespective of postnatal age and that subsequent participation of microfilaments in asialoglycoprotein trafficking is closely related to that of microtubules.

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3

Stoorvogel, W., H. J. Geuze, and G. J. Strous. "Sorting of endocytosed transferrin and asialoglycoprotein occurs immediately after internalization in HepG2 cells." Journal of Cell Biology 104, no. 5 (May 1, 1987): 1261–68. http://dx.doi.org/10.1083/jcb.104.5.1261.

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After receptor-mediated uptake, asialoglycoproteins are routed to lysosomes, while transferrin is returned to the medium as apotransferrin. This sorting process was analyzed using 3,3'-diaminobenzidine (DAB) cytochemistry, followed by Percoll density gradient cell fractionation. A conjugate of asialoorosomucoid (ASOR) and horseradish peroxidase (HRP) was used as a ligand for the asialoglycoprotein receptor. Cells were incubated at 0 degree C in the presence of both 131I-transferrin and 125I-ASOR/HRP. Endocytosis of prebound 125I-ASOR/HRP and 131I-transferrin was monitored by cell fractionation on Percoll density gradients. Incubation of the cell homogenate in the presence of DAB and H2O2 before cell fractionation gave rise to a density shift of 125I-ASOR/HRP-containing vesicles due to HRP-catalyzed DAB polymerization. An identical change in density for 125I-transferrin and 125I-ASOR/HRP, induced by DAB cytochemistry, is taken as evidence for the concomitant presence of both ligands in the same compartment. At 37 degrees C, sorting of the two ligands occurred with a half-time of approximately 2 min, and was nearly completed within 10 min. The 125I-ASOR/HRP-induced shift of 131I-transferrin was completely dependent on the receptor-mediated uptake of 125I-ASOR/HRP in the same compartment. In the presence of a weak base (0.3 mM primaquine), the recycling of transferrin receptors was blocked. The cell surface transferrin receptor population was decreased within 6 min to 15% of its original size. DAB cytochemistry showed that sorting between endocytosed 131I-transferrin and 125I-ASOR/HRP was also blocked in the presence of primaquine. These results indicate that transferrin and asialoglycoprotein are taken up via the same compartments and that segregation of the transferrin-receptor complex and asialoglycoprotein occurs very efficiently soon after uptake.

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4

Schwartz, A. L., A. Ciechanover, S. Merritt, and A. Turkewitz. "Antibody-induced receptor loss. Different fates for asialoglycoproteins and the asialoglycoprotein receptor in HepG2 cells." Journal of Biological Chemistry 261, no. 32 (November 1986): 15225–32. http://dx.doi.org/10.1016/s0021-9258(18)66857-7.

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5

Baricevic, Ivona, Ljiljana Vicovac-Panic, Vesna Marinovic, and Margita Cuperlovic. "Investigations of asialoglycoprotein receptor glycosylation by lectin affinity methods." Journal of the Serbian Chemical Society 67, no. 5 (2002): 331–38. http://dx.doi.org/10.2298/jsc0205331b.

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The asialoglycoprotein receptor belongs to the family of calcium-dependent (C-type) animal lectins. The purified receptor is a glycoprotein in which 10 % of the dry weight consists of sialic acid, galactose, N-acetylglucosamine and mannose. The carbohydrate content of the asialoglycoprotein receptor was investigated by lectin affinity methods. The usefulness of plant lectin affinity methods in the characterization of the saccharide content of the asialoglycoprotein receptor, as an animal lectin, is demonstrated. RCA I ConA, PHA, SNA I and WGA showed greater affinity toward the asialoglycoprotein receptor, while PSL, AAA and PNA showed negligible interactions with the asialoglycoprotein receptor. The obtained results correlated well with the carbohydrate content of the asialoglycoprotein receptor as determined by chemical methods.

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6

Evans, W. H., and N. Flint. "Subfractionation of hepatic endosomes in Nycodenz gradients and by free-flow electrophoresis. Separation of ligand-transporting and receptor-enriched membranes." Biochemical Journal 232, no. 1 (November 15, 1985): 25–32. http://dx.doi.org/10.1042/bj2320025.

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The complexity of rat liver endosome fractions containing internalized radioiodinated asialotransferrin, asialo-(alkaline phosphatase), insulin and prolactin was investigated by using free-flow electrophoresis and isopycnic centrifugation in Nycodenz gradients. Two subfractions were separated by free-flow electrophoresis. Both subfractions contained receptors for asialoglycoprotein and insulin. Glycosyltransferase activities were associated with the more electronegative vesicles, whereas 5′-nucleotidase and alkaline phosphodiesterase activities were associated with the less electronegative vesicles. Three subfractions were separated on Nycodenz gradients. Two subfractions, previously shown to become acidified in vitro, contained the ligands. At short intervals after uptake (1-2 min), ligands were mainly in subfraction DN-2 (density 1.115 g/cm3), but movement into subfraction DN-1 (density 1.090 g/cm3) had occurred 10-15 min after internalization. Low amounts of glycosyltransferase activities were associated with subfraction DN-2, and 5′-nucleotidase and alkaline phosphodiesterase activities were mainly located in subfraction DN-1. The binding sites for asialoglycoproteins and insulin were distributed towards the higher density range in the Nycodenz gradients, thus indicating a segregation of receptor-enriched vesicles and those vesicles containing the various ligands 10-15 min after internalization. Electron microscopy of the subfractions separated on Nycodenz gradients indicated that whereas the ligand-transporting fractions consisted mainly of empty vesicles (average diameter 100-150 nm), the receptor-enriched component was more granular and smaller (average diameter 70-95 nm). The properties of the endosome subfraction are used to assign their origin to the regions of the endocytic compartment where ligand-receptor dissociation and separation occur.

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7

De la Vega, Luis A., and Richard J. Stockert. "Regulation of the insulin and asialoglycoprotein receptors via cGMP-dependent protein kinase." American Journal of Physiology-Cell Physiology 279, no. 6 (December 1, 2000): C2037—C2042. http://dx.doi.org/10.1152/ajpcell.2000.279.6.c2037.

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Biotin regulation of asialoglycoprotein receptor expression and insulin receptor activity has been established in two human hepatoblastoma cell lines, Hep G2 and HuH-7. Second messenger cGMP mimics the effect of biotin on asialoglycoprotein receptor expression at the translational level. Metabolic labeling and subsequent immunoprecipitation indicate that the loss of insulin receptor activity during biotin deprivation was due to suppression of receptor synthesis. Evidence for posttranscriptional regulation of insulin receptor synthesis was provided by rapid biotin induction of receptor synthesis without an increase in gene transcript number. Addition of a cGMP-dependent protein kinase (cGK) inhibitor prevented biotin induction of the insulin and asialoglycoprotein receptors, suggesting that protein phosphorylation propagates the cGMP signal transduction cascade. Coatomer protein COPI was recently identified as the trans-acting factor that regulates in vitro translation of the asialoglycoprotein receptor. Biotin repletion of the culture medium resulted in the hyperphosphorylation of α-COP, which was prevented by simultaneous addition of the cGK inhibitor. These findings suggest that the end point of this cGMP signal cascade is modulated by cGK and that a phosphorylation reaction governs the expression of both receptor proteins.

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8

Lv, Jiaolong, Huanli Sun, Yan Zou, Fenghua Meng, Aylvin A. Dias, Marc Hendriks, Jan Feijen, and Zhiyuan Zhong. "Reductively degradable α-amino acid-based poly(ester amide)-graft-galactose copolymers: facile synthesis, self-assembly, and hepatoma-targeting doxorubicin delivery." Biomaterials Science 3, no. 7 (2015): 1134–46. http://dx.doi.org/10.1039/c4bm00436a.

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9

Lu, Lu, Bing Li, Chuanchuan Lin, Ke Li, Genhua Liu, Zengzilu Xia, Zhong Luo, and Kaiyong Cai. "Redox-responsive amphiphilic camptothecin prodrug nanoparticles for targeted liver tumor therapy." Journal of Materials Chemistry B 8, no. 17 (2020): 3918–28. http://dx.doi.org/10.1039/d0tb00285b.

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10

Witzigmann, Dominik, Pascal Detampel, Fabiola Porta, and Jörg Huwyler. "Isolation of multiantennary N-glycans from glycoproteins for hepatocyte specific targeting via the asialoglycoprotein receptor." RSC Advances 6, no. 100 (2016): 97636–40. http://dx.doi.org/10.1039/c6ra18297f.

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11

Massimi, M., L. Falasca, A. Felici, L. Dini, and L. Conti Devirgiliis. "Expression of the asialoglycoprotein receptor in cultured rat hepatocytes is modulated by cell density." Bioscience Reports 16, no. 6 (December 1, 1996): 477–84. http://dx.doi.org/10.1007/bf01198463.

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The influence of cell density on expression of the asialoglycoprotein receptor system in primary cultures of rat hepatocytes was evaluated by measuring the level of the receptor specific mRNA. When the hepatocytes are cultured at high cellular density and are not in a proliferative condition, the transcript molecules of the receptor appear increased about 50% with respect to the low plating density, indicating a modulation of asialoglycoprotein receptor expression at transcriptional level. Such control may be dependent on surface molecules involved in cell specific reassociation, since it is well known that cell contacts play a significant regulatory role in differentiated cells.

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12

Ivanova, E. A., A. V. Filatov, N. G. Morozova, M. A. Zenkova, and M. A. Maslov. "Novel bivalent spermine-based neutral neogalactolipids for modular gene delivery systems." RSC Advances 5, no. 113 (2015): 93262–66. http://dx.doi.org/10.1039/c5ra17389b.

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13

Chen, Guangxiang, Du Li, Jingchao Li, Xueyan Cao, Jianhua Wang, Xiangyang Shi, and Rui Guo. "Targeted doxorubicin delivery to hepatocarcinoma cells by lactobionic acid-modified laponite nanodisks." New Journal of Chemistry 39, no. 4 (2015): 2847–55. http://dx.doi.org/10.1039/c4nj01916d.

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Lactobionic acid-modified laponite can deliver doxorubicin specifically to hepatocarcinoma cells overexpressing the asialoglycoprotein receptor and display a significantly enhanced therapeutic efficacy.

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14

Bischoff, J., S. Libresco, M. A. Shia, and H. F. Lodish. "The H1 and H2 polypeptides associate to form the asialoglycoprotein receptor in human hepatoma cells." Journal of Cell Biology 106, no. 4 (April 1, 1988): 1067–74. http://dx.doi.org/10.1083/jcb.106.4.1067.

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Antibody-induced degradation and chemical cross-linking experiments have been carried out to assess the nature of the interaction between the two asialoglycoprotein-receptor polypeptides, H1 and H2, synthesized in HepG2 cells. Incubation of HepG2 cell monolayers with anti-H1 antibody caused a specific and equal loss of both H1 and H2 polypeptides. The same result was obtained with anti-H2 antibody. Control serum did not affect the level of H1 or H2 not did anti-H1 or anti-H2 antibodies affect the level of the transferrin receptor. The chemical cross-linking reagent, difluorodinitrobenzene, has been used to demonstrate that H1 can be cross-linked to H2 in HepG2 cell microsomal membranes. Dimer and trimer species with apparent molecular masses of 93 and 148 kD, respectively, were readily observed upon chemical cross-linking and some dimers and trimers were immunoreactive with both anti-H1 and anti-H2 antibodies. The putative trimer, possibly two H1 and one H2 molecules, is a minimum estimate of the true size of the asialoglycoprotein receptor in intact HepG2 cell, and it is possible that larger hetero-oligomeric forms of the receptor exist. The results of both types of experiments indicate that H1 and H2 form an oligomeric complex in HepG2 cells and thus, both polypeptides constitute the human asialoglycoprotein receptor.

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15

Diaz-Galvez, Kevin R., Nayelli G. Teran-Saavedra, Alexel J. Burgara-Estrella, Daniel Fernandez-Quiroz, Erika Silva-Campa, Monica Acosta-Elias, Hector M. Sarabia-Sainz, Martín R. Pedroza-Montero, and Jose A. Sarabia-Sainz. "Specific capture of glycosylated graphene oxide by an asialoglycoprotein receptor: a strategic approach for liver-targeting." RSC Advances 9, no. 18 (2019): 9899–906. http://dx.doi.org/10.1039/c8ra09732a.

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16

Fallon, R. J. "Tyrosine phosphorylation of the asialoglycoprotein receptor." Journal of Biological Chemistry 265, no. 6 (February 1990): 3401–6. http://dx.doi.org/10.1016/s0021-9258(19)39781-9.

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17

Andersson, Göran N., Pehr Rissler, and Lennart C. Eriksson. "Asialoglycoprotein receptors in rat liver nodules." Carcinogenesis 9, no. 9 (1988): 1623–28. http://dx.doi.org/10.1093/carcin/9.9.1623.

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18

Li, Yang, Chao Feng Yang, Hui Zuo, Ao Li, Sushant Kumar Das, and Jin Hong Yu. "Asialoglycoprotein Receptor-Targeted Superparamagnetic Perfluorooctylbromide Nanoparticles." Contrast Media & Molecular Imaging 2021 (May 29, 2021): 1–7. http://dx.doi.org/10.1155/2021/5510071.

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Background. The decrease in asialoglycoprotein receptor (ASGPR) levels is observed in patients with chronic liver disease and liver tumor. The aim of our study was to develop ASGPR-targeted superparamagnetic perfluorooctylbromide nanoparticles (M-PFONP) and wonder whether this composite agent could target buffalo rat liver (BRL) cells in vitro and could improve R2 ∗ value of the rat liver parenchyma after its injection in vivo. Methods. GalPLL, a ligand of ASGPR, was synthesized by reductive amination. ASGPR-targeted M-PFOBNP was prepared by a film hydration method coupled with sonication. Several analytical methods were used to investigate the characterization and safety of the contrast agent in vitro. The in vivo MR T2 ∗ mapping was performed to evaluate the enhancement effect in rat liver. Results. The optimum concentration of Fe3O4 nanoparticles inclusion in GalPLL/M-PFOBNP was about 52.79 µg/mL, and the mean size was 285.6 ± 4.6 nm. The specificity of GalPLL/M-PFOBNP for ASGPR was confirmed by incubation experiment with fluorescence microscopy. The methyl thiazolyl tetrazolium (MTT) test showed that there was no significant difference in the optical density (OD) of cells incubated with all GalPLL/M-PFOBNP concentrations. Compared with M-PFOBNP, the increase in R2 ∗ value of the rat liver parenchyma after GalPLL/M-PFOBNP injection was higher. Conclusions. GalPLL/M-PFOBNP may potentially serve as a liver-targeted contrast agent for MR receptor imaging.

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19

Sørensen, Anne Louise, Viktoria Rumjantseva, Sara Nayeb-Hashemi, Henrik Clausen, John H. Hartwig, Hans H. Wandall, and Karin M. Hoffmeister. "Role of sialic acid for platelet life span: exposure of β-galactose results in the rapid clearance of platelets from the circulation by asialoglycoprotein receptor–expressing liver macrophages and hepatocytes." Blood 114, no. 8 (August 20, 2009): 1645–54. http://dx.doi.org/10.1182/blood-2009-01-199414.

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AbstractAlthough surface sialic acid is considered a key determinant for the survival of circulating blood cells and glycoproteins, its role in platelet circulation lifetime is not fully clarified. We show that thrombocytopenia in mice deficient in the St3gal4 sialyltransferase gene (St3Gal-IV−/− mice) is caused by the recognition of terminal galactose residues exposed on the platelet surface in the absence of sialylation. This results in accelerated platelet clearance by asialoglycoprotein receptor-expressing scavenger cells, a mechanism that was recently shown to induce thrombocytopenia during Streptococcus pneumoniae sepsis. We now identify platelet GPIbα as a major counterreceptor on ST3Gal-IV−/− platelets for asialoglycoprotein receptors. Moreover, we report data that establish the importance of sialylation of the von Willebrand factor in its function.

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20

Marks, William H., Yan &NA;, Getachew Yirdaw, and Lisa Florence. "ASIALOGLYCOPROTEIN/ASIALOGLYCOPROTEIN RECEPTOR (AGP-AGPr) INTERACTION IS AN IMPORTANT MECHANISM FOR THE UPTAKE OF FK506 BY HEPATOCYTES1,2." Transplantation 63, no. 2 (January 1997): 293–98. http://dx.doi.org/10.1097/00007890-199701270-00020.

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21

Kaufman, S. S., P. L. Blain, J. H. Park, and D. J. Tuma. "Altered role of microtubules in asialoglycoprotein trafficking in developing liver." American Journal of Physiology-Gastrointestinal and Liver Physiology 258, no. 1 (January 1, 1990): G129—G137. http://dx.doi.org/10.1152/ajpgi.1990.258.1.g129.

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Efficient receptor-mediated endocytosis of asialoglycoprotein by mature liver requires participation of microtubules that convey newly internalized ligand to lysosomes for degradation and receptor back to plasma membrane to continue endocytosis. To ascertain whether microtubular participation in asialoglycoprotein endocytosis is altered during development, we compared endocytosis of 125I-labeled asialoorosomucoid (ASOR) in neonatal rat hepatocytes to that in adult cells, with and without microtubular disruption by colchicine. Control experiments demonstrated that 125I-ASOR degradation in neonatal hepatocytes occurred at 70% of the adult rate during continuous endocytosis, although neonatal surface receptors were only approximately 40% as numerous. Colchicine disruption of microtubules reduced 125I-ASOR degradation and steady-state intracellular ASOR more in adults during continuous endocytosis. Degradation of 125I-ASOR prebound to surface receptors was equally impaired by colchicine in the two groups. Continuous ASOR endocytosis by colchicine-treated adult hepatocytes progressively depleted their surface receptors but minimally in neonates. Unlike colchicine, the protonophore monensin markedly impaired receptor recycling as well as postinternalization ligand trafficking in both neonates and adults. Thus these experiments demonstrate that asialoglycoprotein processing proceeds as efficiently in neonatal as in adult hepatocytes despite a reduced surface receptor population. Microtubules are required to maintain receptors on cell surface as well as for postinternalization trafficking in adult cells. During development, only the latter process substantially requires microtubules, indicating that microtubular participation in protein trafficking is selectively, not uniformly, diminished at this time in life.

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22

Berg, Trond, Grete M. Kindberg, Terry Ford, and Rune Blomhoff. "Intracellular transport of asialoglycoproteins in rat hepatocytes." Experimental Cell Research 161, no. 2 (December 1985): 285–96. http://dx.doi.org/10.1016/0014-4827(85)90086-2.

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23

Cooper, Allen D., and David Coleman. "Chylomicron remnant and asialoglycoprotein metabolism are independent." Lipids 20, no. 10 (October 1985): 664–67. http://dx.doi.org/10.1007/bf02534384.

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24

Stockert, R. J., and A. G. Morell. "Second messenger modulation of the asialoglycoprotein receptor." Journal of Biological Chemistry 265, no. 4 (February 1990): 1841–46. http://dx.doi.org/10.1016/s0021-9258(19)39905-3.

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25

Balaji, P. V., P. K. Qasba, and V. S. R. Rao. "Molecular dynamics simulations of asialoglycoprotein receptor ligands." Biochemistry 32, no. 47 (November 1993): 12599–611. http://dx.doi.org/10.1021/bi00210a008.

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26

Guy, Clifford S., Sherri L. Rankin, and Tomasz I. Michalak. "Hepatocyte cytotoxicity is facilitated by asialoglycoprotein receptor." Hepatology 54, no. 3 (July 21, 2011): 1043–50. http://dx.doi.org/10.1002/hep.24477.

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27

Mamidyala, Sreeman K., Sanjay Dutta, Boris A. Chrunyk, Cathy Préville, Hong Wang, Jane M. Withka, Alexander McColl, et al. "Glycomimetic Ligands for the Human Asialoglycoprotein Receptor." Journal of the American Chemical Society 134, no. 4 (January 24, 2012): 1978–81. http://dx.doi.org/10.1021/ja2104679.

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28

Grozovsky, Renata, Gerard Jansen, and Karin M. Hoffmeister. "The Hepatic Asialoglycoprotein Receptor Regulates Platelet Homeostasis." Blood 116, no. 21 (November 19, 2010): 2025. http://dx.doi.org/10.1182/blood.v116.21.2025.2025.

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Abstract Abstract 2025 The human body produces and removes more than a 100 billion of platelets every day. The mechanisms responsible for platelet homeostasis are subject to speculation since the 1950's. The most popular hypothesis to date has been antibody-mediated clearance, platelet consumption due to massive blood loss and an internal “senescence timer”. We and others have recently demonstrated that sialic acid deficient platelets due to external triggers such as sepsis or chilling are cleared by hepatic asialoglycoprotein receptors (ASGPR) independently of macrophages. Here, we investigated whether loss of sialic acid mediates platelet clearance in vivo. We show that 1) Injection of the specific sialidase inhibitor 2-deoxy-2,3-dehydro-N-acetylneuraminic acid (DANA) lengthened the survival of biotinylated platelets by ∼50% (T1/2 of 72h), compared to mock treated (PBS injected) control mice (T1/2 of 49h); 2) Similarly, biotinylated platelet survival in ASGPR-null mice was prolonged by ∼ 50% (T1/2 of 74h) compared to platelet survival in wild type (WT) mice (T1/2 of 48h); 3) ASGPR-null mice have significantly increased platelet counts, compared to WT (p=0.0004) and platelets isolated from ASGPR-null mice are ∼15% smaller than WT (p=0.03); 4) Platelets isolated from ASGPR-null mice showed significant increased in b-galactose exposure (∼50% increase, i.e. decrease of sialic acid), compared to WT, as evidenced by binding of the b-galactose specific lectin (RCA-I). These data show that the ASGPR not only removes desialylated platelets due to sepsis or chilling, but also regulates platelet homeostasis. Disclosures: No relevant conflicts of interest to declare.

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29

Zeng, Fu-Yue, Bhupendra S. Kaphalia, G. A. S. Ansari, and Paul H. Weigel. "Fatty Acylation of the Rat Asialoglycoprotein Receptor." Journal of Biological Chemistry 270, no. 36 (September 8, 1995): 21382–87. http://dx.doi.org/10.1074/jbc.270.36.21382.

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30

Takahashi, Tohru, Hiroshi Nakada, Tadayoshi Okumura, Takaya Sawamura, and Yutaka Tashiro. "Phosphorylation of the rat hepatocyte asialoglycoprotein receptor." Biochemical and Biophysical Research Communications 126, no. 3 (February 1985): 1054–60. http://dx.doi.org/10.1016/0006-291x(85)90292-x.

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31

Huang, Guifang, James Diakur, Zhenghe Xu, and Leonard I. Wiebe. "Asialoglycoprotein receptor-targeted superparamagnetic iron oxide nanoparticles." International Journal of Pharmaceutics 360, no. 1-2 (August 2008): 197–203. http://dx.doi.org/10.1016/j.ijpharm.2008.04.029.

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32

Clemens, Dahn L., Dean J. Tuma, and Carol A. Casey. "Cyanamide Potentiates the Ethanol-Induced Impairment of Receptor-Mediated Endocytosis in a Recombinant Hepatic Cell Line Expressing Alcohol Dehydrogenase Activity." International Journal of Hepatology 2012 (2012): 1–5. http://dx.doi.org/10.1155/2012/954157.

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Ethanol administration has been shown to alter receptor-mediated endocytosis in the liver. We have developed a recombinant hepatic cell line stably transfected with murine alcohol dehydrogenase cDNA to serve as anin vitromodel to investigate these ethanol-induced impairments. In the present study, transfected cells were maintained in the absence or presence of 25 mM ethanol for 7 days, and alterations in endocytosis by the asialoglycoprotein receptor were determined. The role of acetaldehyde in this dysfunction was also examined by inclusion of the aldehyde dehydrogenase inhibitor, cyanamide. Our results showed that ethanol metabolism impaired internalization of asialoorosomucoid, a ligand for the asialoglycoprotein receptor. The addition of cyanamide potentiated the ethanol-induced defect in internalization and also impaired degradation of the ligand in the presence of ethanol. These results indicate that the ethanol-induced impairment in endocytosis is exacerbated by the inhibition of aldehyde dehydrogenase, suggesting the involvement of acetaldehyde in this dysfunction.

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33

BIESSEN, Erik A. L., Helene VIETSCH, Erik T. RUMP, Kees FLUITER, Johan KUIPER, Martin K. BIJSTERBOSCH, and Theo J. C. VAN BERKEL. "Targeted delivery of oligodeoxynucleotides to parenchymal liver cells in vivo." Biochemical Journal 340, no. 3 (June 8, 1999): 783–92. http://dx.doi.org/10.1042/bj3400783.

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Anti-sense oligodeoxynucleotides (ODNs) hold great promise for correcting the biosynthesis of clinically relevant proteins. The potential of ODNs for modulating liver-specific genes might be increased by preventing untimely elimination and by improving the local bioavailability of ODNs in the target tissue. In the present study we have assessed whether the local ODN concentration can be enhanced by the targeted delivery of ODNs through conjugation to a ligand for the parenchymal liver cell-specific asialoglycoprotein receptor. A capped ODN (miscellaneous 20-mer sequence) was derivatized with a ligand with high affinity for this receptor, N2-[N2-(N2,N6-bis{N-[p-(β-D-galactopyranosyloxy) anilino] thiocarbamyl} - L - lysyl) - N6 - (N - {p - [β-D -galactopyranosyloxy] anilino} thiocarbamyl) - L - lysyl] - N6 - [N - (p -{β-ᴅ-galactopyranosyloxy}anilino)thiocarbamyl]-ʟ-lysine (L3G4) (Kd 6.5±0.2 nM, mean±S.D.). Both the uptake studies in vitro and the confocal laser scan microscopy studies demonstrated that L3G4-ODN was far more efficiently bound to and taken up by parenchymal liver cells than underivatized ODN. Studies in vivo in rats showed that hepatic uptake could be greatly enhanced from 19±1% to 77±6% of the injected dose after glycoconjugation. Importantly, specific ODN accumulation of ODN into parenchymal liver cells was improved almost 60-fold after derivatization with L3G4, and could be attributed to the asialoglycoprotein receptor. In conclusion, the scavenger receptor-mediated elimination pathway for miscellaneous ODN sequences can be circumvented by direct conjugation to a synthetic tag for the asialoglycoprotein receptor. In this manner a crucial requisite is met towards the application of ODNs in vivo to modulate the biosynthesis of parenchymal liver cell-specific genes such as those for apolipoprotein (a), cholesterol ester transfer protein and viral proteins.

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34

Stockert, R. J., E. Paietta, J. Racevskis, and A. G. Morell. "Posttranscriptional regulation of the asialoglycoprotein receptor by cGMP." Journal of Biological Chemistry 267, no. 1 (January 1992): 56–59. http://dx.doi.org/10.1016/s0021-9258(18)48457-8.

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35

Takezawa, Ryuichi, Kouei Shinzawa, Yoshifumi Watanabe, and Toshihiro Akaike. "Determination of mouse major asialoglycoprotein receptor cDNA sequence." Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1172, no. 1-2 (February 1993): 220–22. http://dx.doi.org/10.1016/0167-4781(93)90300-3.

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36

Kakegawa, Tetsuji, Hirohiko Ise, Nobuhiro Sugihara, Toshio Nikaido, Naoki Negishi, Toshihiro Akaike, and Eiji Tanaka. "Soluble Asialoglycoprotein Receptors Reflect the Apoptosis of Hepatocytes." Cell Transplantation 11, no. 5 (July 2002): 407–15. http://dx.doi.org/10.3727/000000002783985756.

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Cell death is thought to take place through at least two distinct processes: apoptosis and necrosis. There is increasing evidence that dysregulation of the apoptotic program is involved in liver diseases. However, there is no method to simply evaluate apoptosis in the liver tissue at present. It has been reported that the expression of asialoglycoprotein receptors (AGPRs) increases with apoptosis, but there is no report until now that investigates the influence of soluble AGPRs on apoptosis of hepatocytes. Soluble AGPRs have been reported to be present in human serum under physiological conditions. In the present study, in order to investigate the correlation between apoptosis of hepatocytes and soluble AGPR, mouse soluble AGPRs were detected using SDS-PAGE and Western blot analysis was conducted using anti-extracellular mouse hepatic lectin-1 (Ex-MHL-1) antiserum (polyclonal rabbit serum). The mouse soluble AGPRs were present in culture medium and mouse serum when hepatocytes were damaged. The soluble AGPRs increased proportionately, as the number of dead hepatocytes increased. In addition, soluble AGPRs existed more when apoptotic cell death was observed in in vitro and in vivo than when necrotic cell death was observed. The extracellular moiety of MHL-1 exists in the culture medium and mouse serum as a soluble AGPR, but the detailed mechanism of releasing soluble AGPR from hepatocytes has not been revealed yet. We described the first evidence for the relation between quantity of soluble AGPRs with two kinds of cell death: necrosis and apoptosis. Based on the results of our study, soluble AGPRs might become a new marker of apoptosis in the liver tissue and be useful for clinical diagnosis and treatment for liver diseases.

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37

Seleznev, Egor I., Emil Yu Yamansarov, Elena V. Lopatukhina, Anton V. Lopuhov, Dmitry A. Skvortsov, Sergei A. Evteev, Elvira T. Yamansarova, et al. "Synthesis of allobetulin-based asialoglycoprotein receptor-targeted glycoconjugates." Mendeleev Communications 29, no. 5 (September 2019): 526–28. http://dx.doi.org/10.1016/j.mencom.2019.09.016.

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38

Stockert, R. J. "Regulation of the human asialoglycoprotein receptor by cAMP." Journal of Biological Chemistry 268, no. 26 (September 1993): 19540–44. http://dx.doi.org/10.1016/s0021-9258(19)36549-4.

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39

Clemens, Dahn L., Christine M. Halgard, Jack R. Cole, Rodney M. Miles, Michael F. Sorrell, and Dean J. Tuma. "Impairment of the asialoglycoprotein receptor by ethanol oxidation." Biochemical Pharmacology 52, no. 10 (November 1996): 1499–505. http://dx.doi.org/10.1016/s0006-2952(96)00524-2.

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40

NAKADA, Hiroshi, Takaya SAWAMURA, Tadayoshi OKUMURA, and Yutaka TASHIRO. "Three Molecular Forms of a Rat Asialoglycoprotein Receptor1." Journal of Biochemistry 99, no. 3 (1986): 867–76. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a135547.

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41

Tolchinsky, Sandra, Ming Huam Yuk, Michal Ayalon, Harvey F. Lodish, and Gerardo Z. Lederkremer. "Membrane-boundVersusSecreted Forms of Human Asialoglycoprotein Receptor Subunits." Journal of Biological Chemistry 271, no. 24 (June 14, 1996): 14496–503. http://dx.doi.org/10.1074/jbc.271.24.14496.

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42

Bischoff, J., and H. F. Lodish. "Two asialoglycoprotein receptor polypeptides in human hepatoma cells." Journal of Biological Chemistry 262, no. 24 (August 1987): 11825–32. http://dx.doi.org/10.1016/s0021-9258(18)60888-9.

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43

Hyodo, Ichinosuke, Motowo Mizuno, Gotaro Yamada, and Takao Tsuji. "Distribution of asialoglycoprotein receptor in human hepatocellular carcinoma." Liver 13, no. 2 (December 10, 2008): 80–85. http://dx.doi.org/10.1111/j.1600-0676.1993.tb00611.x.

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44

KOHGO, YUTAKA, JUNJI KATO, REIJI NAKAYA, YOSHIRO MOGI, HIROKAZU YAGO, YASUO SAKAI, HIROTOSHI MATSUSHITA, and YOSHIRO NIITSU. "Production and Characterization of Specific Asialoglycoprotein Receptor Antibodies." Hybridoma 12, no. 5 (October 1993): 591–98. http://dx.doi.org/10.1089/hyb.1993.12.591.

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45

YOSHIDA, SEIYA, MADOKA FURUHASHI, and NOBUHIKO SUGANUMA. "Expression of Asialoglycoprotein Receptor in Human Fetal Liver." Endocrine Journal 46, no. 1 (1999): 67–73. http://dx.doi.org/10.1507/endocrj.46.67.

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46

Bon, Charlotte, Thomas Hofer, Alain Bousquet-Mélou, Mark R. Davies, and Ben-Fillippo Krippendorff. "Capacity limits of asialoglycoprotein receptor-mediated liver targeting." mAbs 9, no. 8 (September 21, 2017): 1360–69. http://dx.doi.org/10.1080/19420862.2017.1373924.

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47

Mi, Yiling, Marcy Coonce, Dorothy Fiete, Lindsay Steirer, Gabriela Dveksler, R. Reid Townsend, and Jacques U. Baenziger. "Functional Consequences of Mannose and Asialoglycoprotein Receptor Ablation." Journal of Biological Chemistry 291, no. 36 (July 12, 2016): 18700–18717. http://dx.doi.org/10.1074/jbc.m116.738948.

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48

D'Souza, Anisha A., and Padma V. Devarajan. "Asialoglycoprotein receptor mediated hepatocyte targeting — Strategies and applications." Journal of Controlled Release 203 (April 2015): 126–39. http://dx.doi.org/10.1016/j.jconrel.2015.02.022.

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49

Sun, Pingnan, Junhong Zheng, Guizhou She, Xiujing Wei, Xiaoyu Zhang, Haijun Shi, and Xiaoling Zhou. "Expression pattern of asialoglycoprotein receptor in human testis." Cell and Tissue Research 352, no. 3 (April 21, 2013): 761–68. http://dx.doi.org/10.1007/s00441-013-1616-8.

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50

ENRICH, C., M. VERGES, and W. EVANS. "Asialoglycoprotein receptor modulation in rat liver endocytic compartment." Cell Biology International Reports 14 (September 1990): 213. http://dx.doi.org/10.1016/0309-1651(90)90951-t.

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