Relevant bibliographies by topics / Asialoglycoproteine

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Academic literature on the topic 'Asialoglycoproteine'

Author: Grafiati
Published: 4 June 2021
Last updated: 6 February 2022

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Journal articles on the topic "Asialoglycoproteine"

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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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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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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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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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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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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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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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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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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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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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Dissertations / Theses on the topic "Asialoglycoproteine"

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Dahmane, Bourkhis Amel. "Etude de l'endocytose du recepteur de l'epidermal growth factor dans l'hepatocyte isole de rat ; regulations in vivo (diabete insulino-dependant et vanadate) et in vitro (vanadate et seconds messagers) : comparaison avec le recepteur des asialoglycoproteines." Paris 11, 1996. http://www.theses.fr/1996PA114813.

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Lamaze, Christophe. "Fonctionnement du récepteur humain des asialoglycoprotéines : étude comparée sur hépatocytes cirrhotiques et non cirrhotiques, effet de la vasopressine, du PMA et de la staurosporine." Paris 5, 1991. http://www.theses.fr/1991PA05P208.

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Bon, Charlotte. "Ciblage des médicaments dans le foie : combinaison d'études pharmacocinétiques et de la modélisation pour optimiser les concentrations des médicaments dans les hépatocytes via le récepteur asialoglycoproteine." Thesis, Toulouse 3, 2019. http://www.theses.fr/2019TOU30080.

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Le récepteur asialoglycoproteine (ASGPR) a attiré particulièrement l'attention pour concentrer les médicaments dans le foie, notamment parce que ce récepteur membranaire est exprimé presque exclusivement et avec une abondance élevée à la surface des hépatocytes. Dans cette thèse, un anticorps anti-ASGPR (Ac ASGPR) nouvellement développé ainsi que l'utilisation des techniques de modélisation mathématique sont utilisés pour déduire la cinétique d'absorption du récepteur in-vivo chez la souris, information cruciale pour optimiser le ciblage hépatique des médicaments. Une fois déduites ces informations quantitatives peuvent ensuite être utilisées pour informer et affiner le protocole d'administration de n'importe quelle entité ciblant l'ASGPR. Avec un protocole optimisé, la saturation du récepteur peut être évitée et ainsi obtenir un ciblage maximal des hépatocytes en minimisant la probabilité de survenue d'effets secondaires. Nous avons d'abord effectué une étude pharmacocinétique (PK) en utilisant l'Ac ASGPR pour estimer les paramètres cinétiques d'absorption via l'ASGPR en se focalisant sur son expression, sa vitesse de renouvellement et d'internalisation. L'expression du récepteur a été estimé autour d'un 1.8 million de molécules par cellule, ce qui confirme la forte abondance de récepteurs à la surface des hépatocytes. La demi-vie de dégradation du récepteur a été estimée à environ 15 heures and le complexe ligand-récepteur est internalisé avec une demi-vie de 5 jours. Cette lente internalisation est un avantage pour le ciblage des médicaments puisque cela permet de lier le médicament libre dans la circulation plasmatique et ensuite de l'absorber lentement dans les hépatocytes et cela même si sa clairance (non liée à l'ASGPR) est élevée dans le plasma. La cinétique de l'ASGPR montre que la saturation de l'endocytose est possible à des concentrations thérapeutiques, cependant la modélisation mathématique et l'utilisation de simulations permettent d'optimiser le protocole d'administration. Pour confirmer l'absorption spécifique dans le foie de l'Ac ASGPR mais aussi la description quantitative de son absorption, une étude de biodistribution a été entreprise. L'Ac ASGPR a été radio-marqué pour pouvoir mesurer les concentrations d'anticorps dans le foie et quantifier sa distribution dans les autres tissues. Une large distribution de l'Ac ASGPR a été détectée dans le foie et faiblement dans les autres tissues, confirmant la liaison importante et rapide de l'anticorps au foie. Dans le but de différencier l'absorption spécifique de l'anticorps, i.e. liée à l'ASGPR, de celle de la clairance générale des anticorps par le foie, un anticorps non-spécifique (l'Ac IL17) a été utilisé comme contrôle. En comparaison avec l'Ac ASGPR, l'Ac IL17 est beaucoup moins absorbé par le foie. Les données de l'étude de biodistribution ont permis de conclure que la liaison de l'anticorps à son récepteur a lieu uniquement dans le foie confirmant la description quantitative de l'absorption par l'ASGPR. Le modèle mathématique peut être utilisé à plusieurs fins. D'abord, le modèle peut être appliqué à d'autre molécules que l'Ac ASGPR à condition de changer les paramètres PK qui ne sont pas liés à l'ASGPR, comme par exemple le volume de distribution. Le but final est d'extrapoler le modèle PK construit à partir de données chez la souris à l'homme pour prédire un protocole d'administration chez les patients. Chez l'homme, certains paramètres sont déjà connus comme l'expression du récepteur mais d'autres processus de l'endocytose médiée par l'ASGPR doivent encore être investigués comme par exemple la vitesse de synthèse et de dégradation du récepteur. Une fois le modèle défini chez l'homme, le modèle sera applicable et utile pour estimer l'expression du récepteur chez les patients et investiguer l'impact de la plus faible expression du récepteur chez ces patients sur le protocole d'administration
The asialoglycoprotein receptor (ASGPR) has drawn particular attention to enhance drug delivery to hepatocytes, notably because this membrane endocytic receptor is expressed almost exclusively and with high abundance on hepatocytes making this receptor a target of choice for hepatic delivery. In this thesis we take advantage of a newly developed anti-ASGPR antibody (ASGPR Ab) and mathematical modeling to infer the uptake properties of the receptor in vivo in mice, crucial information to optimize drug delivery to hepatocyte. This quantitative knowledge can then be leveraged to inform the protocol of administration of any molecular entity targeting the ASGPR. With an optimal dosing regimen, receptor saturation can be avoided to obtain a maximal delivery into hepatocytes while minimizing the likelihood for systemic adverse effects. To estimate the ASGPR mediated uptake parameters, focusing on its expression, turnover and internalization rates, we performed a mouse pharmacokinetic (PK) study with the ASGPR Ab. The ASGPR expression level was found to be about 1.8 million molecules per hepatocyte, which confirms the high abundance of receptors expressed at the hepatocytes cell surface. The half-life of the degradation of the receptor was estimated to be about 15 hours and the formed ligand-receptor complex is internalized with a half-life of about 5 days. This slow internalization is an advantage for drug targeting as it allows to capture the free drug from the plasma by binding and then delivers the drug slowly into the hepatocytes even if the targeting drug as a fast non-ASGPR related PK in the plasma. The kinetics of the ASGPR shows that saturation of the shuttle at therapeutic concentrations is possible; however, modeling and simulation allows the dosing protocol to be optimized. Then, to confirm both the specific liver uptake of the ASGPR Ab and the quantitative description of the ASGPR mediated uptake we performed a biodistribution study. To measure the uptake of the ASGPR Ab in the liver and the distribution in other tissues, the antibody was radiolabeled and tissue radioactivity was quantified. A large distribution of the ASGPR Ab was detected in liver and minor distribution was noted in other tissues, confirming the rapid and extensive binding of the ASGPR Ab in the liver. In order to differentiate the specific uptake of the ASGPR Ab from the general liver clearance of antibodies, a radiolabeled non-targeting antibody (IL17 Ab) was used as a control. In comparison to the ASGPR Ab, the IL17 Ab distributes much less in liver confirming the specific distribution of the ASGPR Ab into the liver. From the biodistribution data it was possible to conclude that all the target mediated uptake of the ASGPR Ab happens solely in the liver and therefore confirm the quantitative description of the ASGPR mediated uptake. We suggest the following use of the ASGPR-mediated disposition model. First, it is applicable to any ASGPR targeting drugs by changing the PK properties which are non-ASGPR related, e.g. volume of distribution, non-ASGPR related clearance... etc. Second, the ASGPR mediated drug disposition model supports the selection of an optimal dosing regimen by maximizing liver uptake while minimizing non targeted organs distribution. Extrapolation of the mouse model to human is the final goal in order to predict optimal dosing regimen of ASGPR targeting drugs in patients. In human, some parameters are already known such as the receptor expression but other processes of the receptor mediated endocytosis must however be investigated such as the synthesis and degradation rate. Once defined in human, the model will be applicable and used for two purposes 1) estimate the receptor number in patients as suggested in the manuscript of the second paper 2) investigate the impact of decreased receptor number in the patients on the dosing regimen
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Lundy, Fionuala T. "Asialoglycoproteins of human serum." Thesis, Queen's University Belfast, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.317478.

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Beckett-Bowen, Gloria. "Autoepitope mapping of the Asialoglycoprotein receptor." Thesis, King's College London (University of London), 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.267999.

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Quintero-Martinez, Adrian. "Assembly and selectivity of asialoglycoprotein receptors." Thesis, Imperial College London, 2012. http://hdl.handle.net/10044/1/9232.

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Two galactose-binding receptors, the hepatic asialoglycoprotein receptor (ASGPR) and the macrophage galactose lectin (MGL) have been investigated. The ASGPR is believed to function in glycoprotein clearance from serum while MGL is involved in recognition of pathogens and tumours and in signalling and immunomodulation. This work describes the analysis of the specificity, structure and organisation of both receptors in humans and the two MGLs in mice. The ligand-binding properties of the two subunits of the ASGPR as well as MGL have been separately tested in glycan array analysis. The results show that primary binding to ligands in the human ASGPR occurs via the ASGPR-1 subunit. MGLs have different specificities even though they are highly similar in sequence and the two mouse MGLs differ markedly from the single MGL in humans and in rats. One of the mouse MGLs has a similar specificity to ASGPR-1 that evolved independently. Hydrodynamic studies of ASGPR-1 revealed that it can form homo-oligomers and circular dichroism analysis of the neck fragment showed that it has a coiled-coil structure. Hetero-oligomer formation was monitored using a mutant version of ASGPR1 that allows purification of the complex using double-affinity chromatography on galactose and mannose. Hetero-oligomers containing both types of subunits are more stable than homo-oligomers. The results suggest a model that can account for the variable subunit stoichiometries observed by various investigators. Hydrodynamic studies and circular dichroism of MGL suggest that the extracellular domain of the human protein is an oligomer not as stable as previously thought, and that its neck is a coiled-coil structure. For both receptors, transmembrane and cytoplasmic domains as well as glycosylation may have a role in their stability. The ability of MGL to recognise pathogen glycans was demonstrated using Trichinella spiralis secretions. It was found that similar glycoproteins are bound by the human and mouse receptors.
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Ambury, Rachael. "Bioactive sugar surfaces for hepatocyte cell culture." Thesis, University of Manchester, 2010. https://www.research.manchester.ac.uk/portal/en/theses/bioactive-sugar-surfaces-for-hepatocyte-cell-culture(122af33a-35b1-47c1-9579-4568fef47543).html.

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The primary objective of this study was to identify, develop and characterise a novel bioactive surface capable of binding hepatocytes and enabling the retention of hepatocyte-specific cell function during in-vitro culture. The materials were designed to exploit a unique characteristic of hepatocyte biology, with β-galactose moieties displayed to allow cellular adhesion via the specific asialoglycoprotein receptors (ASGP-R) found on hepatocytes. Hydrogels were created by modifying a commercially available block co-polymer of polyethylene glycol (PEG) and acrylamide, (PEGA) with galactose moieties contained within lactobionic acid (LA), producing a unique bioactive sugar-based gel. A control sugar, D-glucuronic acid (GA), was used as a non-ASGP-R binding control. Monomers used were mono- and bis-acryloamido PEG (Mw=1900 gmol-1), and dimethylacrylamide. The pendant PEGA amine groups were used as ligands to bind to the sugars. The resultant gels were characterised using Fourier Transform Infrared Spectroscopy (FT-IR), protein adsorption, Fmoc-Phe and dansyl chloride labelling. The biocompatibility of the gel surfaces was evaluated using a hepatocyte cell line and the degree of attachment, proliferation, and morphology was characterised using light microscopy, live/dead assays, DNA assays, immunochemical staining, flow cytometry and reverse-transcription polymerase chain reaction (RT-PCR).FT-IR analysis of LA revealed a distinctive band at approximately 1740cm-1 corresponding to carbonyl stretching (C=O) of carboxylic acid. This unique peak disappeared as the galactose moieties within the LA were incorporated into the PEGA gel. A similar trend was also observed with the control GA sugar within the PEGA gel, confirming that the sugars had been integrated into the material. Protein adsorption assays confirmed the non-fouling nature of PEGA. Cell culture experiments showed that hepatocytes attached preferentially to the sugar surfaces, with few cells seen on the PEGA surfaces. It was observed that cells on the PEGA with LA surface were more metabolically active, than the controls and proliferated to a monolayer by day 7 in culture. Immunocytochemical staining of the cells for actin, vinculin and phosphorylated focal adhesion kinase illustrated differences in cell morphology between cells grown on different surfaces. It was determined that the sugar PEGA surfaces maintained some characteristics of hepatocyte functionality e.g. urea synthesis over the course of 7 days. To improve the reproducibility of the surfaces generated, a preliminary investigation of two-dimensional PEG monolayer surfaces as a well defined platform for surface reactions was conducted. These were chemically functionalised in a stepwise manner with the sugars. The number of coupling steps and the choice of solvent were shown to affect the efficiency of the reaction. Further more, the need for careful sample preparation was highlighted as contamination could potentially inhibit the interpretation of the surface chemistry.The overall conclusion of this work is that saccharides within non-fouling surfaces composed of thin layers of PEG-acrylamide hydrogels are able to support hepatocyte attachment and the retention of cell type specific functions in culture. However, this preliminary work has shown that much further research is necessary to elucidate the role that the surface chemistry plays in the attachment of hepatocytes.
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Yuk, Ming Huam. "Degradation and folding of the asialoglycoprotein receptor in the endoplasmic reticulum." Thesis, Massachusetts Institute of Technology, 1995. http://hdl.handle.net/1721.1/32669.

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Dodeur, Michèle. "Etude du récepteur hépatique des asialoglycoprotéines chez le Rat rendu diabétique." Grenoble 2 : ANRT, 1986. http://catalogue.bnf.fr/ark:/12148/cb37597232x.

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McLendon, Patrick Michael. "Cationic Glycopolymers for DNA Delivery: Cellular Internalization Mechanisms and Biological Characterization." Diss., Virginia Tech, 2009. http://hdl.handle.net/10919/29436.

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Understanding the biological mechanisms of polymeric DNA delivery is essential to develop vehicles that perform optimally. In this work, the cellular internalization mechanisms of poly(glycoamidoamine) (PGAA) DNA delivery polymers were investigated. Polymer:DNA complexes interact with cell-surface glycosaminoglycans (GAGs) in a manner independent of electrostatic interactions. Desulfation and GAG removal leads to decreased uptake. Individual polyplexes appear to have differing affinities for specific GAGs, as polyplex dissociation occurs in a charge-independent manner, and may influence binding. Internalization occurs through close interactions with GAGs, as GAGs accumulate on polyplex surfaces, resulting in negatively-charged polyplexes and decompaction of intact polyplexes is observed upon interaction with GAG. PGAA polyplexes enter cells via a complex, multifaceted internalization route. Pharmacological inhibition of endocytosis and visualization by confocal microscopy reveal that internalization occurs primarily through an actin and dynamin-dependent mechanism. Caveolae/raft-mediated endocytosis appears to be the predominant internalization mechanism, with clathrin-mediated endocytosis also significantly involved. Internalization occurs to a smaller degree via macropinocytosis and direct membrane penetration. Caveolae-mediated, but not clathrin-mediated, internalization leads to transgene expression, suggesting a targeting opportunity based on uptake mechanisms. PEGylation of PGAA polyplexes was achieved to minimize polyplex aggregation in serum. Polyplex size increased in serum, but PEGylation prevented further polyplex growth over time compared to non-PEGylated polymers. Specific targeting of hepatocytes through end-modification of PEG with galactose was unsuccessful, likely due to inaccessibility of targeting groups. Further hepatocyte targeting efforts focused on malonate-based polymers with clickable linkages for facile linkage of targeting groups. Despite favorable surface presentation of galactose, receptor-specific internalization of polyplexes was unsuccessful, as competitive inhibition in HepG2 cells resulted in significant polyplex internalization derived from nonspecific membrane interactions. Chemical modification of vehicles allows systematic study of structure-function properties leading to efficient intracellular delivery. Increasing G4 molecular weight generally increases toxicity and decreases transgene expression in HeLa cells. Incorporating galactose into a lanthanide-chelating polymer facilitated efficient cellular internalization that was visualized by two-photon microscopy. Increased gene expression was observed that correlated to increasing galactose, suggesting that polymer degradation increases gene expression. Also studied were branched peptides targeted to HIV-1 TAR, which displayed high biocompatibility and favorable internalization profiles in mammalian cells.
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Books on the topic "Asialoglycoproteine"

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Yik, Jasper Hoi Nei. Palmitoylation of the asialoglycoprotein receptor. [s.n.], 2002.

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Schiff, Jack Michael *. Levels of specificity in the endocystosis and transport of IgA and asialoglycoprotein. 1986.

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Book chapters on the topic "Asialoglycoproteine"

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Stockert, Richard J., Janna C. Collins, and Anatol G. Morell. "The Asialoglycoprotein Receptor." In Receptor Purification, 383–92. Totowa, NJ: Humana Press, 1990. http://dx.doi.org/10.1007/978-1-4612-0477-0_21.

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Das, Saugandha, Pawan Kudale, Prajakta Dandekar, and Padma V. Devarajan. "Asialoglycoprotein Receptor and Targeting Strategies." In Targeted Intracellular Drug Delivery by Receptor Mediated Endocytosis, 353–81. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-29168-6_12.

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Weigel, Paul H. "Endocytosis and Function of the Hepatic Asialoglycoprotein Receptor." In Subcellular Biochemistry, 125–61. Boston, MA: Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-3026-8_5.

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Gupta, Anita. "Asialoglycoprotein Receptor and the Macrophage Galactose-Type Lectin." In Animal Lectins: Form, Function and Clinical Applications, 709–24. Vienna: Springer Vienna, 2012. http://dx.doi.org/10.1007/978-3-7091-1065-2_33.

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Steer, J. Clifford, Peretz Weiss, Peter J. Wirth, and Gilbert Ashwell. "The Hepatic Receptor for Asialoglycoproteins: Search for a Function." In Targeting of Drugs, 29–43. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4684-5574-8_3.

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Furs, Stephen, and George Y. Wu. "Receptor-Mediated Targeted Gene Delivery Using Asialoglycoprotein-Polylysine Conjugates." In Gene Therapeutics, 382–90. Boston, MA: Birkhäuser Boston, 1994. http://dx.doi.org/10.1007/978-1-4684-6822-9_21.

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Harford, Joe, and Gilbert Ashwell. "Chemical and Physical Properties of the Hepatic Receptor for Asialoglycoproteins." In Endocytosis, 69–83. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4615-6904-6_3.

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Berg, T., G. Kindberg, T. Ford, and R. Blomhoff. "Intracellular Degradation of Asialoglycoproteins in Rat Hepatocytes Studied by Fractionation in Nycodenz Gradients." In Receptor-Mediated Uptake in the Liver, 174–82. Berlin, Heidelberg: Springer Berlin Heidelberg, 1986. http://dx.doi.org/10.1007/978-3-642-70956-2_30.

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Rice, Kevin G., and Yuan C. Lee. "Oligosaccharide Valency and Conformation in Determining Binding to the Asialoglycoprotein Receptor of Rat Hepatocytes." In Advances in Enzymology - and Related Areas of Molecular Biology, 41–83. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470123126.ch2.

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Doyle, Darrell, James Petell, and James Sawyer. "Studies on the Structure and Function of the Asialoglycoprotein Receptor in the Cell, in Vitro, and in Reconstituted Membranes." In Molecular Mechanisms of Membrane Fusion, 495–512. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4613-1659-6_36.

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Conference papers on the topic "Asialoglycoproteine"

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Tanaka, Haruyoshi. "Abstract 3112: Roles of asialoglycoprotein receptor 2 in gastric cancer progression." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-3112.

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Fuhlendorff, J., I. Clemmensen, and S. Magnusson. "PRIMARY STRUCTURE OF TETRANECTIN. SEQUENCE HOMOLOGY WITH ASIALOGLYCOPROTEIN RECEPTORS AND WITH PROTEOGLYCAN CORE PROTEIN FROM CARTILAGE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644380.

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Abstract:
Tetranectin (Mr = 68,000) is a tetrameric blood plasma protein, which binds to plasminogen and also to the lysine-binding site of the isolated kringle 4 from plasminogen. Its four polypeptide chains, which are non-covalently bound, each consists of 181 amino acid residues. We have determined the complete amino acid sequence and the disulfide bonds. Each position corresponds to a single amino acid residue except 34 which contains Ala and Ser and 37 which contains Val and Met in equimolar amounts. The three disulfide bonds connect Cys-50 to Cys-60, Cys-77 to Cys-176 and Cys-152 to Cys-168. The sequence of tetranectin was found to be homologous, to an extent indicating common ancestry, with the extracellular part of the asialoglyco-protein receptors and with the C-terminal globular domain of the cartilage proteoglycan core protein. Conserved residues include the six half-cystines of tetranectin. Therefore, we can now propose disulfide bond patterns for the proteins homologous with tetranectin. Supported by NIH-grant HL-16238 (S.M.), the Danish Science and Medical Research Councils, the Danish Cancer Society and NOVO Foundation.
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Ueno, Suguru, Yoshiaki Nodera, Laura Santos Gomez, Nobuaki Higashi, and Tatsuro Irimura. "Abstract 5121: Laminin 511 on human gastric carcinoma cells is a ligand for hepatic asialoglycoprotein receptor involved in liver metastasis." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-5121.

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