Relevant bibliographies by topics / Glycoproteins Receptors

Academic literature on the topic 'Glycoproteins Receptors'

Author: Grafiati
Published: 10 December 2022
Last updated: 30 January 2023

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Journal articles on the topic "Glycoproteins Receptors"

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Garner, Omai B., and Linda G. Baum. "Galectin–glycan lattices regulate cell-surface glycoprotein organization and signalling." Biochemical Society Transactions 36, no. 6 (November 19, 2008): 1472–77. http://dx.doi.org/10.1042/bst0361472.

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The formation of multivalent complexes of soluble galectins with glycoprotein receptors on the plasma membrane helps to organize glycoprotein assemblies on the surface of the cell. In some cell types, this formation of galectin–glycan lattices or scaffolds is critical for organizing plasma membrane domains, such as lipid rafts, or for targeted delivery of glycoproteins to the apical or basolateral surface. Galectin–glycan lattice formation is also involved in regulating the signalling threshold of some cell-surface glycoproteins, including T-cell receptors and growth factor receptors. Finally, galectin–glycan lattices can determine receptor residency time by inhibiting endocytosis of glycoprotein receptors from the cell surface, thus modulating the magnitude or duration of signalling from the cell surface. This paper reviews recent evidence in vitro and in vivo for critical physiological and cellular functions that are regulated by galectin–glycoprotein interactions.
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Dupuis, Gilles, and Marc Letellier. "Functional incorporation and preferred orientation of phytohemagglutinin receptor glycoproteins in phospholipid vesicles." Biochemistry and Cell Biology 65, no. 2 (February 1, 1987): 120–29. http://dx.doi.org/10.1139/o87-017.

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Porcine lymphocyte Phaseolus vulgaris phytohemagglutinin (PHA) receptor glycoproteins purified by affinity chromatography have been reassembled into vesicles made of phosphatidylcholine and phosphatidylserine by detergent (dodecyltrimethylammonium bromide) dialysis. The receptor glycoproteins were incorporated into the lipid vesicles in a nonselective manner with a yield of 65–70%. Vesicles containing the glycoproteins were sealed as evidenced by their impermeability to calcium ions, using quin 2 trapped inside the vesicles. The vesicles were agglutinated by PHA, suggesting that the saccharidic moiety of the reconstituted glycoproteins was, at least in part, oriented towads the extravesicular medium. This observation was further supported by the fact that the vesicles bound 125I-labeled PHA in a specific and saturable manner. At maximum amount of lectin bound, a ratio of 1.01 ± 0.05 μg of PHA per microgram glycoprotein incorporated was measured. When the binding data were analyzed by Scatchard plot, a downward concave profile was observed, suggestive of a positive cooperativity at low concentrations of lectin. The orientation of the reconstituted lectin receptor glycoproteins was determined by proteolytic treatments of labeled glycoproteins. The combined action of trypsin and chymotrypsin released, in the 120 000 × g supernatant, approximately 80% of label when 125I-tagged PHA receptor glycoproteins were incorporated into the vesicles. When the oligosaccharidic moieties of the receptor glycoproteins were specifically labeled, the simultaneous action of the two enzymes released approximately 70% of tritium labeling present in the reconstituted system. Taken together, these results suggest that the reconstituted PHA receptors are preferentially oriented into the phospholipid vesicles. The reconstituted PHA receptor glycoproteins competed effectively with cellular receptors in the assay of PHA-induced porcine lymphocyte activation. A 50% inhibition of [3H]thymidine incorporation was observed when 1 μg of glycoproteins in vesicles was added to the cultured cells, whereas vesicles alone had no effect at this (equivalent) concentration.
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Wessner, David R., Paul C. Shick, Jin-Hua Lu, Christine B. Cardellichio, Sara E. Gagneten, Nicole Beauchemin, Kathryn V. Holmes, and Gabriela S. Dveksler. "Mutational Analysis of the Virus and Monoclonal Antibody Binding Sites in MHVR, the Cellular Receptor of the Murine Coronavirus Mouse Hepatitis Virus Strain A59." Journal of Virology 72, no. 3 (March 1, 1998): 1941–48. http://dx.doi.org/10.1128/jvi.72.3.1941-1948.1998.

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ABSTRACT The primary cellular receptor for mouse hepatitis virus (MHV), a murine coronavirus, is MHVR (also referred to as Bgp1a or C-CAM), a transmembrane glycoprotein with four immunoglobulin-like domains in the murine biliary glycoprotein (Bgp) subfamily of the carcinoembryonic antigen (CEA) family. Other murine glycoproteins in the Bgp subfamily, including Bgp1b and Bgp2, also can serve as MHV receptors when transfected into MHV-resistant cells. Previous studies have shown that the 108-amino-acid N-terminal domain of MHVR is essential for virus receptor activity and is the binding site for monoclonal antibody (MAb) CC1, an antireceptor MAb that blocks MHV infection in vivo and in vitro. To further elucidate the regions of MHVR required for virus receptor activity and MAb CC1 binding, we constructed chimeras between MHVR and other members of the CEA family and tested them for MHV strain A59 (MHV-A59) receptor activity and MAb CC1 binding activity. In addition, we used site-directed mutagenesis to introduce selected amino acid changes into the N-terminal domains of MHVR and these chimeras and tested the abilities of these mutant glycoproteins to bind MAb CC1 and to function as MHV receptors. Several recombinant glycoproteins exhibited virus receptor activity but did not bind MAb CC1, indicating that the virus and MAb binding sites on the N-terminal domain of MHVR are not identical. Analysis of the recombinant glycoproteins showed that a short region of MHVR, between amino acids 34 and 52, is critical for MHV-A59 receptor activity. Additional regions of the N-terminal variable domain and the constant domains, however, greatly affected receptor activity. Thus, the molecular context in which the amino acids critical for MHV-A59 receptor activity are found profoundly influences the virus receptor activity of the glycoprotein.
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Morimoto, Kanta, Noriko Suzuki, Isei Tanida, Soichiro Kakuta, Yoko Furuta, Yasuo Uchiyama, Kentaro Hanada, Yusuke Suzuki, and Toshiyuki Yamaji. "Blood group P1 antigen–bearing glycoproteins are functional but less efficient receptors of Shiga toxin than conventional glycolipid-based receptors." Journal of Biological Chemistry 295, no. 28 (May 14, 2020): 9490–501. http://dx.doi.org/10.1074/jbc.ra120.013926.

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Shiga toxin (STx) is a virulence factor produced by enterohemorrhagic Escherichia coli. STx is taken up by mammalian host cells by binding to the glycosphingolipid (GSL) globotriaosylceramide (Gb3; Galα1-4Galβ1-4Glc-ceramide) and causes cell death after its retrograde membrane transport. However, the contribution of the hydrophobic portion of Gb3 (ceramide) to STx transport remains unclear. In pigeons, blood group P1 glycan antigens (Galα1-4Galβ1-4GlcNAc-) are expressed on glycoproteins that are synthesized by α1,4-galactosyltransferase 2 (pA4GalT2). To examine whether these glycoproteins can also function as STx receptors, here we constructed glycan-remodeled HeLa cell variants lacking Gb3 expression but instead expressing pA4GalT2-synthesized P1 glycan antigens on glycoproteins. We compared STx binding and sensitivity of these variants with those of the parental, Gb3-expressing HeLa cells. The glycan-remodeled cells bound STx1 via N-glycans of glycoproteins and were sensitive to STx1 even without Gb3 expression, indicating that P1-containing glycoproteins also function as STx receptors. However, these variants were significantly less sensitive to STx than the parent cells. Fluorescence microscopy and correlative light EM revealed that the STx1 B subunit accumulates to lower levels in the Golgi apparatus after glycoprotein-mediated than after Gb3-mediated uptake but instead accumulates in vacuole-like structures probably derived from early endosomes. Furthermore, coexpression of Galα1-4Gal on both glycoproteins and GSLs reduced the sensitivity of cells to STx1 compared with those expressing Galα1-4Gal only on GSLs, probably because of competition for STx binding or internalization. We conclude that lipid-based receptors are much more effective in STx retrograde transport and mediate greater STx cytotoxicity than protein-based receptors.
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Melder, Deborah C., Gennett M. Pike, Matthew W. VanBrocklin, and Mark J. Federspiel. "Model of the TVA Receptor Determinants Required for Efficient Infection by Subgroup A Avian Sarcoma and Leukosis Viruses." Journal of Virology 89, no. 4 (December 3, 2014): 2136–48. http://dx.doi.org/10.1128/jvi.02339-14.

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ABSTRACTThe study of the interactions of subgroup A avian sarcoma and leucosis viruses [ASLV(A)] with the TVA receptor required to infect cells offers a powerful experimental model of retroviral entry. Several regions and specific residues in the TVA receptor have previously been identified to be critical determinants of the binding affinity with ASLV(A) envelope glycoproteins and to mediate efficient infection. Two homologs of the TVA receptor have been cloned: the original quail TVA receptor, which has been the basis for most of the initial characterization of the ASLV(A) TVA, and the chicken TVA receptor, which is 65% identical to the quail receptor overall but identical in the region thought to be critical for infection. Our previous work characterized three mutant ASLV(A) isolates that could efficiently bind and infect cells using the chicken TVA receptor homolog but not using the quail TVA receptor homolog, with the infectivity of one mutant virus being >500-fold less with the quail TVA receptor. The mutant viruses contained mutations in the hr1 region of the surface glycoprotein. Using chimeras of the quail and chicken TVA receptors, we have identified new residues of TVA critical for the binding affinity and entry of ASLV(A) using the mutant glycoproteins and viruses to probe the function of those residues. The quail TVA receptor required changes at residues 10, 14, and 31 of the corresponding chicken TVA residues to bind wild-type and mutant ASLV(A) glycoproteins with a high affinity and recover the ability to mediate efficient infection of cells. A model of the TVA determinants critical for interacting with ASLV(A) glycoproteins is proposed.IMPORTANCEA detailed understanding of how retroviruses enter cells, evolve to use new receptors, and maintain efficient entry is crucial for identifying new targets for combating retrovirus infection and pathogenesis, as well as for developing new approaches for targeted gene delivery. Since all retroviruses share an envelope glycoprotein organization, they likely share a mechanism of receptor triggering to begin the entry process. Multiple, noncontiguous interaction determinants located in the receptor and the surface (SU) glycoprotein hypervariable domains are required for binding affinity and to restrict or broaden receptor usage. In this study, further mechanistic details of the entry process were elucidated by characterizing the ASLV(A) glycoprotein interactions with the TVA receptor required for entry. The ASLV(A) envelope glycoproteins are organized into functional domains that allow changes in receptor choice to occur by mutation and/or recombination while maintaining a critical level of receptor binding affinity and an ability to trigger glycoprotein conformational changes.
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Kolchinsky, Peter, Enko Kiprilov, and Joseph Sodroski. "Increased Neutralization Sensitivity of CD4-Independent Human Immunodeficiency Virus Variants." Journal of Virology 75, no. 5 (March 1, 2001): 2041–50. http://dx.doi.org/10.1128/jvi.75.5.2041-2050.2001.

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ABSTRACT Naturally occurring human immunodeficiency virus (HIV-1) variants require the presence of CD4 and specific chemokine receptors to enter a cell. In the laboratory, HIV-1 variants that are capable of bypassing CD4 and utilizing only the CCR5 chemokine receptor for virus entry have been generated. Here we report that these CD4-independent viruses are significantly more sensitive to neutralization by soluble CD4 and a variety of antibodies. The same amino acid changes in the HIV-1 gp120 envelope glycoprotein determined CD4 independence and neutralization sensitivity. The CD4-independent envelope glycoproteins exhibited higher affinity for antibodies against CD4-induced gp120 epitopes but not other neutralizing ligands. The CD4-independent envelope glycoproteins did not exhibit increased lability relative to the wild-type envelope glycoproteins. The utilization of two receptors apparently allows HIV-1 to maintain a more neutralization-resistant state prior to engaging CD4 on the target cell, explaining the rarity of CD4 independence in wild-type HIV-1.
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Bowden, Thomas A., Max Crispin, E. Yvonne Jones, and David I. Stuart. "Shared paramyxoviral glycoprotein architecture is adapted for diverse attachment strategies." Biochemical Society Transactions 38, no. 5 (September 24, 2010): 1349–55. http://dx.doi.org/10.1042/bst0381349.

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Members within the paramyxovirus subfamily Paramyxovirinae constitute a large number of highly virulent human and animal pathogens. The glycoproteins present on these viruses are responsible for mediating host cell attachment and fusion and are key targets for the design of antiviral entry inhibitors. In the present review, we discuss recent structural studies which have led to a better understanding of the various mechanisms by which different paramyxoviruses use their attachment glycoproteins to hijack specific protein and glycan cell-surface receptors to facilitate viral entry. It is observed that the paramyxovirus attachment glycoprotein consists of a conserved overall structure which includes an N-terminal six-bladed β-propeller domain which is responsible for cell receptor binding. Crystal structures of this domain from different biomedically important paramyxoviruses, including measles, Nipah, Hendra, Newcastle disease and parainfluenza viruses, alone and in complex with their functional cell-surface receptors, demonstrate three contrasting mechanisms of receptor engagement that paramyxoviruses have evolved to confer discreet protein- and glycan-receptor specificity. This structural information highlights the adaptability of the paramyxovirus attachment glycoprotein surface and the potential for the emergence of new and potentially harmful viruses in human hosts.
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Federspiel, Mark J. "Reverse Engineering Provides Insights on the Evolution of Subgroups A to E Avian Sarcoma and Leukosis Virus Receptor Specificity." Viruses 11, no. 6 (May 30, 2019): 497. http://dx.doi.org/10.3390/v11060497.

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The initial step of retrovirus entry—the interaction between the virus envelope glycoprotein trimer and a cellular receptor—is complex, involving multiple, noncontiguous determinants in both proteins that specify receptor choice, binding affinity and the ability to trigger conformational changes in the viral glycoproteins. Despite the complexity of this interaction, retroviruses have the ability to evolve the structure of their envelope glycoproteins to use a different cellular protein as receptors. The highly homologous subgroup A to E Avian Sarcoma and Leukosis Virus (ASLV) glycoproteins belong to the group of class 1 viral fusion proteins with a two-step triggering mechanism that allows experimental access to intermediate structures during the fusion process. We and others have taken advantage of replication-competent ASLVs and exploited genetic selection strategies to force the ASLVs to naturally evolve and acquire envelope glycoprotein mutations to escape the pressure on virus entry and still yield a functional replicating virus. This approach allows for the simultaneous selection of multiple mutations in multiple functional domains of the envelope glycoprotein that may be required to yield a functional virus. Here, we review the ASLV family and experimental system and the reverse engineering approaches used to understand the evolution of ASLV receptor usage.
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Zhao, Xuesen, Fang Guo, Mary Ann Comunale, Anand Mehta, Mohit Sehgal, Pooja Jain, Andrea Cuconati, et al. "Inhibition of Endoplasmic Reticulum-Resident Glucosidases Impairs Severe Acute Respiratory Syndrome Coronavirus and Human Coronavirus NL63 Spike Protein-Mediated Entry by Altering the Glycan Processing of Angiotensin I-Converting Enzyme 2." Antimicrobial Agents and Chemotherapy 59, no. 1 (October 27, 2014): 206–16. http://dx.doi.org/10.1128/aac.03999-14.

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ABSTRACTEndoplasmic reticulum (ER)-resident glucosidases I and II sequentially trim the three terminal glucose moieties on the N-linked glycans attached to nascent glycoproteins. These reactions are the first steps of N-linked glycan processing and are essential for proper folding and function of many glycoproteins. Because most of the viral envelope glycoproteins contain N-linked glycans, inhibition of ER glucosidases with derivatives of 1-deoxynojirimycin, i.e., iminosugars, efficiently disrupts the morphogenesis of a broad spectrum of enveloped viruses. However, like viral envelope proteins, the cellular receptors of many viruses are also glycoproteins. It is therefore possible that inhibition of ER glucosidases not only compromises virion production but also disrupts expression and function of viral receptors and thus inhibits virus entry into host cells. Indeed, we demonstrate here that iminosugar treatment altered the N-linked glycan structure of angiotensin I-converting enzyme 2 (ACE2), which did not affect its expression on the cell surface or its binding of the severe acute respiratory syndrome coronavirus (SARS-CoV) spike glycoprotein. However, alteration of N-linked glycans of ACE2 impaired its ability to support the transduction of SARS-CoV and human coronavirus NL63 (HCoV-NL63) spike glycoprotein-pseudotyped lentiviral particles by disruption of the viral envelope protein-triggered membrane fusion. Hence, in addition to reducing the production of infectious virions, inhibition of ER glucosidases also impairs the entry of selected viruses via a post-receptor-binding mechanism.
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Coller, B. S. "Activation affects access to the platelet receptor for adhesive glycoproteins." Journal of Cell Biology 103, no. 2 (August 1, 1986): 451–56. http://dx.doi.org/10.1083/jcb.103.2.451.

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Blood platelets have a receptor for macromolecular adhesive glycoproteins, located on a heteroduplex membrane glycoprotein complex (GPIIb/IIIa) that only becomes "exposed" when platelets are activated. Binding of the adhesive glycoproteins, in particular fibrinogen, to the receptor is required for platelet aggregation, which in turn is required to arrest bleeding. A murine monoclonal antibody whose rate of binding to the receptor is affected by platelet activation was both cross-linked and fragmented to assess the effects of changes in molecular size on its rate of binding to unactivated and activated platelets. The results indicate that small molecules can bind more rapidly to the receptors on unactivated platelets than can large molecules and that activation involves a conformational and/or microenvironmental change that permits the large molecules to bind more rapidly.
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Dissertations / Theses on the topic "Glycoproteins Receptors"

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Hyland, Robert H. "Heterodimer formation and activation of the leukocyte integrins." Thesis, University of Oxford, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.365411.

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Tiu, Hiu-kwan. "Vitellogenesis and vitellogenin receptor in shrimp : from the sites of synthesis to the final storage in the ovary /." View the Table of Contents & Abstract, 2007. http://sunzi.lib.hku.hk/hkuto/record/B38481030.

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Thomas, Elaine Rhiannon. "Neutralisation of HIV-2 interactions between viral glycoproteins and cell surface receptors." Thesis, University College London (University of London), 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.397817.

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Lau, Suk-ling Joanna, and 劉淑玲. "Molecular characterization of the chicken growth hormone receptorgene." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2005. http://hub.hku.hk/bib/B45015430.

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Mirza, Deeman. "Probing the interaction of hepatitis C virus glycoproteins with putative receptors and neutralising antibodies." Thesis, University of Nottingham, 2012. http://eprints.nottingham.ac.uk/12685/.

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Hepatitis C virus (HCV) is a hepatotropic blood-borne virus which causes chronic hepatitis in the majority of cases and represents a global health burden. In order for HCV to enter cells, proteins on the surface of the virus must interact and bind to receptors on target cells. HCV surface molecules involved with receptor binding, and cellular entry, as well as immune escape, are the glycoproteins E1 and E2. The cellular receptors SRBI, CD81, CLDNs and most recently occludin have been shown to facilitate HCV entry into hepatocytes. Several conservative regions on E1E2 have, through substitution mutagenesis, proven to be important for receptor binding and antibody neutralisation. We aimed to characterise one discontinuous region, amino acid residues 611, 613-619 and 621, and its role in the interaction with CD81 by single alanine substitution mutagenesis. Mutant plasmids were transfected into HEK 293FT cells and assessed for protein expression and binding by conformation-sensitive, CD81-inhibiting antibodies. Also, to investigate whether a conformational change of the E1E2 occurs upon SRB1 binding, rendering the CD81 binding domains accessible, two assays have been compared. A plate based experiment, exclusive of SRBI and a cell based assay, including SRBI was designed to examine the antigenic exposure of the CD81 binding regions to targeting monoclonal antibodies. Additionally, Huh-7 cells expressing different levels of SRBI were used to investigate whether some HCVpp isolates rely on high SRB1 levels for infectivity and sensitivity to neutralising antibodies. These studies were performed to help elucidate the regions and residues important in HCV E1E2: receptor interaction and their interplay with each other and with neutralising antibodies.
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Gantner, Benjamin N. "Dectin-1 and toll-like receptor 2 : recognition of pathogens through multiple receptors shapes the innate immune response /." Thesis, Connect to this title online; UW restricted, 2004. http://hdl.handle.net/1773/8346.

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Lau, Suk-ling Joanna. "Molecular characterization of the chicken growth hormone receptor gene /." View the Table of Contents & Abstract, 2005. http://sunzi.lib.hku.hk/hkuto/record/B32037211.

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Tiu, Hiu-kwan, and 刁曉君. "Vitellogenesis and vitellogenin receptor in shrimp: from the sites of synthesis to the final storage in theovary." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2007. http://hub.hku.hk/bib/B39360623.

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Lam, Pui-yi, and 林佩儀. "Characterization of neutralizing and receptor binding activities in human coronavirus NL63 spike protein." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2009. http://hub.hku.hk/bib/B41896865.

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Lam, Pui-yi. "Characterization of neutralizing and receptor binding activities in human coronavirus NL63 spike protein." Click to view the E-thesis via HKUTO, 2009. http://sunzi.lib.hku.hk/hkuto/record/B41896865.

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Books on the topic "Glycoproteins Receptors"

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T, Preissner Klaus, ed. Biology of vitronectins and their receptors: Proceedings of the First International Vitronectin Workshop, Rauischholzhausen Castle, Marburg, Germany, 25-28 August, 1993. Amsterdam: Excerpta Medica, 1993.

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Murphy, Natalie P. Coronary thrombosis and thrombolysis: The role of platelet glycoprotein IIb/IIIa. Dublin: University College Dublin, 1996.

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Pharand, Chantal. The use of platelet glycoprotein IIB/IIIA receptor antagonists in the management of unstable angina and non-st-elevation myocardial infarction: A critical evaluation. [Toronto?: s.n., 2000.

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E, Vance Dennis, and Vance Jean E, eds. Biochemistry of lipids, lipoproteins, and membranes. Amsterdam: Elsevier, 1991.

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Rich, Tina. Toll and Toll-Like Receptors : : An Immunologic Perspective. Springer, 2010.

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Rich, Tina. Toll and Toll-Like Receptors : : An Immunologic Perspective. Springer London, Limited, 2007.

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Preissner, Klaus T., and Sylvia Rosenblatt. Biology of Vitronectins and Their Receptors: Proceedings of the First International Vitronectin Workshop, Rauischholzhausen Castle, Marburg, Germany (International Congress Series). Elsevier Science Pub Co, 1993.

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Zona Pellucida Domain Proteins. John Wiley and Sons Ltd, 2016.

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Toll and Toll-Like Receptors:: An Immunologic Perspective (Molecular Biology Intelligence Unit). Springer, 2005.

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Jarvie, Keith Roger. The glycoprotein nature of dopamine D1 and D2 receptors. 1990.

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Book chapters on the topic "Glycoproteins Receptors"

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Phillips, David R. "Receptors for Platelet Agonists." In Platelet Membrane Glycoproteins, 145–69. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-4880-1_7.

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Lüscher, Ernst F. "Plasma Membrane Receptors and Platelet Response." In Platelet Membrane Glycoproteins, 3–9. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-4880-1_1.

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Brockhausen, Inka, and William Kuhns. "Growth- and Hormone-Related Functions of Glycoproteins and Cell Surface Receptors." In Glycoproteins and Human Disease, 85–98. Berlin, Heidelberg: Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-662-21960-7_11.

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Cosman, David, Jan Chalupny, Mei-Ling Hsu, Claire Sutherland, Jürgen Müllberg, Marek Kubin, Neil Fanger, and Luis Borges. "Interaction of human cytomegalovirus glycoproteins with immunoreceptors." In Activating and Inhibitory Immunoglobulin-like Receptors, 91–98. Tokyo: Springer Japan, 2001. http://dx.doi.org/10.1007/978-4-431-53940-7_12.

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Weiss, Robin A. "Cellular Receptors and Viral Glycoproteins Involved in Retrovirus Entry." In The Retroviridae, 1–108. Boston, MA: Springer US, 1993. http://dx.doi.org/10.1007/978-1-4899-1627-3_1.

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Douville, Philippe, and Salvatore Carbonetto. "Extracellular Matrix Adhesive Glycoproteins and Their Receptors in the Nervous System." In Neurobiology of Glycoconjugates, 383–409. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4757-5955-6_13.

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Hensley, Lisa E., and Ralph S. Baric. "Human Biliary Glycoproteins Function as Receptors for Interspecies Transfer of Mouse Hepatitis Virus." In Advances in Experimental Medicine and Biology, 43–52. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-5331-1_6.

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Saji, Motoyasu, Shoichiro Ikuyama, Hiroki Shimura, Toshiaki Ban, Shinji Kosugi, Akinari Hidaka, Fumikazu Okajima, et al. "Structure and Regulated Expression of the TSH Receptor Gene: Differences and Similarities to Gonadotropin Receptors." In Glycoprotein Hormones, 177–216. New York, NY: Springer New York, 1994. http://dx.doi.org/10.1007/978-1-4613-8386-4_16.

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Bock, Hans H., and Joachim Herz. "Apolipoprotein E Receptor 2 and Very-Low-Density Lipoprotein Receptor: An Overview." In Reelin Glycoprotein, 15–35. New York, NY: Springer New York, 2008. http://dx.doi.org/10.1007/978-0-387-76761-1_2.

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Ji, Tae H., Huawei Zeng, and Inhae Ji. "Hormone Binding and Activation of the LH/CG Receptor." In Glycoprotein Hormones, 226–49. New York, NY: Springer New York, 1994. http://dx.doi.org/10.1007/978-1-4613-8386-4_18.

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Conference papers on the topic "Glycoproteins Receptors"

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Gorski, J., L. Van Hove, F. Vanlangendonck, M. A. Boogaerts, R. L. Verwilghen, and J. Vermylen. "PLATELET MEMBRANE GLYCOPROTEINS ABNORMALITIES IN PATIENTS WITH ACUTE LEUKEMIAS AND MALIGNANT LYMPHOMAS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643201.

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Membrane glycoproteins are implicated in platelet functions.In myeloproliferative disorders some of the platelet functions are known to be perturbated and an abnormal glycoproteins pattern was demonstrated ear-lier.In this study flow cytometry analysis of human platelet membrane glycoproteins IIa and IIIa in patients with acute leukemias and malignant lymphomas has been performed using monoclonal antibodies against these glycoproteins.A reduction in number of glycoproteins receptors on platelet membrane was demonstrated in patients with acute leukemias and malignant lymphomas in comparison with platelets of healthy donors.In patients with leukemias the positive correlation of percentage of platelets recovered in various density receptor regions to bleeding time and negative correlation to platelet number for both glycoproteins have been found.The study demonstrated that flow cytometry can be a useful method of analysis of platelet membrane glycoproteins, and that the patients with acute leukemias and malignant lymphomas have the number of glycoproteins reduced.
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Phillips, David R., Laurence A. Fitzgerald, Leslie V. Parise, and Israel F. Charo. "The Platelet Membrane Glycoprotein IIb-III a Complex: Member of a Superfamily of Adhesive Protein Receptors." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643727.

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The glycoprotein (GP) IIb-IIIa complex isthe receptor for fibrinogen,fibronectin and von Willebrand factor on the surface of activated platelets that mediates platelet aggregation.The GP IIb-IIIa complex contains two subunits; an a subunit, GP IIb, and a smaller 8 subunit, GP IIIa. To identify the subunits of GP IIb-IIIa responsible for fibrinogen binding, we examined the ability of purified subunitsto bind to immobilized fibrinogen. Both the GP IIb and the GP III a subunits have fibrinogen binding activity, suggesting that fibrinogen binds to multiple sites onthe GP I Ib-IIIa complex.A GP Ilb-IIIa-like complex has been identified on endothelial cells which is immunoreactive with antibodies raised against platelet GP IIb-III a. This complex binds a similar broadspectrum of adhesive proteins as plateletGP IIb-IIIa and appears to mediate the attachment of endothelial cells to the extracellular matrix. We have established, however, that while GP Ilia in endothelial cells is the same primary translation product as platelet GP Ilia, the endothelialcell "GP lib" is a different, but closely related, protein from platelet GP lib. This close relationship of the receptors on these two cells is reflective of recent observations in several laboratories which have shown that a wide variety of cells contain surface glycoproteins which have structural and functionalsimilarities to the GP IIb-IIIa complexinplatelets and the "GP IIb-IIIa-like" complex in endothelial cells.These glycoproteins, which have been termed "integrins" or "cytoadhesins", are complexes of highly homologous a and 8 subunits, mediate cell-cell or cel 1-substrata interactions, and may also bind the RGD sequence on adhesive proteins. Although in vertebrates this family includes at least ten receptor complexes, there are only three known 8 subunits, each of which defines a subset of receptors. One is GP IIIa, the 8 subunit for GP IIb-IIIa and the vitronectin receptor; another is the 8 subunit for the fibronectin receptors and the very late antigens on lymphocytes; the third is the 8subunit of the Mac-1, LFA-1, and P150/95 antigens on leukocytes. These three 6 subunits have been cloned and sequenced. Each contains 746-777 amino acids, a singletransmembrane domain near the carboxy terminus, 56 cysteines in identical positionsof the proteins, 31 of which are clustered into four repeats, and an overall identity in 45-47% of their amino acids. The asubunits are more diverse in size but appear to have a similar degree of homology.The available sequence information indicates that they contain a single transmembrane domain near their carbody terminii and four tandem repeats near their amino terminii which include sequences indicativeof four Ca2+-binding sites. These may account for the known Ca2+-binding properties of GP IIb. GP I Ib-IIIa and the other adhesive protein receptors therefore appear to have two membrane insertion sites, one on each subunit,with short cytoplasmic domains derived from the carboxy terminii of the two subunits. The amino terminii along with most ofthe mass of these proteins is extracellular. It can be anticipated that the highlyhomologous sequences between GP IIb-IIIa and the other adhesive protein receptors will help identify the functional domainswhich have been conserved since their evolutionary divergences.
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Butler-Zimrin, A. E., J. S. Bennett, M. Poncz, E. Schwartz, S. Surrey, R. Eisman, R. A. Heidenreich, and G. Vilaire. "ISOLATION AND CHARACTERIZATION OF cDNA CLONES FOR THE PLATELET MEMBRANE GLYCOPROTEINS IIb and IIIa." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643961.

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The platelet membrane GPIIb/GPIIIa complex on activated platelets contains receptors for fibrinogen, von Willebrand factor, and fibronectin. GPIIb and GPIlia also appear to be members of a family of membrane receptors involved in cell-cell and cell-matrix interactions. To study the structure of GPIIb and GPIIIa, we have constructed an expression library in the vector lambda gtll using mRNA from the HEL cell line and screened it with polyclonal antibody against each platelet protein. HEL cells constitutively express proteins similar to platelet GPIIb and GPIIIa. A 3.2kb GPIIb cDNA clone was identified that encodes for all 1008 amino acids of GPIIb including the known N-terminal amino acids of the α Cand βsubunits. This confirms that GPIIb is synthesized as a single chain polypeptide that is cleaved into two disulfide-linked subunits posttranslation. Analysis of the amino acid sequence revealed a major C-terminal transmembrane domain in the βsubunit, two potential transmembrane domains near the N-terminus of the αsubunit, and four possible N-linked glycosylation sites. Approximately 30% amino acid identity was found between GPIIb and the available amino acid sequences for the larger chains of the fibronectin and vitronectin receptors. Initial sequence analysis of a 3.8kb cDNA for GPIIIa included the known N-terminal amino acids of the platelet protein. Northern blot analysis was performed using HEL cell total RNA. The GPIIb cDNA hybridized to a 4.1kb mRNA while the GPIIIa cDNA hybridized to a 5.8kb mRNA. This indicates that the two cDNAs do not cross-hybridize and suggests that GPIIb and GPIIIa are encoded by separate genes. The availability of these cDNA for GPIIb and GPIIIa will facilitate study of the structure and function of the proteins and will aid in clarifying their relationship to other adhesive protein receptors.
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Bakhit, C., D. Lewis, R. Billings, and B. Malfroy. "CELLULAR CATABOLISM OF RECOMBINANT TISSUE-TYPE PLASMINOGEN ACTIVATOR: IDENTIFICATION AND CHARACTERIZATION OF A NOVEL HIGH AFFINITY UPTAKE SYSTEM ON RAT HEPATOCYTES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644400.

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The uptake, internalization and intracellular degradation of 125I-labeled rt-PA (125I-rt-PA) by isolated rat hepatocytes was investigated. Incubation at 37°C resulted in internalization of 125I-rt-PA, followed by the appearance of labeled trichloroacetic acid-soluble (TCA) material in the inclubation media due to degradation of rt-PA. Degradation of rt-PA was inhibited by the presence of NH4Cl (10mM) or chloroquine (ImM) (lysosoma tropic agents) in the incubation media. This suggests that rt-PA degradation occurs intracellularly, perhaps within the lysosomes. 125I-rt-PA was taken up by rat hepatocytes through a specific, high affinity mechanism. Scatchard analysis of the data indicated that 106 molecules of rt-PA were taken up per cell/hour and the calculated dissociation constant was lOnM. Uptake of 125I-rt-PA was not inhibited by glycopeptides isolated from rt-PA nor by several other glycoproteins known to be cleared by identified hepatic receptors. These results suggest that the uptake of rt-PA by rat hepatocytes involves a receptor specific for t-PA and is not mediated by a carbohydrate specific receptor.
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Mazzucato, M., M. G. Del Ben, A. Casonato, V. De Angelis, and L. De Marco. "PLATELET MEMBRANE GLYCOPROTEINS ABNORMALITIES IN MYELOPROLIFERATIVE DISORDERS. STRUCTURE/FUNCTION RELATIONSHIP." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643508.

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The platelet membrane glycoproteins (GP) lb and GPIIb/IIIa were investigated in 10 patients with myeloproliferative disorders. 2 patients had essential thrombocytemia (ET), 2 had chronic myeloid leukemia (CML) and 6 policytemia vera (PV). The number of GP molecules were detected by radiolabelled monoclonal antibodies anti GPIb and anti GPIIb/IIIa complex (gift of dr. Z.M. Ruggeri) and their function was evaluated by using, in a binding assay, purified radiolabelled asialo von Willebrand factor (1251 ASvWF) and purified radiolabelled fibrinogen (1251 F). Binding isotherms were evaluated by Scatchard type analysis using the computer assisted programLigand. The binding of 1251 anti GPIb to the platelets of the ten patients showed 14,955 ∓ 4,636 molecules/platelet (M/Plt) compared to 19,790 ∓ 3,791 M/Plt of 11 normals with a p value < 0.01. The binding of 125IAsvWF to the GPIb of nonstimulated platelets in platelet rich plasma (PRP) was then measured and ound to be decreased. The dissociation constants (Kds) were within normal values except in one patient. There was a good correlation (r = 0.91, p < 0.01) between the amount of 1251 ASvWF bound and GPIb molecules. The binding of radiolabelled anti GPIIb/IIIa to the platelets of six patients (4 with PV and 2 with CML) was measured and found to be constantly decreased in all patients with a mean value of 25,349 ∓ 2,077 M/Plt compared to 43,192 ∓ 6,354 M/Plt found in normals (p < 0.01). 1251 fibrinogen binding to the GPIIb/IIIa complex of ADP + adrenalin stimulated washed platelet was studied in 2 patients and we found 16,267 M/Plt and 14,752 M/Plt respectively, significantly diminished when compared to the mean value of 36,591 M/Plt found in 2 normal controls. The Kds were within normal values. Our studies demonstrate a significant decrease of GPIb and GPIIb/IIIa on the platelet membrane of patients with myeloproliferative disorders. Furthermore this decrease is accompanied by a diminished binding of both vWF and F to their platelets receptors. These findings may partly explain the hemorragic tendency often encountered in these patients.
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Charo, I. F., L. A. Fitzgerald, D. Meyer, L. S. Bekeart, and D. R. Phillips. "PLATELET GLYCOPROTEIN IIb-IIIa-LIKE PROTEINS MEDIATE ENDOTHELIAL CELL ATTACHMENT TO ADHESIVE MATRIX PROTEINS AND ARE UP-REGULATED BY PHORBOL ESTERS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642816.

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Human endothelial cells (EC) express glycoproteins that are similar to the platelet glycoprotein IIb-IIIa complex (GP IIb-IIIa), the platelet receptor for adhesive proteins. Although GP IIb—IIIa is abundant in both platelets and EC, its only known function is to mediate platelet aggregation. The present study tests the hypotheses that EC attachment to adhesive proteins in the extracellular matrix is mediated by the GP IIb-IIIa-1ike proteins. Endothelial cells attached well to glass slides that were previously coated with adhesive proteins, but not albumin. To determine whether GP IIb-IIIa was involved, EC adherence was measured in the presence and absence of a GP IIb-IIIa monoclonal antibody (7E3) which inhibits fibrinogen (Fg) binding to platelets. The attachment of EC to Fg and von Willebrand factor (vWf), but not fibronectin (Fn) coated slides, was completely inhibited by 7E3. Attachment to vitronectin was partially inhibited. In contrast, EC attachment to Fn was specifically inhibited by a Fn-receptor antibody. Endothelial cell adherence to vWf was also inhibited by a monoclonal antibody (Mab9) against the GP IIb-IIIa binding domain of vWf, but not by antibodies agains.t other portions of vWf. We have further found that 7E3 disrupts monolayers of endothelial cells by detaching the cells from their extracellular matrix. EC incubated in phorbol myris-tate.acetate (PMA) increase in size and appear more tightly adherent to their extracellular matrix. To determine if PMA increases synthesis of cellular receptors for matrix proteins, we have used cDNA probes to measure the mRNA levels of the large subunit of the Fn-receptor (FnRα) and GP IIIa in EC. After a 4 hour incubation in the presence of PMA (10 nM), there was a 2-fold increase in the mRNA levels of both FnRα and GP IIIa, as well as increased cell spreading on the matrix. We conclude: i) the GP Ilb-IIIa complex in EC is a surface receptor for specific adhesive proteins, and is distinct from the FnR, and ii) both GP IIIa and FnRα synthesis are increased by PMA, which causes a concomittant change in cell morphology.
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Hawiger, J. "PLATELET RECEPTOR RECOGNITION DOMAINS AND THEIR SYNTHETIC PEPTIDE ANALOGS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643726.

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Adhesive molecules and their receptorsplay an essential role in hemostasis and thrombosis. Platelet thrombi are formed through the interaction of cell adhesion molecules (CAMs) with intercellular adhesion molecules (IAMs)and substrate adhesion molecules (SAMs). Platelet CAMs encompass membrane glycoproteins lb, lib, Ilia,and possibly la and IV, which constitutemembrane receptors for IAMs(e.g., fibrinogen) and for SAMs encompassingvon Willebrand Factor (vWF), fibronectin, vitronectin, collagen, and thrcmbospondin. Receptorfunction of platelet CAMs can be specific,i.e., only one adhesive protein among IAMs and SAMs is selected forbinding as exemplified by GPIb and vWF. Alternatively,more than one adhesive protein can interact with platelet CAMs comprising the GPIIb/IIIa complex.This common adhesive receptor mechanism switched on by thrombin, ADP, phorbol ester or ionophore A23187 is turned off by a rise in intraplatelet cyclic AMP which provides a negative control.Fibrinogen, the most abundant adhesiveprotein in plasma, interacts with platelet CAMs via receptor recognition domains on gamma and alpha chains. Pinpointing platelet receptor recognition domain to a carboxy-terminal segment of the gamma chain encompassing residues 400-411gave rise to a series of synthetic peptide analogs which do not interfere with themetabolic pathways of platelets but blockbinding of I fibrinogen to its receptors on stimulated platelets, inhibit their aggregation in vitro, and formation of a platelet thrombus in vivo. The alpha chain of human fibrinogen contains the sequenceRGD (residues 95-97 and 572-574). Synthetpeptide analogs of the RGD sequence, which constitute the "cell adhesion site" of fibronectin, also inhibit binding of 125I-fibrinogen to stimulated platelets. However, these synthetic peptides are not "specific" for fibrinogen chains because thealpha chain of human fibrinogen which hasnosequence homology with gamma 400-411 is prevented by a peptide gamma 400-411 from interaction with platelet receptors. Viceversa, the human gamma chain is blocked by tetrapeptide RGDS not expressed in the human gamma chain. Interaction of human vWF with human platelets is blocked by synthetic peptide analogs of gamma 400-411 (not present in vWF)and of RGD sequence (present in vWF).These synthetic peptides inhibite "common" receptor pathwaystimulated with ADP, thrombin, or phorbolester, but they do not interfere with binding of 125I-vWF via a "specific" pathvoy induced with ristocetin and involving GPIb.The design of synthetic peptide analogs which inhibit platelet receptors for adhesive molecules includes the following considerations: ligand specificity (is thepeptide inhibitory toward binding of one or more adhesive molecules?),cell speciicity (is the peptide specific for platelets or does it perturb the adhesive properties of other cells, e.g.,endothelium?);the hydrophilic character; protection against degradation by peptidases; and a sufficiently long half-life to achieve platelet inhibitory potency in vivo without overloading the blood with excessive amounts of peptide.This is accomplished by constructing a peptide-albumin conjugate with ahalf-life extended at least 30 times.Whenpeptides are modeled with predominantly hydrophilic or hydrophobic residues, only the hydrophilic peptide remained active to block the platelet receptor. This agreed with the general observation that sequences on adhesive molecules that are knownto interact with cellular receptors have a hydrophilic rather than a hydrophobic character. Furthermore, changing the charge of synthetic peptides toward the negative reduced the reactivity, whereas introducing additional arginine residues enhanced the reactivity toward platelet receptors. Localization of the functionally important binding domain in the flexible segment of an adhesive protein increases the likelihood that the synthetic peptide will assume the conformation mimicking such a domain in the native adhesive protein. Structure-function studies of the receptor recognition domains on adhesive molecules led to development of a new class of platelet inhibitors acting at the membranereceptors responsible for anchoring of platelets to the vessel wall and linking them to each other.
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8

Marchant, David, Farnoosh Tayyari, Theo Moraes, Peter Mastrangelo, Samuel J. Wadsworth, and Richard G. Hegele. "The Respiratory Syncytial Virus F And G Glycoproteins Bind Specific Cellular Receptors To Facilitate Virus Entry Into Bronchial Epithelial Cells." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a6880.

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Altieri, Dario C., Rossella Bader, and Pier M. Mannucci. "STRUCTURAL DIVERSITY AMONG CELLULAR ADHESION RECEPTORS: FIBRINOGEN BINDING IS A NOVEL BIOLOGICAL PROPERTY OF THE MONOCYTE DIFFERENTIATION ANTIGEN OKM1." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643851.

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A family of related glycoproteins (GP) mediate the interaction between the circulating adhesive proteins and a variety of cells (cytyoadhesins). In this study we have compared two cell-surface antigens which share the property to bind fibrinogen: the platelet GP IIb/IIIa, prototype of the cytoadhesins, and the receptor for fibrinogen costitutively synthesized by monocytes. Two anti-GP IIb/IIIa monoclonal antibodies (Mabs) (LJP9, LJP5), recognizing functionally distinct epitopes of the GP IIb/IIIa did not react with monocytes nor inhibited 125I-fibrinogen binding to monocytes. Similarly, an Arg-Gly-Asp containing peptide which completely abolished platelet-fibrinogen interaction, had no effect on monocytes. Structurally, the monocyte fibrinogen receptor was dimeric and composed of two subunits with molecular weight (Mr) of 155,000 and 95,000. This structural organization was different from that of the GP IIb/IIIa (Mr= 116,000), but in close analogy with the family of leukocyte differentiation antigens OKM1, LFA-1. Therefore, this possible relationship was investigated. A Mab to OKM1 antigen (10 μg/ml) completely suppressed fibrinogen binding to monocytes while it was ineffective on plateles. Iodinated monocyte lysate subjected to immunoprecipitation with OKM1 Mab (60 μg/ml) showed a dimeric antigen with the same molecular size of the monocyte fibrinogen receptor. Moreover, preclearing of the monocyte lysate with OKM1 Mab removed the immunoprecipitate corresponding to the monocyte fibrinogen receptor. These data indicate that the immunologic differentiation antigen OKM1, in addition to function as a complement receptor, displays also the novel biological adhesion property to mediate the binding of fibrinogen to monocytes.
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Vigh, Zs, and I. Scharrer. "INVESTIGATIONS ON MULTIMERIC STRUCTURE OF PLATELET VON WILLE-BRAND FACTOR IN PATIENTS WITH HEREDITARY DISORDERS OF PLATELET FUNCTION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644087.

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Von Willebrand factor (vWF), a multimeric glycoprotein, plays an essential and multifunctional role in the hemostatic process. It is well known that platelet glycoproteins IB, IIB and IIIA contain receptors for vWF. Von Willebrand factor was also found in alpha granules of platelets. Therefore we investigated the multimeric structure of platelet vWF in 12 patients with different inherited disorders of platelet function. The patients had the following diagnosis: Hermansky Pudlak syndrome, Thrombasthenia and up to new undefined hereditary disorders of platelet function. The method is based upon:1) washing of platelets 2) release of platelet vWF 3) separation of vWF multimers by SDS-agarose electrophoresis 4) subsequent blotting of vWF mul timers onto nitrocellulose 5) staining by peroxidase conjugated antibodies.The investigations were repeated 3 times and compared to those of normal platelets. In 2 patients with Hermansky-Pudlak syndrane no multimeric structure could be detected in platelets whereas the multimeric pattern of plasma of these patients was normal. Also in one patient with the tentative diagnosis: thrombasthenia we couldn't find any multimeric structure in platelets compared to the normal multimeric composition of plasma. In 2 patients with giant platelets the multimeric distribution was normal. In the remaining 6 patients we observed multimeric structure which was different from that seen in vWd variants and in healthy volunteers. In 1 patient we found normal multimeric pattern in plasma and platelets.Based on our findings it can be assumed that the analysis of multimeric structure of platelet vWF can be helpful for the diagnostic approach and for the insight in pathogenesis of inherited disorders of platelet function.
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Reports on the topic "Glycoproteins Receptors"

1

Fusco, Deborah L. The Role of the Hendra Virus and Nipah Virus Attachment Glycoproteins in Receptor Binding and Antibody Neutralization. Fort Belvoir, VA: Defense Technical Information Center, January 2014. http://dx.doi.org/10.21236/ad1012829.

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Lu, Jinhua. The Role of the MHV Receptor and Related Glycoproteins in Murine Hepatitis Virus Infection of Murine Cell Lines. Fort Belvoir, VA: Defense Technical Information Center, March 1995. http://dx.doi.org/10.21236/ad1011449.

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3

Yaron, Zvi, Martin P. Schreibman, Abigail Elizur, and Yonathan Zohar. Advancing Puberty in the Black Carp (Mylopharyngodon Piceus) and the Striped Bass (Morone Saxatilis). United States Department of Agriculture, August 1993. http://dx.doi.org/10.32747/1993.7568102.bard.

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The black carp (bc)GtH IIb cDNA was amplified and isolated, cloned and sequenced. Comparison of the bcGtH IIb deduced a.a. sequence with that of GtH IIb from other teleosts revealed high homology to cyprinid species and a lower homology to salmonid or perciform fish. The gene coding for the GtH IIb was isolated and sequenced. Three bc recombinant phages which hybridized to the goldfish GtH Ib cDNA probe were isolated and are currently being characterized. The region coding for the mature GtH IIb was expressed in a bacterial expression vector resulting in the production of a recombinant protein. In vitro folding resulted in a protein only 1.3% of which displaced the native common carp GtH II in a RIA. Therefore, the common carp GtH RIA was utilized for the physiological studies at the current phase of the project. Two non-functional sites were identified along the brain-pituitary gonadal axis in the immature black carp. The pituitary is refractory to GnRH stimulation due to a block proximal to the activation of PKA and PKC probably at the level of GnRH receptors. The gonads, although capable of producing steroids, are refractory to gonadotropic stimulation but do respond to cAMP antagonists, indicating a block at the GtH receptor level. Attempts to advance puberty in 2 and 3 y old black carp showed that testosterone (T) stimulates GtH synthesis in the pituitary and increases its sensitivity to GnRh. A 2 month treatment combining T+GnRH increased the circulating GFtH level in 3 y old fish. Addition of domperidone to such a treatment facilitated both the accumulation of GtH in the pituitary and its response to GnRH. The cDNA of striped bass GtH a, Ib and IIb subunits were amplified, isolated, cloned and sequenced, and their deduced a.a. sequences were compared with those of other teleosts. A ribonuclease protection assay was developed for a sensitive and simultaneous determination of all GtH subunits, and of b-actin mRNAs of the striped bass. GnRH stimulated dramatically the expression of the a and GtH IIb subunits but the level of GtH Ib mRNA increased only moderately. These findings suggest that GtH-II, considered in salmonids to be involved only in final stages of gametogenesis, can be induced by GnRH to a higher extent than GtH-I in juvenile striped bass. The native GtH II of the striped bass was isolated and purified, and an ELISA for its determination was developed. The production of all recombinant striped bass GtH subunits is in progress using the insect cell (Sf9) culture and the BAC-TO-BAC baculovirus expression system. A recombinant GtH IIb subunit has been produced already, and its similarity to the native subunit was confirmed. The yield of the recombinant glycoprotein can reach 3.5 mg/ml after 3 days culture. All male striped bass reach puberty after 3 y. However, precocious puberty was discovered in 1 and 2 y old males. Females become vitellogenic during their 4th year. In immature 2 y old females, T treatment elevates the pituitary GtH II content while GnRH only potentiates the effect. However, in males GnRH and not T affects GtH accumulation in the pituitary. Neither GnRH, nor T treatment resulted in gonadal growth in 2 y old striped bass, indicating that either the accumulated GtH II was not released, or if released, the gonads were refractory to GtH stimulation, similar to the situation in the immature black carp. In 3 y old female striped bass, 150 day GnRHa treatment resulted in an increase in GSI, while T treatment, with or without GnRHa, resulted in a decrease in oocyte diameter, similar to the effect seen in the black carp. Further attempts to advance puberty in both fish species should take into account the positive effect of T on pituitary GtH and its negative effect of ovarian growth.
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