Academic literature on the topic 'Cell receptors'
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Journal articles on the topic "Cell receptors"
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Tibrewal, Richa, Reynoldly Kharsyntiew, Farida Dawood, and Archana Sharma. "A REVIEW ON G-PROTEIN COUPLED RECEPTOR." International Journal of Current Pharmaceutical Review and Research 13, no. 04 (2021): 01–09. https://doi.org/10.5281/zenodo.12664417.
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AbstractG protein–coupled receptors (GPCRs), also known as seven-(pass)-transmembrane domainreceptors, 7TM receptors, heptahelical receptors, serpentine receptor, and G protein–linkedreceptors (GPLR), constitute a large protein family of receptors that detect molecules outsidethe cell and activate internal signal transduction pathways and, ultimately, cellular responses.Coupling with G proteins, they are called seven-transmembrane receptors because they passthrough the cell membrane seven times. G protein–coupled receptors are found only ineukaryotes, including yeast, choanoflagellates, and animals. The ligands that bind andactivate these receptors include light-sensitive compounds, odors, pheromones, hormones,and neurotransmitters, and vary in size from small molecules to peptides to large proteins. Gprotein–coupled receptors are involved in many diseases and are also the target ofapproximately 34% of all modern medicinal drugs
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Steverding, Dietmar. "Cycle Numbers of Cell Surface Recycling Receptors." Receptors 2, no. 2 (2023): 160–65. http://dx.doi.org/10.3390/receptors2020010.
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The cycle number (nc) of a recycling receptor is defined as the average number of round trips (cell surface–endosome–cell surface) the receptor can make before it is degraded. This characteristic parameter of recycling receptors can be easily determined from the receptor’s half-life (t½, the time in which 50% of the receptor is degraded) and cycling time (Tc, the time a receptor needs to complete a round trip). Relationship analyses revealed that nc increases linearly with increasing t½ and decreases exponentially with increasing Tc. For commonly observed t½ and Tc values, it was calculated that recycling receptors have nc values of <300. In addition, it was found that recycling receptors in cancer cells have generally smaller nc values (<100), whereas recycling receptors in normal cells have larger nc values (>100). Based on this latter finding, the cycle number nc may be a useful criterion for distinguishing between cancer and normal cells.
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Gao, Yin, Xue Luan, Jacob Melamed, and Inka Brockhausen. "Role of Glycans on Key Cell Surface Receptors That Regulate Cell Proliferation and Cell Death." Cells 10, no. 5 (2021): 1252. http://dx.doi.org/10.3390/cells10051252.
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Cells undergo proliferation and apoptosis, migration and differentiation via a number of cell surface receptors, most of which are heavily glycosylated. This review discusses receptor glycosylation and the known roles of glycans on the functions of receptors expressed in diverse cell types. We included growth factor receptors that have an intracellular tyrosine kinase domain, growth factor receptors that have a serine/threonine kinase domain, and cell-death-inducing receptors. N- and O-glycans have a wide range of functions including roles in receptor conformation, ligand binding, oligomerization, and activation of signaling cascades. A better understanding of these functions will enable control of cell survival and cell death in diseases such as cancer and in immune responses.
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Thermos, K., M. D. Meglasson, J. Nelson, K. M. Lounsbury, and T. Reisine. "Pancreatic beta-cell somatostatin receptors." American Journal of Physiology-Endocrinology and Metabolism 259, no. 2 (1990): E216—E224. http://dx.doi.org/10.1152/ajpendo.1990.259.2.e216.
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The characteristics of somatostatin (SRIF) receptors in rat pancreatic beta-cells were investigated using rat islets and the beta-cell line HIT-T15 (HIT). The biochemical properties of the SRIF receptors were examined with 125I-labeled des-Ala-1,Gly-2-desamino-Cys-3-[Tyr-11]- dicarba3,14-somatostatin (CGP 23996). 125I-CGP 23996 bound to SRIF receptors in HIT cells with high affinity and in a saturable manner. The binding of 125I-CGP 23996 to SRIF receptors was blocked by SRIF analogues with a rank order of potency of somatostatin 28 (SRIF-28) greater than D-Trp-8-somatostatin greater than somatostatin 14 (SRIF-14). To investigate the physical properties of the HIT cell SRIF receptor, the receptor was covalently labeled with 125I-CGP 23996 using photo-cross-linking techniques. 125I-CGP 23996 specifically labeled a protein of 55 kDa in HIT cell membranes. The size of the SRIF receptor in HIT cells is similar to the size of the SRIF receptor labeled with 125I-CGP 23996 in membranes of freshly isolated islets, suggesting that the physical properties of SRIF receptors in HIT cells and rat islet cells are similar. The binding studies suggest that beta-cells predominantly express a SRIF-28-preferring receptor. In freshly isolated islets, glucose- and arginine-stimulated insulin release was effectively blocked by SRIF-28 but not by SRIF-14. SRIF-14 did inhibit arginine-stimulated glucagon secretion from freshly isolated islets. The dissociation of the inhibitory effects of SRIF-28 and SRIF-14 on insulin and glucagon release from freshly isolated islets suggests that the two peptides act through different receptors in islets to regulate hormone secretion.
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Gao, Zihan. "The structure and function of cell membrane receptor." Highlights in Science, Engineering and Technology 74 (December 29, 2023): 441–47. http://dx.doi.org/10.54097/bncesw47.
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Cell membrane receptors play a key role in regulating cell communication and maintaining cell homeostasis. This paper explores the complex relationship between the structure and function of cell membrane receptors, and elucidates their multiple roles in signal transduction, cellular response, and disease pathways. Different receptor types, including as G protein-coupled receptors (GPCRs), ligand-gated ion channels, receptor tyrosine kinases (RTKs), and cytokine receptors, have varied structural properties that serve different biological purposes and are necessary for cell division, proliferation, and metabolism. The function of membrane receptors that translate extracellular signals into intracellular responses is diverse. The organization of lipid rafts and other receptors within membrane microdomains can influence signal transduction efficiency and specificity. There are inseparable interactions among receptor internalization, recycling and degradation, and regulating the duration and intensity of receptor signaling is closely related to the treatment of diseases. In summary, the current research status of cell membrane receptor structure and function is reviewed in this paper. It contributes to a broader understanding of how receptors regulate important cellular processes at the molecular level. Understanding the nuances of receptor structure-function relationships holds great promise for developing new therapeutic strategies and advancing drug discovery for a variety of diseases.
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Atif, Muhmmad, Abdullah Alsrhani, Farrah Naz, et al. "Targeting Adenosine Receptors in Neurological Diseases." Cellular Reprogramming 23, no. 2 (2021): 57–72. http://dx.doi.org/10.1089/cell.2020.0087.
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Uings, I. J. "Cell receptors and cell signalling." Molecular Pathology 53, no. 6 (2000): 295–99. http://dx.doi.org/10.1136/mp.53.6.295.
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Desforges, Jane F. "T-Cell Receptors." New England Journal of Medicine 313, no. 9 (1985): 576–77. http://dx.doi.org/10.1056/nejm198508293130909.
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Abbas, Atheir, and Bryan L. Roth. "Electrifying cell receptors." Nature Nanotechnology 3, no. 10 (2008): 587–88. http://dx.doi.org/10.1038/nnano.2008.292.
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Deller, M. "Cell surface receptors." Current Opinion in Structural Biology 10, no. 2 (2000): 213–19. http://dx.doi.org/10.1016/s0959-440x(00)00072-5.
Full textDissertations / Theses on the topic "Cell receptors"
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Ferletta, Maria. "The Laminins and their Receptors." Doctoral thesis, Uppsala University, Department of Cell and Molecular Biology, 2002. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-1771.
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<p>Basement membranes are thin extracellular sheets that surround muscle, fat and peripheral nerve cells and underlay epithelial and endothelial cells. Laminins are one of the main protein families of these matrices. Integrins and dystroglycan are receptors for laminins, connecting cells to basement membranes. Each laminin consists of three different chains, (α, β, γ). Laminin-1 (α1β1γ1) was the first laminin to be found and is the most frequently studied. Despite this, it was unclear where its α1 chain was expressed. A restricted distribution of the α1 chain in the adult epithelial basement membranes was demonstrated in the present study. In contrast, dystroglycan was found to have a much broader distribution. Dystroglycan is an important receptor for α2-laminins in muscle, but binds also α1-laminins. The more ubiquitous α5-laminins were also shown to bind dystroglycan, but with distinctly lower affinity than α1- and α2- laminins. </p><p>The biological roles of different laminin isoforms have been investigated. Differences were found in the capacity of various tested laminins to promote epithelial cell adhesion. The α5-laminins were potent adhesive substrates, a property shown to be dependent on α3 and α6 integrins. Each receptor alone could promote efficient epithelial cell adhesion to α5-laminins. Yet, only α6 integrin and in particular the α6A cytoplasmic splice variant could be linked to laminin-mediated activation of a mitogen-activated protein kinase (MAP kinase) pathway. Attachment to either α1- or α5-laminins activated extracellular-signal regulated kinase (ERK) in cells expressing the integrin α6A variant, but not in cells expressing α6B. A new role for dystroglycan as a suppressor of this activation was demonstrated. Dystroglycan antibodies, or recombinant fragments with high affinity for dystroglycan, decreased ERK activation induced by integrin α6 antibodies. Integrin αvβ3 was identified as a novel co-receptor for α5-laminin trimers. Cell attachment to α5-laminins was found to facilitate growth factor induced cell proliferation. This proliferation could be blocked by antibodies against integrin αvβ3 or by an inhibitor of the MEK/ERK pathway. Therefore, integrin αvβ3 binding to α5-laminins could be of biological significance.</p>
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Eckl-Dorna, J. "How B cell receptors and Toll-like receptors collaborate in shaping B cell responses." Thesis, University College London (University of London), 2009. http://discovery.ucl.ac.uk/18762/.
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Antigen recognition by B cells results in their activation followed by specific antibody production. These events are initiated by antigen binding to their surface B cell receptors (BCR) which triggers both signalling and internalization of the receptor bound antigen to the endosome. However B cells also express features of the innate immune system such as Toll like receptors (TLRs), that can be located either on the surface of the cell or intracellularly where they recognize bacterial and viral nucleic acids. Engagement of these receptors within B cells is associated with enhancement of humoral responses. The aim of my PhD project was to investigate how endosomal TLR ligands in a particulate form could gain access to their intracellular receptors in the B cell and which impact the subsequent TLR engagement had on B cell fate. To achieve this, I directly linked both antigen and TLR9 ligand to particulates. Immunisation of mice with those particulates resulted in enhanced specific antibody titers compared to stimulation with particulate antigen alone. To dissect the underlying mechanism, I employed transgenic B cells bearing BCR specificity for the same antigen and stimulated them with particulate antigen-TLR9 ligand conjugates. Particulate TLR9 ligand could not gain access to its receptor within B cells via unspecific macropinocytosis and instead depended on BCRmediated internalization. Subsequent engagement of intracellular TLR9 by its ligand present in the conjugates resulted in B cell activation and proliferation, followed by differentiation into plasma cells and antigen specific antibody secretion. The uptake of the antigen-TLR9 ligand particulates both in vitro and in vivo depended on the affinity of the antigen once a defined threshold required for internalization was surpassed. The extent of plasma cell differentiation however could be modulated by the amount of TLR9 ligand present on the particulates. Thus I observed that direct linking of antigen and TLR ligand resulted in PC differentiation through antigen specific BCR mediated internalization and subsequent TLR engagement. This reveals a mechanism that may operate during the initiation of a primary immune response.
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Betson, Martha Elizabeth. "Regulation of cell-cell adhesion in keratinocyes." Thesis, University College London (University of London), 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.274930.
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Jorgenson, Rebecca L. "The innate immune response and toll-like receptors in the human endometrium." Diss., Columbia, Mo. : University of Missouri-Columbia, 2005. http://hdl.handle.net/10355/4178.
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Thesis (Ph. D.)--University of Missouri-Columbia, 2005.<br>The entire dissertation/thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file (which also appears in the research.pdf); a non-technical general description, or public abstract, appears in the public.pdf file. Vita. "December 2005" Includes bibliographical references.
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Jiang, Ning. "Kinetic analysis of Fcγ receptor and T cell receptor interacting with respective ligands". Diss., Georgia Institute of Technology, 2005. http://hdl.handle.net/1853/26716.
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Low affinity Fcg receptor III (FcgRIII, CD16) triggers a variety of cellular events upon binding to the Fc portion of IgG. A real-time flow cytometry method was developed to measure the affinity and kinetics of such low affinity receptor/ligand interactions, which was shown as an easily operated yet powerful tool. Results revealed an unusual temperature dependence of reverse rate of CD16aTM dissociating from IgG. Except for a few studies using mammalian cell CD16s, most kinetics analyses use purified aglycosylated extracellular portion of the molecules, making it impossible to assess the importance of the receptor anchor and glycosylation on ligand binding. We used a micropipette adhesion frequency assay to demonstrate that the anchor length affects the forward rate and affinity of CD16s for IgG in a species specific manner, most likely through conformational changes. Receptor glycosylation dramatically reduced ligand binding by 100 folds. T cell receptor (TCR) is arguably the most important receptor in the adaptive human immune system. Together with coreceptor CD4 or CD8, TCR can discriminate different antigen peptides complexed with major histocompatibility complex (MHC) molecule (pMHC), which differ by as few as only one amino acid, and trigger different T cell responses. When T cell signaling was suppressed, TCR had similar affinity and kinetics for agonist and antagonist pMHC whose binding to CD8 was undetectable. TCR on activated T cell had a higher affinity for pMHCs, suggesting that TCRs organize themselves differently on activated T cells than on naïve T cells. In the absence of inhibitors for signaling, TCR binds agonist pMHC with several orders of magnitude higher affinity than antagonist pMHC. In addition, engagement of TCR by pMHC signals an upregulation of CD8 binding to pMHC, which is much stronger than the TCR-pMHC binding. The transition from weak TCR binding to the strong CD8 binding takes place around 0.75 second after TCR in contact with pMHC and can be reduced by several inhibitors of tyrosine and lipid phosphorylation, membrane rafts, and actin cytoskeleton. These results provide new insights to understanding T cell discrimination.
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Im, Jin Seon. "Molecular characterization of T cell receptors and non-MHC restricted T cell receptor binding peptides." Diss., The University of Arizona, 1999. http://hdl.handle.net/10150/284969.
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T cells recognize antigenic peptides presented by MHC molecules on antigen presenting cells (APC) through T cell receptors (TCRs). Since TCRs are very similar to antibodies in structure and genetics, TCRs might have the potential to bind free antigens as antibodies do. Here, peptides which bound TCRs irrespective of MHC molecules have been identified by screening "one-bead one-peptide" combinatorial libraries. Peptides: VRENAR, RTGNYV, GKMHFK, KDAVKR and RKPQAI bound recombinant Jurkat single chain T cell receptors (scTcrs). GKMHFK, KDAVKR and RKPQAI were also specific for natural TCRs on the Jurkat cell surface. Molecular modeling implies that Glu96 in the CDR3 loop of TCR alpha chain is a candidate for the peptide interaction site. However, TCR-binding peptides did not induce biological effects on parental Jurkat cells. To extend this study to a biologically relevant system, diabetogenic T cells involved in insulin-dependent diabetes mellitus (IDDM) have been characterized. GAD(524-543) responding T cells showed restricted TCR variable gene usage, which utilized preferentially Vα17 and Vβ12. Three domain single chain T cell receptors (3D scTcr) were constructed as tools to investigate potential therapies for IDDM and to identify peptides which bind to TCR without association of MHC molecules. Functional analysis has demonstrated that GAD(524-543)-specific scTcrs retained the ability to bind GAD(524-543)/IAg7 complex. This work shows that recombinant scTcrs can bind cognate peptide presented by MHC molecules, therefore they can be used as substitutes for natural TCRs in screening "one-bead one-peptide" combinatorial libraries to identify TCR-binding peptide.
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Ihenetu, Kenneth. "Characterisation of cannabinoid receptors on immune cells and cell lines." Thesis, University of Hertfordshire, 2003. http://hdl.handle.net/2299/14124.
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Cannabinoids may inhibit immune cell function by modulating cytokine/chemokine release but the receptors mediating these events are poorly characterised. The aim of this thesis is to characterise cannabinoid receptors mediating cytokine/chemokine release from immune and inflammatory cells by measuring the effects of cannabinoids on cytokine release using ELISA technique. Apoptosis of inflammatory cells was also assessed by visual evaluation of cells treated with cannabinoids using a nuclear fluorochrome 4'6-diamidino-2 phenyl indole dihydrochloride (DAPI). Non-selective cannabinoid receptor agonists CP55,940 (10-6 -10-4 M- 10 'S M), A? - THC (10 -10 M) and anandamide (10 M- 10-4 M) inhibited LPS-induced release of TNF-a from THP-1 cells, a monocytic cell line. The cannabinoid CB2 receptor antagonist SR144528 (10 -6 M) but not the cannabinoid CB1 receptor antagonist SR141716A (10 -6 M) antagonised the inhibitory effects of CP55,940 (pA2 = 6.1 t 0.1, n=6) on THP-1 cells. Similarly, CP55,940 (10-6-104 M -10 'S M), 09-THC (10 10 M -10 -S M) and anandamide (10 -6 M -10'4 M) inhibited PHA/PMA-induced IL-2 release from Jurkat cells, a lymphocytic cell line. However in contrast to THP-1 cells, neither SR141716A (10 -6 M) nor SR144528 (10 -6 M) antagonised the inhibitory effects of CP55,940 on this cell line. In peripheral blood mononuclear cells a nonselective cannabinoid receptor agonist WIN55212-2 (10'10 M-10'5 M) and a selective cannabinoid CB2 receptor agonist JWH 015 (10 -10 M- 10 -S M) inhibited PHAinduced release of IL-2. These effects were antagonised by SR144528 (10-6 M) (pA2 = 6.3 ± 0.1; 6.5 ± 0.1, n=5 respectively) but not by SR141716A (10 -6 M). CP55,940 (10 -10 M -10 -5 M) produced a small, non-significant (P> 0.05) inhibitory effect on IL-2 release. 09-THC (10 -10 M-10-6 M) and ACEA (10 -'0 M- 10 -6 M) had no significant inhibitory effect on the release of IL-2 from PBMC. CP55,940 (10 M) and A9- THC (10 M) antagonised the inhibitory effects of WIN55212-2 (pA2 = 6.1 ± 0.1; 6.96 ± 0.16, n=5 respectively). In HT-29 cells, CP55,940 (10"10 -10"5 M- 10 M), A9-THC (10 -10 M -10 -5 M), WIN55212-2 (10"10 M-10-5 M) and JWH 015 (10 -10 M- 10 -5 M) inhibited IL-8 release. SR141716A (10 -6 M) antagonised the inhibitory effects of CP55,940 (pA2 = 8.3 ± 0.2 n=6) but did not antagonise the effects of WIN55212-2 and JWH 015. SR144528 (10 -6 M) but not SR141716A (10 -6 M) antagonised the inhibitory effects of CP55,940 (pA2 = 8.2 ± 0.8, n=6), WIN55212-2 (pA2 = 7.1± 0.3, n=6), JWH 015 (pA2 = 7.6 ± 0.4, n=6) respectively. A protein the size of cannabinoid CB2 receptors was localised in this cell line by Western blotting. CP55,940 and WIN55212-2 inhibited basal and agonist-evoked increases in both intracellular cyclic AMP and intracellular calcium at the same concentration as that inhibiting TNF-a-induced release of IL-8. Furthermore anandamide (>1 μM) but not CP55,940 caused apoptosis in Jurkat and HT-29 cell. These data suggest that activation of cannabinoid CB2 receptors in THP-1 cells, PBMC and HT-29 cells could lead to inhibition of cytokine/chemokine release. Furthermore,c annabinoid-evokedin hibition of basal and agonist stimulated increases in HT-29 cells may be related to cannabinoid-evokedin hibition of IL-8 release. Thus data presented in this thesis suggest that cannabinoid CB2 receptor agonists with high efficacy may have potential clinical utility in the treatment of inflammatory conditions such as inflammatory bowel disease (IBD) or chronic obstructive pulmonary disease (COPD) and other inflammatory disorders where epithelial cells have a major role.
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Campbell, M.-A. "Functional receptors on B-cell membranes." Thesis, Open University, 1988. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.383704.
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Paramasivam, Anbalakan. "Regulation of immune cell P2X receptors." Thesis, University of Cambridge, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.612427.
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Hannan, S. B. "Cell surface mobility of GABAB receptors." Thesis, University College London (University of London), 2011. http://discovery.ucl.ac.uk/1335825/.
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Type-B γ-aminobutyric acid receptors (GABABRs) are important for mediating slow inhibition in the central nervous system and the kinetics of their internalisation and lateral mobility will be a major determinant of their signalling efficacy. Functional GABABRs require R1 and R2 subunit co-assembly, but how heterodimerisation affects the trafficking kinetics of GABABRs is unknown. Here, an α-bungarotoxin binding site (BBS) was inserted into the N-terminus of R2 to monitor receptor mobility in live cells. GABABRs are internalised via clathrin- and dynamin-dependent pathways and recruited to endosomes. By mutating the BBS, a new technique was developed to differentially track R1a and R2 simultaneously, revealing the subunits internalise as heteromers and that R2 dominantly-affects constitutive internalisation of GABABRs. Notably, the internalisation profile of R1aR2 heteromers, but not R1a homomers devoid of their ER retention motif (R1ASA), is similar to R2 homomers in heterologous systems. The internalisation of R1aASA was slowed to that of R2 by mutating a di-leucine motif in the R1 C-terminus, indicating a new role for heterodimerisation, whereby R2 subunits slow the internalization of surface GABABRs. R1a and R1b are the predominant GABABR1 isoforms in the brain, differing by the two Sushi Domains (SDs) in R1a. Introduction of a BBS into the N-terminus of R1b and comparison with R1a revealed that R1bR2 internalises faster than R1aR2. Introduction of the SDs into the BBS-tagged metabotropic glutamate receptor-2 also conferred a decrease in internalisation. Finally, the lateral surface mobility of GABABRs was studied by extending the BBS-tagging method to single-particle tracking using quantum dots. R1aR2 and R1bR2 exhibited different mobility profiles on hippocampal neurons and differentially responded to baclofen. In conclusion, this study provides new and important insight into the mobility of cell surface GABABRs and the underlying mechanisms that ensure they provide efficacious slow synaptic inhibition.
Books on the topic "Cell receptors"
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Seifert, G., ed. Cell Receptors. Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-75515-6.
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I, Bell John, Owen M. J, and Simpson Elizabeth Dr, eds. T cell receptors. Oxford University Press, 1995.
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Mak, Tak W., ed. The T-Cell Receptors. Springer US, 1988. http://dx.doi.org/10.1007/978-1-4684-5406-2.
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1941-, Greenberg Arnold H., ed. Invertebrate models: Cell receptors and cell communication. Karger, 1987.
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K, Harrison Jeffrey, and Lukacs Nicholas W, eds. The chemokine receptors. Humana, 2007.
Find full textBook chapters on the topic "Cell receptors"
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Law, S. K. Alex. "Complement Receptors." In Blood Cell Biochemistry. Springer US, 1993. http://dx.doi.org/10.1007/978-1-4757-9534-9_9.
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Kaur, Prabhjot. "B-Cell Receptors." In Molecular and Translational Medicine. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-70603-0_3.
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Marrack, P., A. M. Pullen, A. Herman, et al. "T Cell Receptors." In Progress in Immunology. Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-83755-5_1.
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Dillon, Joseph S., Ming Lu, Michael B. Wheeler, and Aubrey E. Boyd. "β-Cell Receptors." In Molecular Biology of Diabetes. Humana Press, 1994. http://dx.doi.org/10.1007/978-1-4612-0241-7_12.
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Jevtovic-Todorovic, Vesna. "Neurotransmitters and Receptors." In Neural Cell Biology. CRC Press, 2017. http://dx.doi.org/10.1201/9781315370491-14.
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Mennes, A. M., A. Maan, and M. A. Hall. "Plant Hormone Receptors." In Cell to Cell Signals in Plants and Animals. Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-76470-7_20.
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Yoneyama, Hiroyuki, Kenjiro Matsuno, and Kouji Matsushima. "Chemokine Receptors and Dendritic Cell Trafficking." In The Receptors. Humana Press, 2007. http://dx.doi.org/10.1007/978-1-59745-020-1_6.
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Ferrell, James E. "Receptors 1." In Systems Biology of Cell Signaling. Garland Science, 2021. http://dx.doi.org/10.1201/9781003124269-2.
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Ferrell, James E. "Receptors 2." In Systems Biology of Cell Signaling. Garland Science, 2021. http://dx.doi.org/10.1201/9781003124269-3.
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Smith, C. A., and E. J. Wood. "Nerves, neurotransmitters and their receptors." In Cell Biology. Springer US, 1996. http://dx.doi.org/10.1007/978-1-4613-0441-8_12.
Full textConference papers on the topic "Cell receptors"
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Watson, Andrew B. "Constraints on sensitivity of linear visual neurons." In OSA Annual Meeting. Optica Publishing Group, 1988. http://dx.doi.org/10.1364/oam.1988.tuh4.
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Many visual neurons linearly combine signals from the receptors or from other cells which themselves form linear combinations of receptor signals. In both cases, if the noise that limits cell performance is confined to the receptors, the peak sensitivity of the cell is entirely determined by the magnitude of the receptor noise and the normalized shape of the cells’ receptive field. This simple result may be used to estimate the receptor noise from the sensitivity of retinal or geniculate cells as well as to predict sensitivity of higher-order cells from that of lower-order cells. Consequences of this constraint are illustrated for actual primate geniculate and cortical cells and for model cortical cells.
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Karnik, Rohit, Seungpyo Hong, Suman Bose, et al. "Microfluidic Separation of Cells by Rolling on Patterned Receptors." In ASME 2008 6th International Conference on Nanochannels, Microchannels, and Minichannels. ASMEDC, 2008. http://dx.doi.org/10.1115/icnmm2008-62217.
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Cell separation based on markers present on the cell surface has extensive biological applications. However, current separation methods involve labeling and label removal steps which are often slow and intrusive. We envisioned that the ability to control the direction of transport of cells based on specific receptors on the cell surface without labeling and label removal steps would enable simple continuous-flow microfluidic cell separation systems with minimal processing steps and active components. We therefore explored whether receptor patterning could be used to direct the transport of cells in a label-free manner through the formation of transient receptor-ligand bonds that result in cell rolling.
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Chesla, Scott E., Bryan T. Marshall, and Cheng Zhu. "Measuring the Probability of Receptor Extraction From the Cell Membrane." In ASME 1997 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 1997. http://dx.doi.org/10.1115/imece1997-0262.
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Abstract Recently, there has been an increasing interest in measuring the interaction forces between cell adhesion receptors and their ligands [1–3]. These molecules are either anchored on the membrane of a cell or coated on the surface of a substratum. The two surfaces are joined together as a result of the formation of non-covalent bonds between the receptors and ligands. The forces are measured when the two surfaces are separated. In a theoretical paper published nineteen years ago, George Bell estimated the force required to break a receptor-ligand bond and that required to uproot the receptor from the cell membrane to be of the same order of magnitude [4]. The interpretation of the force data therefore requires the knowledge of detachment mode, i.e., via adhesive mechanism if the receptor-ligand bond is dissociated or via cohesive mechanism if the receptor-membrane anchor is disrupted.
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Zheng, Xiangjun, Siu Lun Cheung, Lian Wang, et al. "Specific Binding of Cancer Cells Using a Microchamber Array Functionalized With Antibodies." In ASME 2009 International Mechanical Engineering Congress and Exposition. ASMEDC, 2009. http://dx.doi.org/10.1115/imece2009-13217.
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Specific binding of target suspended metastatic cancer cells to an antibody-functionalized surface utilizing a microfluidic device has experimentally been investigated under various conditions. The microfluidic devices, fabricated in silicon using DRIE process, consisted of a 5×5 micochamber array; each 1mm×1mm in area, and 50μm in depth. The oxide surface of the microchammber array was functionalized with various antibodies immobilized on a protein G layer. The microfluidic device design allows accurate counting of cells loaded into each microchamber and, thus, enabling a reliable counting of cells captured from homogeneous suspensions. The effects of cell suspension concentration, incubation times and ambient temperature on cell capture efficiency have been examined. Furthermore, to evaluate the specificity of the cell-surface interaction, several cell cancer types expressing different membrane receptors have been incubated on surfaces functionalized with various counter receptors. Specific binding of up to 100% of the suspended cells is observed when using surfaces functionalized with counter receptors matching the cell receptors; otherwise, non-specific binding of less than 15% of suspended cells is obtained if the functionalized counter receptors do not match the cell receptors.
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Brill, Michael H., Doreen W. Bergeron, and William W. Stoner. "Trichromatic retinal model with adaptive contrast sensitivity and resolution." In OSA Annual Meeting. Optica Publishing Group, 1987. http://dx.doi.org/10.1364/oam.1987.thc4.
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A computer-simulated retina called IRIS is described which discriminates small differences in reflected light when these differences occur in a restricted domain of space and time and maintains sensitivity to these differences for a wide range of light environments. As prevailing light levels de crease and photon noise becomes significant, IRIS automatically reduces its spatiotemporal resolution to provide greater redundancy. The temporal resolution depends on light intensity because each receptor’s response is governed by photopigment kinetics whose rate increases with light level. The spatial resolution depends on light intensity because the receptors are individual circuits (with voltage sources and photoconductors) coupled by a passive conducting grid. At high light intensity, the conductances within each receptor circuit are much greater than the lateral conductance, hence the receptor circuits are effectively uncoupled. Decreasing light intensity causes the lateral conductance to become more significant, thereby coupling the receptors and reducing spatial resolution. The simulation (implemented in FORTRAN) is adapted from the dissertation work of one of the authors.1 Simulation results are presented, and parallels to human vision are noted—including implications for trichromatic vision. The conducting grid might be achieved by tight-junction coupling of receptors and horizontal-cell interconnections that form an effective syncytium.
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Gupta, M., and G. J. Stewart. "INFLUENCE OF CELL CYCLING ON MAGNITUDE OF RESPONSE OF HUMAN UMBILICAL VEIN ENDOTHELIAL CELLS (EC) TO NOREPINEPHRINE (NE) AND HISTAMINE (H)." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644830.
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EC have several roles in preventing thrombosis. Efficiency with which EC fulfill these might well influence outcome of potentially thrombotic stimuli. Thus, factors that influence EC function are of interest. As a general measure of EC response to NE and H the level of cAMP was measured. EC were harvested and passaged by enzymatic digestion and grown in DMEM plus 10% fetal calf serum and antibiotics. cAMP was assayed by radioimmunoassay. Percentage cycling cells was determined by autoradiography of cultures pulse labeled with tritiated thymidine and was increased by hydroxyurea treatment.Basal cAMP was remarkably consistent (less than 10% difference) for cells isolated from different cords, studied after different number of passages, fresh or frozen and with varying percentage of cells cycling. However, magnitude of response to agonists was highly variable. Within the same cell lot between 5-8 passages, magnitude of response was directly proportional to percentage of cycling cells but magnitude ofresponse for different cell lots varied over several fold.EC response to NE was mediated through B-adrenergic receptors and that to H through H receptors. Variability might be caused by differences in receptor number or some intracellular process.
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Skierczynski, Boguslaw A. "Probability Density of the Rolling Velocity of the Cell." In ASME 1998 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 1998. http://dx.doi.org/10.1115/imece1998-0056.
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Abstract Rolling of the cell under flow conditions is an important process in PMN emigration. It is a finely regulated process involving membrane receptors and cell-matrix recognition. Several models have been proposed to explain how the strength and lifetime of the bonds in receptor-mediated cell-substratum are related to cell rolling velocity (Hammer, 1992, Tozeren, 1992, Zhao, 1995). The paper presents a simple model of the cell rolling based on the experimental measurements that will allow to gain information relevant to the molecular processes underlying the rolling motion of the cell.
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Marquerie, G., A. Duperray, G. Uzan, and R. Berthier. "BIOSYNTHETIC PATHWAYS OF THE PLATELET FIBRINOGEN RECEPTOR IN HUMAN MEGAKARYOCYTES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642954.
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Interaction between cells and between cells and extracellular matrices are critical for a number of biological processes, including organ development, cell differenciation, cell motility, and the inimune' response. These interactions are mediated by a family of adhesion receptors that recognize short sequences such as Arg-Gly-Asp (RGD). These receptors share similar structural properties. They are heterodimers composed of a and B subunits and sometime express common epitopes. This suggests that the structural and functional relationship of these receptors may result from the transcription of related genes or may arise from cell specific post-transcriptional events. Thus, analysis of the biosynthesis and processing of these receptors would provide valuable insights into the molecular mechanism which control their expression at the surface,of different cells. Platelet membrane glycoprotein (GP) IIb-IIIa is a member of this receptor family. This protein is a non covalent heterodimer composed of two distinct polypeptides, Glib which consists of two subunits Ilba and IlbB (Mr = 116 kD, Mr = 25 kD) and GPIIIa (Mr = 100 kD, reduced). GPIIb-IIIa functions at site of platelet aggregation and serves as receptor for RGD containing factors including fibrinogen, fibronectin and von Willebrand factor. We report here on the investigation of the biosynthetic pathways of this RGD receptor in human megakaryocytes. High number of megakaryocytic cells from the megakaryoblastic stage to the polyploid mature megakaryocyte were obtained from liquid culture of cryopreserved leukocyte stem cell concentrates from patients with chronic myelogenous leukemia (CML). After sorting, using a FACS IV and indirect immunofluores-cent labeling with monoclonal antibodies anti-GPIIb-IIIa, 95 % of the cells in culture were of the megakaryocytic lineage. These megakarocytes represented an excellent tool to delineate at the molecular level events associated with the biosynthesis of GPIIb-IIIa.Metabolic labeling and pulse-chase experiments indicated that GPIIb and GPIIIa are synthesized from separate mRNA and that the two subunits of GPIIb derive from a common precursor. This was further confirmed by cell-free translation of megakaryocyte mRNA and the identification of separate cDNA containing sequences coding for the pro-GPIIb and for GPIIIa. These cDNA were isolated from a Xgt11 expression library constructed with purified megakaryocyte RNA, and were used to size the messengers coding for the two polypeptides. A single mRNA species of 3.9 kB was found to encode the pro-GPIIb, whereas two different mRNA species of 2.9 kB and 4. 1 kB were identified with the GPIIIa cDNA.The newly synthesized GPIIIa associates early with the pro-GPIIb in the rough endoplasmic reticulum. Examination of the glycosylation pathways with endoglycosidase H, tunicamycin and monensin indicated that high mannose oligosaccharides are added to the GPIIIa and pro-GPIIb polypeptide backbone. The pro-GPIIb is then processed with conversion of high mannose to the complex type carbohydrate, whereas GPIIIa remains endoH sensitive. Glycosylation of pro-GPIIb-IIIa and processing of oligosaccharides are prerequisite for proteolytic maturation of pro-GPIIb and the expression of the mature complex at the surface of the cell. Thus post-translational processing of GPIIb-IIIa requires an early assembly of the complex. This may have important implications in the maturation of megakaryocyte granules and in the molecular mechanism underlying the Glanzmann thrombastenic disease.
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Milanović, Žiko, Marko Antonijević, Dušica Simijonović, Jelena Đorović Jovanović, and Marijana Stanojević Pirković. "Investigating the potential inhibitory effect of the megaphone (molecule) on nasopharyngeal cancer growth factor receptors." In 2nd International Conference on Chemo and Bioinformatics. Institute for Information Technologies, University of Kragujevac, 2023. http://dx.doi.org/10.46793/iccbi23.682m.
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Nasopharyngeal cancer (NPC) is a type of cancer that originates in the nasopharynx, which is the upper part of the throat behind the nasal cavity. Like other cancers, the growth and progression of nasopharyngeal cancer are influenced by various proteins involved in cell signaling, growth regulation, and tumor development such as Epidermal Growth Factor Receptor (EGFR), Vascular Endothelial Growth Factor (VEGF), Fibroblast growth factor receptor (FGFR) and Cyclin D1 (CD1). Megaphone ((1′R,5′R,7R,8S)-7-Hydroxy-3,4,5,5′-methoxy-5′,6′-dihydro-2′H-8,1′-neolign-8′-en-2′-one, MG) is the main component of the alcohol extract of the ground root of Aniba megaphylla, which in vitro inhibits the growth of cells derived from human nasopharyngeal carcinoma. Due to the lack of literature data, the main goal of this study was to examine the first step of the mechanisms of anti-carcinogenic activity by examining the inhibitory potential of MG against the above-mentioned cancer cell growth factor receptors.
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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.
Reports on the topic "Cell receptors"
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Cheepsunthorn, Poonlarp, and Yong Poovorawan. Identification of receptors for H5N1 virus on human nerve cells using protromics-based approaches. Chulalongkorn University, 2013. https://doi.org/10.58837/chula.res.2013.12.
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In this study, we investigated neuroinfectious capacity of H5N1 (A/Thailand/NK165/2005) isolated from plasma of infected individual during the third wave of Thailand outbreaks using human neuroblastoma SH-SY5Y cells. This was due to lack of information regarding neuroinfectivity of this variant. Results demonstrated that H5N1/NK165 induced servere CPEs in these neuronal cells. H5N1-specific hemagglutinin was found in the cytoplasm of the infected cells as early as 12 h post-infection. By 24 h post-infection, all cells in the cultures were infected. These findings coincided with time course of CPEs and the presence of virus progeny in the culture medium of infected cells. Virus titer increased exponentially overtime. After 24 h post-infection, viability of the infected cell began to decline. By 72 h, only cellular debris remained in the infected cultures. Moreover, with this isolate we identified host cell proteins that might be involved in H5N1 entry to nerve cells using 1D-VOPBA coupled with LC-MS/MS analysis. RACK1 and prohibitin were identified as potential receptor for H5N1. Expression of RACK1 and prohibitin was confirmed by western blot analysis. There was a significant decrease in Expression of RACK1 and prohibitin preteins compared with mock-infected cells, suggesting that both RACK1 and prohibitin might be involved in the initial step of H5N1 binding to the neuronal cell membrane and/or internalization. Further studies are needed to explore whether both RACK1 and prohibitin are actual receptors for H5N1. This will ultimatel lead to improved therapeutics and provide an insight into neuronal mechanism of H5N1 infection.
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Silver, Pamela A. The Identification of Novel Ligands for Cell Surface Receptors. Defense Technical Information Center, 2000. http://dx.doi.org/10.21236/ada392930.
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Silver, Pamela A. The Identification of Novel Ligands for Cell Surface Receptors. Defense Technical Information Center, 1999. http://dx.doi.org/10.21236/ada382512.
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Rafaeli, Ada, and Russell Jurenka. Molecular Characterization of PBAN G-protein Coupled Receptors in Moth Pest Species: Design of Antagonists. United States Department of Agriculture, 2012. http://dx.doi.org/10.32747/2012.7593390.bard.
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The proposed research was directed at determining the activation/binding domains and gene regulation of the PBAN-R’s thereby providing information for the design and screening of potential PBAN-R-blockers and to indicate possible ways of preventing the process from proceeding to its completion. Our specific aims included: (1) The identification of the PBAN-R binding domain by a combination of: (a) in silico modeling studies for identifying specific amino-acid side chains that are likely to be involved in binding PBAN with the receptor and; (b) bioassays to verify the modeling studies using mutant receptors, cell lines and pheromone glands (at tissue and organism levels) against selected, designed compounds to confirm if compounds are agonists or antagonists. (2) The elucidation ofthemolecular regulationmechanisms of PBAN-R by:(a) age-dependence of gene expression; (b) the effect of hormones and; (c) PBAN-R characterization in male hair-pencil complexes. Background to the topic Insects have several closely related G protein-coupled receptors (GPCRs) belonging to the pyrokinin/PBAN family, one with the ligand pheromone biosynthesis activating neuropeptide or pyrokinin-2 and another with diapause hormone or pyrokinin-1 as a ligand. We were unable to identify the diapause hormone receptor from Helicoverpa zea despite considerable effort. A third, related receptor is activated by a product of the capa gene, periviscerokinins. The pyrokinin/PBAN family of GPCRs and their ligands has been identified in various insects, such as Drosophila, several moth species, mosquitoes, Triboliumcastaneum, Apis mellifera, Nasoniavitripennis, and Acyrthosiphon pisum. Physiological functions of pyrokinin peptides include muscle contraction, whereas PBAN regulates pheromone production in moths plus other functions indicating the pleiotropic nature of these ligands. Based on the alignment of annotated genomic sequences, the primary and secondary structures of the pyrokinin/PBAN family of receptors have similarity with the corresponding structures of the capa or periviscerokinin receptors of insects and the neuromedin U receptors found in vertebrates. Major conclusions, solutions, achievements Evolutionary trace analysisof receptor extracellular domains exhibited several class-specific amino acid residues, which could indicate putative domains for activation of these receptors by ligand recognition and binding. Through site-directed point mutations, the 3rd extracellular domain of PBAN-R was shown to be critical for ligand selection. We identified three receptors that belong to the PBAN family of GPCRs and a partial sequence for the periviscerokinin receptor from the European corn borer, Ostrinianubilalis. Functional expression studies confirmed that only the C-variant of the PBAN-R is active. We identified a non-peptide agonist that will activate the PBAN-receptor from H. zea. We determined that there is transcriptional control of the PBAN-R in two moth species during the development of the pupa to adult, and we demonstrated that this transcriptional regulation is independent of juvenile hormone biosynthesis. This transcriptional control also occurs in male hair-pencil gland complexes of both moth species indicating a regulatory role for PBAN in males. Ultimate confirmation for PBAN's function in the male tissue was revealed through knockdown of the PBAN-R using RNAi-mediated gene-silencing. Implications, both scientific and agricultural The identification of a non-peptide agonist can be exploited in the future for the design of additional compounds that will activate the receptor and to elucidate the binding properties of this receptor. The increase in expression levels of the PBAN-R transcript was delineated to occur at a critical period of 5 hours post-eclosion and its regulation can now be studied. The mysterious role of PBAN in the males was elucidated by using a combination of physiological, biochemical and molecular genetics techniques.
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Sessa, Guido, and Gregory Martin. role of FLS3 and BSK830 in pattern-triggered immunity in tomato. United States Department of Agriculture, 2016. http://dx.doi.org/10.32747/2016.7604270.bard.
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Pattern-recognition receptors (PRRs) located on the plant cell surface initiate immune responses by perceiving conserved pathogen molecules known as pathogen-associated molecular patterns (PAMPs). PRRs typically function in multiprotein complexes that include transmembrane and cytoplasmickinases and contribute to the initiation and signaling of pattern-triggered immunity (PTI). An important challenge is to identify molecular components of PRR complexes and downstream signaling pathways, and to understand the molecular mechanisms that mediate their function. In research activities supported by BARD-4931, we studied the role of the FLAGELLIN SENSING 3 (FLS3) PRR in the response of tomato leaves to flagellin-derivedPAMPs and PTI. In addition, we investigated molecular properties of the tomato brassinosteroid signaling kinase 830 (BSK830) that physically interacts with FLS3 and is a candidate for acting in the FLS3 signaling pathway. Our investigation refers to the proposal original objectives that were to: 1) Investigate the role of FLS3 and its interacting proteins in PTI; 2) Investigate the role of BSK830 in PTI; 3) Examine molecular and phosphorylation dynamics of the FLS3-BSK830 interaction; 4) Examine the possible interaction of FLS3 and BSK830 with Pstand Xcveffectors. We used CRISPR/Cas9 techniques to develop plants carrying single or combined mutations in the FLS3 gene and in the paralogsFLS2.1 and FLS2.2 genes, which encode the receptor FLAGELLIN SENSING2 (FLS2), and analyzed their function in PTI. Domain swapping analysis of the FLS2 and FLS3 receptors revealed domains of the proteins responsible for PAMP detection and for the different ROS response initiated by flgII-28/FLS3 as compared to flg22/FLS2. In addition, in vitro kinase assays and point mutations analysis identified FLS2 and FLS3 domains required for kinase activity and ATP binding. In research activities on tomato BSK830, we found that it interacts with PRRs and with the co-receptor SERK3A and PAMP treatment affects part of these interactions. CRISPR/Cas9 bsk830 mutant plants displayed enhanced pathogen susceptibility and reduced ROS production upon PAMP treatment. In addition, BSK830 interacted with 8 Xanthomonastype III secreted effectors. Follow up analysis revealed that among these effectors XopAE is part of an operon, is translocated into plant cells, and displays E3 ubiquitinligase activity. Our investigation was also extended to other Arabidopsis and tomato BSK family members. Arabidopsis BSK5 localized to the plant cell periphery, interacted with receptor-like kinases, and it was phosphorylatedin vitro by the PEPR1 and EFRPRRs. bsk5 mutant plants displayed enhanced susceptibility to pathogens and were impaired in several, but not all, PAMP-induced responses. Conversely, BSK5 overexpression conferred enhanced disease resistance and caused stronger PTI responses. Genetic complementation suggested that proper localization, kinase activity, and phosphorylation by PRRs are critical for BSK5 function. BSK7 and BSK8 specifically interacted with the FLS2 PRR, their respective mutant plants were more susceptible to B. cinereaand displayed reduced flg22-induced responses. The tomato BSK Mai1 was found to interact with the M3KMAPKKK, which is involved in activation of cell death associated with effector-triggered immunity. Silencing of Mai1 in N. benthamianaplants compromised cell death induced by a specific class of immune receptors. In addition, co-expression of Mai1 and M3Kin leaves enhanced MAPKphosphorylation and cell death, suggesting that Mai1 acts as a molecular link between pathogen recognition and MAPK signaling. Finally, We identified the PP2C phosphatase Pic1 that acts as a negative regulator of PTI by interacting with and dephosphorylating the receptor-like cytoplasmickinase Pti1, which is a positive regulator of plant immunity. The results of this investigation shed new light on the molecular characteristics and interactions of components of the immune system of crop plants providing new knowledge and tools for development of novel strategies for disease control.
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Roth, Sharon Y. P/CAF Function in Transcriptional Activation by Steroid Hormone Receptors and Mammary Cell Proliferation. Defense Technical Information Center, 1999. http://dx.doi.org/10.21236/ada375129.
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Roth, Sharon Y. P/CAF Function in Transcriptional Activation by Steroid Hormone Receptors and Mammary Cell Proliferation. Defense Technical Information Center, 2000. http://dx.doi.org/10.21236/ada392348.
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Diamond, Betty. Determination of the Role of Estrogen Receptors and Estrogen Regulated Genes in B Cell Autoreactivity. Defense Technical Information Center, 2009. http://dx.doi.org/10.21236/ada509183.
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Diamond, Betty. Determination of the Role of Estrogen Receptors and Estrogen Regulated Genes in B Cell Autoreactivity. Defense Technical Information Center, 2011. http://dx.doi.org/10.21236/ada549046.
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Diamond, Betty. Determination of the Role of Estrogen Receptors and Estrogen Regulated Genes in B cell Autoreactivity. Addendum. Defense Technical Information Center, 2012. http://dx.doi.org/10.21236/ada570138.
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