Academic literature on the topic 'Actins DNA-Binding Proteins Macrophages Phagocytosis Receptors'

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Journal articles on the topic "Actins DNA-Binding Proteins Macrophages Phagocytosis Receptors"

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Coppolino, Marc G., Matthias Krause, Petra Hagendorff та ін. "Evidence for a molecular complex consisting of Fyb/SLAP, SLP-76, Nck, VASP and WASP that links the actin cytoskeleton to Fcγ receptor signalling during phagocytosis". Journal of Cell Science 114, № 23 (2001): 4307–18. http://dx.doi.org/10.1242/jcs.114.23.4307.

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Phagocytosis by macrophages and neutrophils involves the spatial and temporal reorganisation of the actin-based cytoskeleton at sites of particle ingestion. Local polymerisation of actin filaments supports the protrusion of pseudopodia that eventually engulf the particle. Here we have investigated in detail the cytoskeletal events initiated upon engagement of Fc receptors in macrophages. Ena/vasodilator-stimulated phosphoprotein (VASP) proteins were recruited to phagosomes forming around opsonised particles in both primary and immortalised macrophages. Not only did the localisation of Ena/VASP
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Finnemann, Silvia C., and Enrique Rodriguez-Boulan. "Macrophage and Retinal Pigment Epithelium Phagocytosis." Journal of Experimental Medicine 190, no. 6 (1999): 861–74. http://dx.doi.org/10.1084/jem.190.6.861.

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Noninflammatory monocyte macrophages use αvβ3 integrin to selectively bind apoptotic cells, initiating their phagocytic removal. In a related process, the retinal pigment epithelium (RPE) employs αvβ5 integrin to recognize spent photoreceptor outer segment particles (OS). Here, we show that apoptotic cells and OS compete for binding to these receptors, indicating that OS and apoptotic cells expose surface signals recognizable by αvβ3 and αvβ5. Particle binding to αvβ5 required protein kinase C (PKC) activation. In RPE, αvβ5 binding was maximally activated even before any phagocytic challenge a
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Hart, Derek N. J., Seema Khan, Elisabetta d’Aniello, Kylie J. McDonald, and Masato Kato. "Role of Novel C-Type Lectin Receptor DCL-1 in Phagocytes and Dendritic Cells." Blood 110, no. 11 (2007): 2419. http://dx.doi.org/10.1182/blood.v110.11.2419.2419.

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Abstract Cell surface C-type lectins are implicated in many aspects of immunity. For example, professional phagocytes utilise cell surface C-type lectins in pathogen recognition/binding and phagocytosing the pathogens for destruction and/or antigen processing (e.g. mannose receptor, DC-SIGN, dectin-1). Some C-type lectins are involved in cell-cell adhesion and trafficking of leukocytes (e.g. selectins). DCL-1 is a small type I transmembrane C-type lectin receptor, discovered as a genetic fusion partner of DEC-205. DCL-1 protein was highly conserved amongst the human, mouse and rat orthologs. T
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Castellano, F., P. Montcourrier, and P. Chavrier. "Membrane recruitment of Rac1 triggers phagocytosis." Journal of Cell Science 113, no. 17 (2000): 2955–61. http://dx.doi.org/10.1242/jcs.113.17.2955.

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Rac1 is a Ρ-family GTP-binding protein that controls lamellipodia formation and membrane ruffling in fibroblasts. Recently, Rac1 and Cdc42, another member of the Ρ-family, have been shown to regulate Fc receptor-mediated phagocytosis in macrophages by controlling different steps of membrane and actin dynamics leading to particle engulfment. Here, we investigated the function of Rac1 using a membrane recruitment system that mimics phagocytosis. Recruitment of an activated Rac1 protein to the cytoplasmic domain of an engineered membrane receptor by using rapamycin as a bridge induces ingestion o
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Lewkowicz, Elodie, Floriane Herit, Christophe Le Clainche, Pierre Bourdoncle, Franck Perez, and Florence Niedergang. "The microtubule-binding protein CLIP-170 coordinates mDia1 and actin reorganization during CR3-mediated phagocytosis." Journal of Cell Biology 183, no. 7 (2008): 1287–98. http://dx.doi.org/10.1083/jcb.200807023.

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Microtubule dynamics are modulated by regulatory proteins that bind to their plus ends (+TIPs [plus end tracking proteins]), such as cytoplasmic linker protein 170 (CLIP-170) or end-binding protein 1 (EB1). We investigated the role of +TIPs during phagocytosis in macrophages. Using RNA interference and dominant-negative approaches, we show that CLIP-170 is specifically required for efficient phagocytosis triggered by αMβ2 integrin/complement receptor activation. This property is not observed for EB1 and EB3. Accordingly, whereas CLIP-170 is dynamically enriched at the site of phagocytosis, EB1
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Morrissette, N. S., E. S. Gold, J. Guo, et al. "Isolation and characterization of monoclonal antibodies directed against novel components of macrophage phagosomes." Journal of Cell Science 112, no. 24 (1999): 4705–13. http://dx.doi.org/10.1242/jcs.112.24.4705.

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In order to identify novel proteins associated with various stages of macrophage phagocytosis, we have generated monoclonal antibodies that recognize phagosomes. Purified Fc receptor-mediated phagosomes, isolated by feeding IgG-conjugated magnetic beads to LPS-primed murine peritoneal macrophages, were used as the immunogen. An immunofluorescence screen was used to isolate and single-cell clone approximately 150 monoclonal antibodies that recognize mouse macrophage phagosomes as well as labeling other cellular components in patterns which are frequently distinct from those observed with previo
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Diakonova, Maria, Gary Bokoch та Joel A. Swanson. "Dynamics of Cytoskeletal Proteins during Fcγ Receptor-mediated Phagocytosis in Macrophages". Molecular Biology of the Cell 13, № 2 (2002): 402–11. http://dx.doi.org/10.1091/mbc.01-05-0273.

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Particle ingestion by phagocytosis results from sequential rearrangements of the actin cytoskeleton and overlying membrane. To assemble a chronology of molecular events during phagosome formation and to examine the contributions of phosphoinositide 3-kinase (PI 3-kinase) to these dynamics, a method was developed for synchronizing Fcγ receptor-mediated phagocytosis by murine macrophages. Erythrocytes opsonized with complement component C3bi were bound to macrophages at 37°C, a condition that does not favor particle phagocytosis. Addition of soluble anti-erythrocyte IgG resulted in rapid opsoniz
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Braun, Virginie, Chantal Deschamps, Graça Raposo, et al. "AP-1 and ARF1 Control Endosomal Dynamics at Sites of FcR–mediated Phagocytosis." Molecular Biology of the Cell 18, no. 12 (2007): 4921–31. http://dx.doi.org/10.1091/mbc.e07-04-0392.

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Phagocytosis, the mechanism of ingestion of large material and microorganisms, relies on actin polymerization and on the focal delivery of intracellular endocytic compartments. The molecular mechanisms involved in the formation and delivery of the endocytic vesicles that are recruited at sites of phagocytosis are not well characterized. Here we show that adaptor protein (AP)-1 but not AP-2 clathrin adaptor complexes are recruited early below the sites of particle attachment and are required for efficient receptor-mediated phagocytosis in murine macrophages. Clathrin, however, is not recruited
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Sukumaran, Sunil K., Hiroyuki Shimada, and Nemani V. Prasadarao. "Entry and Intracellular Replication of Escherichia coli K1 in Macrophages Require Expression of Outer Membrane Protein A." Infection and Immunity 71, no. 10 (2003): 5951–61. http://dx.doi.org/10.1128/iai.71.10.5951-5961.2003.

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ABSTRACT Interactions between Escherichia coli K1, which causes meningitis in neonates, and macrophages have not been explored well. In this study we found that E. coli K1 was able to enter, survive, and replicate intracellularly in both murine and human macrophage cell lines, as well as in monocytes and macrophages of newborn rats. In addition, we demonstrated that OmpA + E. coli also enters and replicates in human peripheral blood monocytes in vitro. Outer membrane protein A (OmpA) expression on E. coli contributes to binding to macrophages, phagocytosis, and survival within macrophages. Ops
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Niedergang, Florence, Emma Colucci-Guyon, Thierry Dubois, Graça Raposo, and Philippe Chavrier. "ADP ribosylation factor 6 is activated and controls membrane delivery during phagocytosis in macrophages." Journal of Cell Biology 161, no. 6 (2003): 1143–50. http://dx.doi.org/10.1083/jcb.200210069.

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Engulfment of particles by phagocytes is induced by their interaction with specific receptors on the cell surface, which leads to actin polymerization and the extension of membrane protrusions to form a closed phagosome. Membrane delivery from internal pools is considered to play an important role in pseudopod extension during phagocytosis. Here, we report that endogenous ADP ribosylation factor 6 (ARF6), a small GTP-binding protein, undergoes a sharp and transient activation in macrophages when phagocytosis was initiated via receptors for the Fc portion of immunoglobulins (FcRs). A dominant-n
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Dissertations / Theses on the topic "Actins DNA-Binding Proteins Macrophages Phagocytosis Receptors"

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Mehta, Harshini. "Role of adaptor protein SLAT in Fc[gamma]R mediated phagocytosis in macrophages." Oklahoma City : [s.n.], 2009.

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