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Results for “Immunologic Capping”

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At least 55 records · Page 3Linked to original sources
PubMed1983

Stimulation of lymphocyte receptor capping by the ionophore monensin.

The carboxylic ionophore monensin has a biphasic effect on antibody-induced Thy-1 cap formation. At higher concentrations, 5 X 10(-6)-5 X 10(-5) M monesin causes a significant inhibition of receptor capping similar to that previously found with the Ca2+ selective ionophore A23187. At lower concentrations, 5 X 10(-8)-5 X 10(-7) M capping is stimulated. It is concluded that capping at lower ionophore concentrations is a specific response to the ability of monensin to induce a rise in intracellular Na+, which indirectly elevates intracellular Ca2+ activity. This in turn activates the contractile machinery required for the aggregation of surface receptors into capped structures. At higher concentrations monensin acts as a nonspecific detergent, which causes detrimental structural alterations in some of the membrane components involved in the capping process.

Animals↗
PubMed1989

The role of caldesmon in the regulation of receptor capping in mouse T-lymphoma cell.

Several complementary techniques, including immunocytochemical and immunobiochemical analyses, two-dimensional gel electrophoresis, and peptide mapping, were used in this study to examine the involvement of caldesmon in lymphocyte receptor capping. We have found a lymphoma 140-kDa polypeptide that is structurally similar to muscle caldesmon, suggesting that this polypeptide may be a lymphoma caldesmon. When lymphoma 140-kDa polypeptide is extracted from permeabilized cells using 25 mM MgCl2, capping is inhibited. Adding the 140-kDa protein or gizzard caldesmon back to the extracted cells restores their ability to cap. These findings suggest that actin-linked regulatory proteins such as caldesmon may be critically important to actomyosin-mediated contraction which, in turn, is responsible for collecting receptors into cap structures.

Animals↗
PubMed1999

The human natural killer cell immune synapse.

Inhibitory killer Ig-like receptors (KIR) at the surface of natural killer (NK) cells induced clustering of HLA-C at the contacting surface of target cells. In this manner, inhibitory immune synapses were formed as human NK cells surveyed target cells. At target/NK cell synapses, HLA-C/KIR distributed into rings around central patches of intercellular adhesion molecule-1/lymphocyte function-associated antigen-1, the opposite orientation to mature murine T cell-activating synapses. This organization of protein was stable for at least 20 min. Cells could support multiple synapses simultaneously, and clusters of HLA-C moved as NK cells crawled over target cells. Clustering required a divalent metal cation, explaining how metal chelators inhibit KIR function. Surprisingly, however, formation of inhibitory synapses was unaffected by ATP depletion and the cytoskeletal inhibitors, colchicine and cytochalsins B and D. Clearly, supramolecular organization within plasma membranes is critical for NK cell immunosurveillance.

Actins↗
PubMed1985

T cell activation via CD2 [T, gp50] molecules: accessory cells are required to trigger T cell activation via CD2-D66 plus CD2-9.6/T11(1) epitopes.

Binding monoclonal antibodies (MAb) both to D66 and 9.6/T11(1) epitopes on the CD2 [T,gp50]-defined molecule produces a high level of T cell mitosis. This was observed with a battery of MAb of different isotypes. In contrast, none of the anti-D66 or anti-9.6/T11(1)Ab could trigger T cell proliferation in combination with anti-T11(3). Moreover, all anti-D66-9.6/T11(1) pairs of MAb tested required monocytes to activate T cells which were recruited through their Fc receptors. Variations among normal individuals were observed in the level of response to anti-D66-9.6/T11(1) pairs of Ab, 75% of a population of French Caucasians giving a high response. The level of response of a given individual was determined by his accessory cells. However, the level of response of an individual appeared to be minimally influenced by the isotype of a peculiar anti-D66 or anti-9.6/T11(1) Ab. The addition of exogeneous IL 2 could overcome the removal of accessory cells or the modulation of CD3 molecules. In contrast, IL 2 receptor appearance was not overcome by removal of monocytes. Thus, T cell activation via CD2 seems to be produced by "touching" several definite regions of this molecule which trigger a cascade of events similar to those produced by mitogenic lectins. One can assume that the appropriate conformational changes of the CD2 molecule induced by anti-D66-9.6/T11(1) pairs of Ab are solely produced when they are presented by accessory cells. This leaves open the question of whether accessory cells would also play a more active role.

Antibodies, Monoclonal↗
PubMed1987

Systemic membrane defect and the inhibition of lymphocyte capping in Duchenne muscular dystrophy.

Eight reversible inhibitors were used to study decreases in lymphocyte capping in patients with Duchenne Muscular Dystrophy (DMD) when compared to controls. The inhibitors included hydrocortisone, chlorpromazine, calcium ionophore, Cytochalasin D, propranolol, dibucaine, fluoride and azide. All of these inhibitors disrupt cap formation. Mononuclear leukocytes from DMD patients and controls were isolated from whole blood, incubated with fluorescein-conjugated polyvalent antisera and inhibitor, induced to form caps, and the caps counted using a fluorescent microscope. Cell viabilities and morphology were assessed. After removal of inhibitor, the cells were recounted. All of the inhibitors significantly lowered capping in controls (p less than 0.001), but this effect was seen with only four out of the eight inhibitors in DMD patients. Dibucaine and azide were less inhibitory in patients (p less than 0.005, p greater than 0.05, and p greater than 0.05 respectively) while capping in patients was not inhibited by fluoride and hydrocortisone (p greater than 0.5). The lack of hydrocortisone inhibition suggests that the differences in capping between DMD patients and controls may lie within the membrane itself, rather than its associated components (i.e. cytoskeletal network), and that the defect occurs toward the beginning of the capping sequence.

Cell Membrane↗
PubMed1983

The participation of adenylate cyclase in lymphocyte capping.

In this study, we have observed that cells increase their intracellular cAMP to relatively high levels during receptor capping induced by either ligand-dependent (anti-Thy-1 antibody) or ligand-independent (colchicine) treatment. In addition, we have found that under capping conditions, membrane-bound adenylate cyclase is induced to co-cap with independent membrane molecules such as Thy-1 antigens. These findings suggest that the binding of anti-Thy-1 to its receptors or treatment with colchicine induces the molecular reorganization of membrane-bound adenylate cyclase which may be responsible for activating the contractile machinery required for the collection of surface receptors into a cap structure.

Adenylyl Cyclases↗
PubMed1987

Isolation and initial biochemical characterisation of caps of two major rat thymocyte glycoproteins: evidence for the involvement of a 205 K Con A binding protein and cytoskeletal components in capping.

Two major rat thymocyte surface glycoproteins, the leucocyte-common (L-C) antigen and the leucocyte sialoglycoprotein (LSGP), were induced to cap independently, using the specific monoclonal antibodies OX-1 and W3/13, respectively, and an appropriate fluorescently labeled second antibody layer. The caps were subsequently isolated from detergent extracted cells by a procedure involving gentle shearing. TRITC-phalloidin staining of the isolated caps demonstrated the presence of F-actin within these structures, and lectin-affinity staining after fractionation on SDS polyacrylamide gels revealed the presence of a concanavalin A (Con A) binding protein of relative molecular weight (Mr) 205,000, gp205, in both the L-C antigen and LSGP caps, but absent from the detergent-insoluble residue isolated from unchallenged cells. These results suggest that gp205 may be involved in the association of cross-linked glycoproteins with the cytoskeleton during capping.

Animals↗
PubMed1979

Isolation of concanavalin A caps during various stages of formation and their association with actin and myosin.

Regions of plasma membrane of dictyostelium discoideum amoebae that contain concanavalin A (Con A)-receptor complexes are more resistant to disruption by Triton X-100. This resistance makes possible the isolation of Con A-associated membrane fragments in sufficient quantity and homogeneity to permit the direct biochemical and ultrastructural study of receptor-cytoskeletal interactions across the cell membrane. After specific binding of Con A to the cell surface, a large amount of the cell's actin and myosin copurifies with the plasma membrane fragments. Myosin is more loosely bound to the isolated membranes that actin and is efficiently removed by treating membranes with ATP and low ionic strength. If cells are not lysed immediately after lectin binding, all of the Con A that is bound to the cell surface is swept into a cap in a process requiring metabolic energy. When cells are lysed at different stages of cap formation, the amount of actin and myosin that copurifies with the isolated membranes remains the same. Thick and thin filaments that are attached to the protoplasmic surface of the isolated membranes underlie lectin-receptor complexes during all stages of cap formation. Once the cap is complete, the amount of actin and myosin that tightly bound to the plasma membrane is concentrated into the cap along with the Con A-receptor complexes. These results suggest that the ATP-dependent sliding of membrane-associated actin and myosin filaments is responsible for the accumulation of Con A-receptor complexes into a cap on the cell surface.

Actins↗
PubMed2002

Interface accumulation of receptor/ligand couples in lymphocyte activation: methods, mechanisms, and significance.

Cellular interaction is vital to the activation of most lymphocytes. At the interface between the lymphocyte and the cell that activates it, multiple receptor/ligand pairs accumulate in distinct patterns. This accumulation is intriguing, as it is likely to shape the quality of receptor signaling and thereby lymphocyte behavior. Here we address such receptor/ligand accumulation with an emphasis on T and natural killer (NK) cells. First, we discuss the strengths and limitations of commonly used approaches to visualize receptor/ligand accumulation. Second, we discuss two principal mechanisms of receptor and ligand translocation, diffusion and cytoskeletal transport, as understanding these mechanisms can be invaluable in the determination of the significance of receptor/ligand accumulation. We show that the extent of receptor/ligand accumulation at the T cell/antigen presenting cell interface is dominated by diffusion for all but the lowest affinity interactions, while patterning of these receptors/ligands within the interface is strongly influenced by cytoskeletal transport. Third, we discuss two specific issues in lymphocyte receptor/ligand accumulation. We review the abundant but frequently controversial data on T cell receptor (TCR)/major histocompatibility complex (MHC) accumulation and suggest that central TCR/MHC accumulation is a mediator of efficient T cell activation. In the investigation of NK cell/target cell interactions, we characterize the often tentative NK cell/target cell couple maintenance, as it creates a major obstacle in studying receptor/ligand accumulation.

Animals↗