Accessory Cell Signals Involved in T‐Cell Activation

Geppert, Thomas D.; Davis, Laurie S.; Gur, Hanan; Wacholtz, Mary C.; Lipsky, Peter E.

doi:10.1111/j.1600-065x.1990.tb00566.x

Cited by 182 publications

(94 citation statements)

References 215 publications

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“…Although class I proteins are best known for their important role in immunity (reviewed in Yewdell & Bennink, 1992), they have also been found in association with several peptide hormone and growth factor receptors (reviewed in Edidin, 1988). Also, cross-linking class I proteins with antibodies triggers partial activation of T cells (Geppert et al, 1988;Dissing et al, 1990).…”

Section: Discussionmentioning

confidence: 99%

Extracellular Simian Virus 40 Induces an ERK/MAP Kinase-independent Signalling Pathway that Activates Primary Response Genes and Promotes Virus Entry

Dangoria

Breau

Anderson

et al. 1996

Journal of General Virology

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Section: Discussionmentioning

confidence: 99%

Extracellular Simian Virus 40 Induces an ERK/MAP Kinase-independent Signalling Pathway that Activates Primary Response Genes and Promotes Virus Entry

Dangoria

Breau

Anderson

et al. 1996

Journal of General Virology

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“…Interferon 'y (IFN-y), a cytokine secreted from stimulated T cells, is a potent activator of monocytes and macrophages and, therefore, is a critical component for host defense and inflammation (1)(2)(3). The diverse effects elicited by IFN-y are in part due to the induction of various early-response genes.…”

mentioning

confidence: 99%

Interferon gamma rapidly induces in human monocytes a DNA-binding factor that recognizes the gamma response region within the promoter of the gene for the high-affinity Fc gamma receptor.

Wilson

Finbloom²

1992

Proc. Natl. Acad. Sci. U.S.A.

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“…We suspect that some of the variability described for insolubilization of different cell surface proteins (30) may simply reflect variations in the degree of aggregation induced by different anti-receptor antibodies and in the rates at which the aggregated proteins became solubilized. These factors, as well as other methodological differences, presumably explain why some investigators (30) have reported that the CD45 (T200) protein remains soluble after aggregation, whereas others (27,31) have reported the contrary.…”

Section: Discussionmentioning

confidence: 85%

“…We wanted to avoid centrifugation because it is difficult, if not impossible, to discriminate between simple sedimentation of the immune complexes formed when aggregation is induced and insolubilization due to interaction between the aggregated receptors and the membrane skeletons. Flow cytometry (5,29,30) was an effective solution to this problem.…”

Section: Discussionmentioning

confidence: 99%

Interaction of aggregated native and mutant IgE receptors with the cellular skeleton.

Mao

Alber

Rivera

et al. 1992

Proc. Natl. Acad. Sci. U.S.A.

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When aggregated, cell surface proteins become resistant to solubilization by detergents, presumably because of aggregation-induced or -stabilized interactions between the membrane protein and the cytoskeleton or plasma membrane skeleton. We genetically engineered variants of the tetrameric high-affinity receptor for IgE (Fc6RI) to identify a site on its a, (3, or y chains that mediates such putative interactions. Using flow cytofluorometry, we studied rat basophilic leukemia cells, transiently transfected COS cells, and stably transfected P815 cells bearing wild-type and mutated receptors. We observed that (i) solubilization was markedly dependent on the degree of aggregation, the extent varying somewhat with the cell type and, particularly at lower levels of aggregation, with the time after addition of detergent; (iu) truncation of no single cytoplasmic domain of the a, 13, or y chains ablated the insolubilization effect; and (ii) incomplete receptors were also efficiently insolubilized by aggregation. Thus receptors consisting only of a and y chains, a "receptor" consisting of only the ectodomain of the a chain attached to the plasma membrane by a glycosyl-phosphatidyl inositol anchor, and "receptors" consisting only of minimally modified Y chains were resistant to solubilization after aggregation. We conclude that no unique subunit or domain of FcRI mediates the insolubilization phenomenon. Our results support a model in which the bridging of membrane proteins leads to their becoming nonspecifically enmeshed in a network of membrane skeletal proteins on either the outside and/or the inside of the membrane so that dissolution of the lipid bilayer becomes irrelevant.Aggregation of a variety of membrane proteins leads to changes in their topological properties: their translational and rotational mobility is markedly decreased, they become segregated into clusters ("patching" and "capping"), they may be internalized by coated pits or by an alternative mechanism, and they become resistant to solubilization by detergents that dissolve the lipid bilayer in which the proteins are embedded. Most workers have plausibly postulated that these phenomena are related to interactions between the aggregated protein and other cellular components such as those that constitute the cytoskeleton or plasma membrane skeleton.The receptor that binds IgE with high affinity (Fc6RI) has been widely studied with respect to these phenomena because of the relative ease with which its aggregation can be systematically altered and the changes in its properties can be monitored (1-3). The receptor is known to consist of three transmembrane peptides (one a chain and two y chains) and a single 83 chain with four transmembrane domains and substantial N-terminal and C-terminal cytoplasmic domains (4). However, as yet no specific regions of this tetrameric (a, 13, y2) receptor have been implicated as mediating the interactions that lead to the changes in the receptor's topological characteristics, nor have the cellular components with whic...

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Accessory Cell Signals Involved in T‐Cell Activation

Cited by 182 publications

References 215 publications

Extracellular Simian Virus 40 Induces an ERK/MAP Kinase-independent Signalling Pathway that Activates Primary Response Genes and Promotes Virus Entry

Extracellular Simian Virus 40 Induces an ERK/MAP Kinase-independent Signalling Pathway that Activates Primary Response Genes and Promotes Virus Entry

Interferon gamma rapidly induces in human monocytes a DNA-binding factor that recognizes the gamma response region within the promoter of the gene for the high-affinity Fc gamma receptor.

Interaction of aggregated native and mutant IgE receptors with the cellular skeleton.

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