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Cited by 44

The DOI matches its Crossref record; 46 of the 46 references it cites were found in a registry or an index.

Association of GM3 with Zap-70 Induced by T Cell Activation in Plasma Membrane Microdomains

Garofalo, Tina, Lenti, Luisa, Longo, Agostina, Misasi, Roberta, Mattei, Vincenzo, Pontieri, Giuseppe M., Sorice, Maurizio, Pavan, Antonio·2002·Journal of Biological Chemistry
DOI 10.1074/jbc.m109601200
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Abstract

Recent evidence demonstrated that T cell activation leads to the redistribution of membrane and intracellular kinase-rich raft microdomains at the site of TCR engagement. In this investigation we demonstrated by high performance thin layer chromatography, gas chromatographic, and mass spectrometric analyses that GM3 is the main ganglioside constituent of these microdomains in human lymphocytes. Then we analyzed GM3 distribution and its interaction with the phosphorylation protein Zap-70. Human T lymphocytes were stimulated with anti-CD3 and anti-CD28. Immunofluorescence microscopy analysis revealed a clustered GM3 distribution over the cell surface and an intracellular localization resembling specific cytoplasmic compartment(s). Scanning confocal microscopy showed that T cell activation induced a significant association between GM3 and Zap-70, as revealed by nearly complete colocalization areas; very few colocalization areas were detected in unstimulated cells. Coimmunoprecipitation experiments revealed that GM3 was immunoprecipitated by anti-Zap-70 only after co-stimulation through CD3 and CD28 as detected by both thin layer chromatography and immunoblotting. Therefore, T cell activation does not promote a redistribution of glycosphingolipid-enriched microdomains but induces Zap-70 translocation in selective membrane domains in which Zap-70 may interact with GM3. These findings suggest that GM3 is a component of a multimolecular signaling complex involved in T cell activatio…

Overview

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Crossref · 10.1074/jbc.m109601200

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46 of 46 references verified0 citation errors · 0 not checkable

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Citations

Cites

Research works printed but not linked: 5

  1. Harder, 1999, Eur. J. Immunol., 29, 556, 10.1002/(SICI)1521-4141(199902)29:02<556::AID-IMMU556>3.0.CO;2-2 · DOI
  2. Millan, 2001, Eur. J. Immunol., 31, 467, 10.1002/1521-4141(200102)31:2<467::AID-IMMU467>3.0.CO;2-1 · DOI
  3. Esselman, 1972, Methods Enzymol., 28, 149
  4. Schauer, 1978, Methods Enzymol., 50, 83
  5. Iwabuchi, 2000, Methods Enzymol., 312, 448

Cited by

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Metadata

Authors
Garofalo, T., Lenti, L., Longo, A., Misasi, R., Mattei, V., Pontieri, G. M., Sorice, M., & Pavan, A.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2002-03
Volume
277
Issue
13
Pages
11233-11238
ISSN
0021-9258
DOI
10.1074/jbc.m109601200
Cited by
44
References
46
Language
en
Licence

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.