Abstract
In this study we analyzed the interaction of prion protein PrP(C) with components of glycosphingolipid-enriched microdomains in lymphoblastoid T cells. PrP(C) was distributed in small clusters on the plasma membrane, as revealed by immunoelectron microscopy. PrP(C) is present in microdomains, since it coimmunoprecipitates with GM3 and the raft marker GM1. A strict association between PrP(C) and Fyn was revealed by scanning confocal microscopy and coimmunoprecipitation experiments. The phosphorylation protein ZAP-70 was immunoprecipitated by anti-PrP after T cell activation. These results demonstrate that PrP(C) interacts with ZAP-70, suggesting that PrP(C) is a component of the multimolecular signaling complex within microdomains involved in T cell activation.
MeSH terms
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Adaptor Proteins, Signal Transducing*
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Antibodies, Monoclonal / metabolism
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CD28 Antigens / metabolism
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CD3 Complex / metabolism
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Carrier Proteins / metabolism
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Cell Line, Tumor
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Cell Membrane / metabolism
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Cell Membrane / ultrastructure
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Fluorescent Antibody Technique
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G(M1) Ganglioside / metabolism
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G(M3) Ganglioside / metabolism
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Humans
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Lymphocyte Activation*
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Membrane Microdomains / chemistry
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Membrane Microdomains / metabolism
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Membrane Microdomains / ultrastructure
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Microscopy, Confocal
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PrPC Proteins / metabolism*
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PrPC Proteins / ultrastructure
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Precipitin Tests
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Protein-Tyrosine Kinases / metabolism
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Signal Transduction*
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T-Lymphocytes / chemistry
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T-Lymphocytes / immunology*
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ZAP-70 Protein-Tyrosine Kinase
Substances
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Adaptor Proteins, Signal Transducing
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Antibodies, Monoclonal
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CD28 Antigens
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CD3 Complex
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Carrier Proteins
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FYB1 protein, human
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G(M3) Ganglioside
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PrPC Proteins
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G(M1) Ganglioside
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Protein-Tyrosine Kinases
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ZAP-70 Protein-Tyrosine Kinase
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ZAP70 protein, human