NR AQDI
AU Mattei,V.; Garofalo,T.; Misasi,R.; Circella,A.; Manganelli,V.; Lucania,G.; Pavan,A.; Sorice,M.
TI Prion protein is a component of the multimolecular signaling complex involved in T cell activation
QU FEBS Letters 2004 Feb 27; 560(1-3): 14-8
PT journal article
AB In this study we analyzed the interaction of prion protein PrPc with components of glycosphingolipid-enriched microdomains in lymphoblastoid T cells. PrPc was distributed in small clusters on the plasma membrane, as revealed by immunoelectron microscopy. PrPc is present in microdomains, since it coimmunoprecipitates with GM3 and the raft marker GM1. A strict association between PrPc 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 PrPc interacts with ZAP-70, suggesting that PrPc is a component of the multimolecular signaling complex within microdomains involved in T cell activation.
MH Antibodies, Monoclonal/metabolism; Antigens, CD28/metabolism; Antigens, CD3/metabolism; Carrier Proteins/metabolism; Cell Line, Tumor; Cell Membrane/metabolism/ultrastructure; Fluorescent Antibody Technique; G(M1) Ganglioside/metabolism; G(M3) Ganglioside/metabolism; Human; *Lymphocyte Activation; Membrane Microdomains/chemistry/metabolism/ultrastructure; Microscopy, Confocal; PrPc Proteins/*metabolism/ultrastructure; Precipitin Tests; Protein-Tyrosine Kinase/metabolism; *Signal Transduction; T-Lymphocytes/chemistry/*immunology
AD Dipartimento di Medicina Sperimentale e Patologia, Universita 'La Sapienza', viale Regina Elena 324, 00161 Rome, Italy.
SP englisch
PO Niederlande