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Signaling assemblies formed in mast cells activated via Fce receptor I dimers
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SYSNO ASEP 0109000 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Ostatní články Title Signaling assemblies formed in mast cells activated via Fce receptor I dimers Title Signalizační soustavy tvořené v žírných buňkách aktivovaných dimery Fce receptoru I Author(s) Dráberová, Lubica (UMG-J) RID
Lebduška, Pavel (UMG-J)
Hálová, Ivana (UMG-J) RID, ORCID
Tolar, Pavel (UMG-J)
Štokrová, Jitka (UMG-J)
Tolarová, Helena (UMG-J)
Korb, Jan (UMG-J)
Dráber, Petr (UMG-J) RIDSource Title European Journal of Immunology. - : Wiley - ISSN 0014-2980
Roč. 34, č. 8 (2004), s. 2209-2219Number of pages 11 s. Language eng - English Country DE - Germany Keywords mast cell ; protein kinase ; IgE receptor Subject RIV EB - Genetics ; Molecular Biology R&D Projects LN00A026 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) GA204/03/0594 GA ČR - Czech Science Foundation (CSF) GA301/03/0596 GA ČR - Czech Science Foundation (CSF) GA204/00/0204 GA ČR - Czech Science Foundation (CSF) GA310/00/0205 GA ČR - Czech Science Foundation (CSF) IAA5052005 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR) IAA7052006 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR) IAA5052310 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR) CEZ AV0Z5052915 - UMG-J Annotation In this study, we analyzed the activation events induced by FcepsilonRI dimers, elicited by binding of anti-FcepsilonRI mAb to rat basophilic leukemia cells. We found that, in contrast to extensively aggregated FcepsilonRI, receptor dimers (1) induced a less extensive association of FcepsilonRI with detergent-resistant membranes, (2) delayed the tyrosine phosphorylation and membrane recruitment of several signaling molecules, (3) triggered a slower but more sustained increase in concentration of free cytoplasmic calcium, (4) induced degranulation which was not inhibited at higher concentrations of the cross-linking mAb, and (5) failed to produce clusters of FcepsilonRI, Syk kinase and Grb2 adapter in osmiophilic membranes, as detected by immunogold electron microscopy on membrane sheets. Despite striking differences in the topography of FcepsilonRI dimers and multimers, biochemical differences were less pronounced. The combined data suggest that FcepsilonRI-activated mast cells propagate signals from small signaling domains formed around dimerized/oligomerized FcepsilonRI; formation of large FcepsilonRI aggregates in osmiophilic membranes seems to promote both strong receptor triggering and rapid termination of the signaling responses Workplace Institute of Molecular Genetics Contact Nikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217 Year of Publishing 2005
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