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NTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.

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dc.contributor.authorTkaczyk, C-
dc.contributor.authorHorejsi, V-
dc.contributor.authorIwaki, S-
dc.contributor.authorDraber, P-
dc.contributor.authorSamelson, LE-
dc.contributor.authorSatterthwaite, AB-
dc.contributor.authorNahm, DH-
dc.contributor.authorMetcalfe, DD-
dc.contributor.authorGilfillan, AM-
dc.date.accessioned2011-06-30-
dc.date.available2011-06-30-
dc.date.issued2004-
dc.identifier.issn0006-4971-
dc.identifier.urihttp://repository.ajou.ac.kr/handle/201003/3123-
dc.description.abstractAggregation of high-affinity receptors for immunoglobulin E (Fc epsilon RI) on the surface of mast cells results in degranulation, a response that is potentiated by binding of stem cell factor (SCF) to its receptor Kit. We observed that one of the major initial signaling events associated with Fc epsilon RI-mediated activation of human mast cells (HuMCs) is the rapid tyrosine phosphorylation of a protein of 25 to 30 kDa. The phosphorylation of this protein was also observed in response to SCF. This protein was identified as non-T-cell activation linker (NTAL), an adaptor molecule similar to linker for activated T cells (LAT). Unlike the Fc epsilon RI response, SCF induced NTAL phosphorylation in the absence of detectable LAT phosphorylation. When SCF and antigen were added concurrently, there was a marked synergistic effect on NTAL phosphorylation, however, SCF did not enhance the phosphorylation of LAT induced by Fc epsilon RI aggregation. Fc epsilon RI- and SCF-mediated NTAL phosphorylation appear to be differentially regulated by Src kinases and/or Kit kinase, respectively. Diminution of NTAL expression by silencing RNA oligonucleotides in HuMCs resulted in a reduction of both Kit- and Fc epsilon RI-mediated degranulation. NTAL, thus, appears to be an important link between the signaling pathways that are initiated by these receptors, culminating in mast cell degranulation.-
dc.language.isoen-
dc.subject.MESHAdaptor Proteins, Signal Transducing-
dc.subject.MESHAnimals-
dc.subject.MESHAntigens-
dc.subject.MESHCarrier Proteins-
dc.subject.MESHCell Degranulation-
dc.subject.MESHCell Line-
dc.subject.MESHEnzyme Activation-
dc.subject.MESHEnzyme Inhibitors-
dc.subject.MESHHumans-
dc.subject.MESHMast Cells-
dc.subject.MESHMembrane Proteins-
dc.subject.MESHMice-
dc.subject.MESHPhosphoproteins-
dc.subject.MESHPhosphorylation-
dc.subject.MESHProteins-
dc.subject.MESHProto-Oncogene Proteins c-kit-
dc.subject.MESHPyrimidines-
dc.subject.MESHRNA, Small Interfering-
dc.subject.MESHReceptors, IgE-
dc.subject.MESHSignal Transduction-
dc.subject.MESHStem Cell Factor-
dc.subject.MESHStilbenes-
dc.subject.MESHTyrosine-
dc.subject.MESHsrc-Family Kinases-
dc.titleNTAL phosphorylation is a pivotal link between the signaling cascades leading to human mast cell degranulation following Kit activation and Fc epsilon RI aggregation.-
dc.typeArticle-
dc.identifier.pmid15010370-
dc.identifier.urlhttp://www.bloodjournal.org/cgi/pmidlookup?view=long&pmid=15010370-
dc.contributor.affiliatedAuthor남, 동호-
dc.type.localJournal Papers-
dc.identifier.doi10.1182/blood-2003-08-2769-
dc.citation.titleBlood-
dc.citation.volume104-
dc.citation.number1-
dc.citation.date2004-
dc.citation.startPage207-
dc.citation.endPage214-
dc.identifier.bibliographicCitationBlood, 104(1). : 207-214, 2004-
dc.identifier.eissn1528-0020-
dc.relation.journalidJ000064971-
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Allergy
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