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Syk 519

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https://www.readbyqxmd.com/read/20828828/syk-and-lyn-mediate-distinct-syk-phosphorylation-events-in-fc%C3%A9-ri-signal-transduction-implications-for-regulation-of-ige-mediated-degranulation
#1
Michael P Sanderson, Eva Wex, Takeshi Kono, Katsuhiro Uto, Andreas Schnapp
Spleen tyrosine kinase (Syk) is a key regulatory factor in the IgE-mediated allergic signal transduction pathway in mast cells and basophils. Syk is phosphorylated on a number of tyrosines following the binding of IgE/allergen complexes to FcɛRI receptors leading to initiation of inflammatory signaling via downstream enzymes and scaffolding proteins. We examined the kinases responsible for the phosphorylation of key Syk tyrosines in rat RBL-2H3 basophilic cells and bone marrow-derived mast cells (BMMCs). The phosphorylation of Syk tyrosine 346 was completely blocked by the novel Src family kinase inhibitor BIRA766, suggesting this tyrosine is a pure substrate for Src family kinases...
November 2010: Molecular Immunology
https://www.readbyqxmd.com/read/11380624/requirement-of-syk-phospholipase-c-gamma2-pathway-for-phorbol-ester-induced-phospholipase-d-activation-in-dt40-cells
#2
T Hitomi, S Yanagi, R Inatome, J Ding, T Takano, H Yamamura
BACKGROUND: Treatment of many cell types with phorbol esters stimulates phospholipase D (PLD) activity implying regulation of the enzyme by protein kinase C. Studies of the effects of several protein-tyrosine kinase (PTK) inhibitors have suggested that PTK(s) play some roles in the phorbol ester-induced PLD activation, but it remains unclear how and which PTK(s) is involved in this pathway. In this study, we investigated the roles of Syk and other PTKs for the phorbol esters, 12-O-tetradecanoylphorbol 13-acetate (TPA)-induced PLD activation in K562 and DT40 cells...
May 2001: Genes to Cells: Devoted to Molecular & Cellular Mechanisms
https://www.readbyqxmd.com/read/9780214/mutations-in-the-activation-loop-tyrosines-of-protein-tyrosine-kinase-syk-abrogate-intracellular-signaling-but-not-kinase-activity
#3
J Zhang, T Kimura, R P Siraganian
The protein tyrosine kinase Syk plays a pivotal role in mediating the high-affinity IgE receptor (Fc epsilonRI)-induced degranulation of mast cells. To examine the mechanism of Syk regulation, the two tyrosine residues at 519 and 520 in the putative activation loop of rat Syk were mutated to phenylalanine either singly or in combination. The various mutants were expressed in a Syk-negative variant of the RBL-2H3 (rat basophilic leukemia 2H3) mast cell line. In these transfected cell lines, mutant Syk did show increased tyrosine phosphorylation in vivo and increased enzymatic activity in vitro after Fc epsilonRI aggregation...
October 15, 1998: Journal of Immunology: Official Journal of the American Association of Immunologists
https://www.readbyqxmd.com/read/7500027/role-of-the-syk-autophosphorylation-site-and-sh2-domains-in-b-cell-antigen-receptor-signaling
#4
T Kurosaki, S A Johnson, L Pao, K Sada, H Yamamura, J C Cambier
To explore the mechanism(s) by which the Syk protein tyrosine kinase participates in B cell antigen receptor (BCR) signaling, we have studied the function of various Syk mutants in B cells made Syk deficient by homologous recombination knockout. Both Syk SH2 domains were required for BCR-mediated Syk and phospholipase C (PLC)-gamma 2 phosphorylation, inositol 1,4,5-triphosphate release, and Ca2+ mobilization. A possible explanation for this requirement was provided by findings that recruitment of Syk to tyrosine-phosphorylated immunoglobulin (Ig) alpha and Ig beta requires both Syk SH2 domains...
December 1, 1995: Journal of Experimental Medicine
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