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Syk 323

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https://www.readbyqxmd.com/read/27048659/bi-1002494-a-novel-potent-and-selective-oral-spleen-tyrosine-kinase-inhibitor-displays-differential-potency-in-human-basophils-and-b-cells
#1
David J Lamb, Stefan Lutz Wollin, Andreas Schnapp, Daniel Bischoff, Klaus J Erb, Thierry Bouyssou, Bernd Guilliard, Christine Strasser, Eva Wex, Sylvia Blum, Eva Thaler, Helga Nickel, Oliver Radmacher, Hannah Haas, Jennifer L Swantek, Don Souza, Melissa Canfield, Della White, Mark Panzenbeck, Mohammed A Kashem, Mary Sanville-Ross, Takeshi Kono, Katherina Sewald, Armin Braun, Helena Obernolte, Olga Danov, Gerhard Schaenzle, Georg Rast, Gerd-Michael Maier, Matthias Hoffmann
BI 1002494 [(R)-4-{(R)-1-[7-(3,4,5-trimethoxy-phenyl)-[1,6]napthyridin-5-yloxy]-ethyl}pyrrolidin-2-one] is a novel, potent, and selective spleen tyrosine kinase (SYK) inhibitor with sustained plasma exposure after oral administration in rats, which qualifies this molecule as a good in vitro and in vivo tool compound. BI 1002494 exhibits higher potency in inhibiting high-affinity IgE receptor-mediated mast cell and basophil degranulation (IC50 = 115 nM) compared with B-cell receptor-mediated activation of B cells (IC50 = 810 nM)...
June 2016: Journal of Pharmacology and Experimental Therapeutics
https://www.readbyqxmd.com/read/23960082/tyrosine-phosphorylation-on-spleen-tyrosine-kinase-syk-is-differentially-regulated-in-human-and-murine-platelets-by-protein-kinase-c-isoforms
#2
Lorena Buitrago, Dheeraj Bhavanasi, Carol Dangelmaier, Bhanu Kanth Manne, Rachit Badolia, Alessandra Borgognone, Alexander Y Tsygankov, Steven E McKenzie, Satya P Kunapuli
Protein kinase C (PKC) isoforms differentially regulate platelet functional responses downstream of glycoprotein VI (GPVI) signaling, but the role of PKCs regulating upstream effectors such as Syk is not known. We investigated the role of PKC on Syk tyrosine phosphorylation using the pan-PKC inhibitor GF109203X (GFX). GPVI-mediated phosphorylation on Syk Tyr-323, Tyr-352, and Tyr-525/526 was rapidly dephosphorylated, but GFX treatment inhibited this dephosphorylation on Tyr-525/526 in human platelets but not in wild type murine platelets...
October 4, 2013: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/20670933/determination-of-the-substrate-specificity-of-protein-tyrosine-phosphatase-tula-2-and-identification-of-syk-as-a-tula-2-substrate
#3
Xianwen Chen, Lige Ren, Soochong Kim, Nicholas Carpino, James L Daniel, Satya P Kunapuli, Alexander Y Tsygankov, Dehua Pei
TULA-1 (UBASH3A/STS-2) and TULA-2 (p70/STS-1) represent a novel class of protein-tyrosine phosphatases. Previous studies suggest that TULA-2 is sequence-selective toward phosphotyrosyl (Tyr(P)) peptides. In this work the substrate specificity of TULA-1 and -2 was systematically evaluated by screening a combinatorial Tyr(P) peptide library. Although TULA-1 showed no detectable activity toward any of the Tyr(P) peptides in the library, TULA-2 recognizes two distinct classes of Tyr(P) substrates. On the N-terminal side of Tyr(P), the class I substrates contain a proline at the Tyr(P)-1 position, a hydrophilic residue at the Tyr(P)-2 position, and aromatic hydrophobic residues at positions Tyr(P)-3 and beyond...
October 8, 2010: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/17987119/syk-mediated-translocation-of-pi3kdelta-to-the-leading-edge-controls-lamellipodium-formation-and-migration-of-leukocytes
#4
Jürgen Schymeinsky, Cornelia Then, Anca Sindrilaru, Ronald Gerstl, Zoltán Jakus, Victor L J Tybulewicz, Karin Scharffetter-Kochanek, Barbara Walzog
The non-receptor tyrosine kinase Syk is mainly expressed in the hematopoietic system and plays an essential role in beta(2) integrin-mediated leukocyte activation. To elucidate the signaling pathway downstream of Syk during beta2 integrin (CD11/CD18)-mediated migration and extravasation of polymorphonuclear neutrophils (PMN), we generated neutrophil-like differentiated HL-60 (dHL-60) cells expressing a fluorescently tagged Syk mutant lacking the tyrosine residue at the position 323 (Syk-Tyr323) that is known to be required for the binding of the regulatory subunit p85 of the phosphatidylinositol 3-kinase (PI3K) class I(A)...
2007: PloS One
https://www.readbyqxmd.com/read/9857068/cbl-mediated-negative-regulation-of-the-syk-tyrosine-kinase-a-critical-role-for-cbl-phosphotyrosine-binding-domain-binding-to-syk-phosphotyrosine-323
#5
M L Lupher, N Rao, N L Lill, C E Andoniou, S Miyake, E A Clark, B Druker, H Band
The proto-oncogene product Cbl has emerged as a potential negative regulator of the Syk tyrosine kinase; however, the nature of physical interactions between Cbl and Syk that are critical for this negative regulation remains unclear. Here we show that the phosphotyrosine-binding (PTB) domain within the N-terminal transforming region of Cbl (Cbl-N) binds to phosphorylated Tyr323 in the linker region between the Src homology 2 and kinase domains of Syk, confirming recent results by another laboratory using the yeast two-hybrid approach (Deckert, M...
December 25, 1998: Journal of Biological Chemistry
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