scholarly journals Synthesis and In Vitro Protein Tyrosine Kinase Inhibitory Activity of Furan-2-yl(phenyl)methanone Derivatives

Molecules ◽  
2011 ◽  
Vol 16 (6) ◽  
pp. 4897-4911 ◽  
Author(s):  
Fei Lang Zheng ◽  
Shu Rong Ban ◽  
Xiu E Feng ◽  
Cheng Xiao Zhao ◽  
Wenhan Lin ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Inhibitory Activity ◽  
Protein Tyrosine Kinase ◽  
Protein Tyrosine ◽  
Kinase Inhibitory Activity ◽  
Vitro Protein

New Cytotoxic Bisindole Alkaloids with Protein Tyrosine Kinase Inhibitory Activity from a Myxomycete Lycogala epidendrum.

ChemInform ◽  
2005 ◽  
Vol 36 (42) ◽  
Author(s):  
Takahiro Hosoya ◽  
Yukinori Yamamoto ◽  
Yoshimasa Uehara ◽  
Masahiko Hayashi ◽  
Kanki Komiyama ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Inhibitory Activity ◽  
Protein Tyrosine Kinase ◽  
Protein Tyrosine ◽  
Kinase Inhibitory Activity

New cytotoxic bisindole alkaloids with protein tyrosine kinase inhibitory activity from a myxomycete Lycogala epidendrum

2005 ◽  
Vol 15 (11) ◽  
pp. 2776-2780 ◽  
Author(s):  
Takahiro Hosoya ◽  
Yukinori Yamamoto ◽  
Yoshimasa Uehara ◽  
Masahiko Hayashi ◽  
Kanki Komiyama ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Inhibitory Activity ◽  
Protein Tyrosine Kinase ◽  
Protein Tyrosine ◽  
Kinase Inhibitory Activity

Characterization of elk, a brain-specific receptor tyrosine kinase

1991 ◽  
Vol 11 (5) ◽  
pp. 2496-2502
Author(s):  
V Lhoták ◽  
P Greer ◽  
K Letwin ◽  
T Pawson
Keyword(s):  
Tyrosine Kinase ◽  
Receptor Tyrosine Kinase ◽  
Tyrosine Kinases ◽  
Protein Tyrosine Kinase ◽  
Catalytic Domain ◽  
Signal Sequence ◽  
Tyrosine Kinase Domain ◽  
Rat Tissues ◽  
Protein Tyrosine

The elk gene encodes a novel receptorlike protein-tyrosine kinase, which belongs to the eph subfamily. We have previously identified a partial cDNA encompassing the elk catalytic domain (K. Letwin, S.-P. Yee, and T. Pawson, Oncogene 3:621-678, 1988). Using this cDNA as a probe, we have isolated cDNAs spanning the entire rat elk coding sequence. The predicted Elk protein contains all the hallmarks of a receptor tyrosine kinase, including an N-terminal signal sequence, a cysteine-rich extracellular domain, a membrane-spanning segment, a cytoplasmic tyrosine kinase domain, and a C-terminal tail. In both amino acid sequence and overall structure, Elk is most similar to the Eph and Eck protein-tyrosine kinases, suggesting that the eph, elk, and eck genes encode members of a new subfamily of receptorlike tyrosine kinases. Among rat tissues, elk expression appears restricted to brain and testes, with the brain having higher levels of both elk RNA and protein. Elk protein immunoprecipitated from a rat brain lysate becomes phosphorylated on tyrosine in an in vitro kinase reaction, consistent with the prediction that the mammalian elk gene encodes a tyrosine kinase capable of autophosphorylation. The characteristics of the Elk tyrosine kinase suggest that it may be involved in cell-cell interactions in the nervous system.

scholarly journals Contributions of F-BAR and SH2 Domains of Fes Protein Tyrosine Kinase for Coupling to the FcεRI Pathway in Mast Cells

2008 ◽  
Vol 29 (2) ◽  
pp. 389-401 ◽  
Author(s):  
Victor A. McPherson ◽  
Stephanie Everingham ◽  
Robert Karisch ◽  
Julie A. Smith ◽  
Christian M. Udell ◽  
...  
Keyword(s):  
Mast Cells ◽  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
Regulatory Protein ◽  
Sh2 Domain ◽  
Wild Type ◽  
Protein Tyrosine ◽  
Bar Domain ◽  
Sh2 Domains

ABSTRACT This study investigates the roles of Fer-CIP4 homology (FCH)-Bin/amphiphysin/Rvs (F-BAR) and SH2 domains of Fes protein tyrosine kinase in regulating its activation and signaling downstream of the high-affinity immunoglobulin G (IgE) receptor (FcεRI) in mast cells. Homology modeling of the Fes F-BAR domain revealed conservation of some basic residues implicated in phosphoinositide binding (R113/K114). The Fes F-BAR can bind phosphoinositides and induce tubulation of liposomes in vitro. Mutation of R113/K114 to uncharged residues (RK/QQ) caused a significant reduction in phosphoinositide binding in vitro and a more diffuse cytoplasmic localization in transfected COS-7 cells. RBL-2H3 mast cells expressing full-length Fes carrying the RK/QQ mutation show defects in FcεRI-induced Fes tyrosine phosphorylation and degranulation compared to cells expressing wild-type Fes. This correlated with reduced localization to Lyn kinase-containing membrane fractions for the RK/QQ mutant compared to wild-type Fes in mast cells. The Fes SH2 domain also contributes to Fes signaling in mast cells, via interactions with the phosphorylated FcεRI β chain and the actin regulatory protein HS1. We show that Fes phosphorylates C-terminal tyrosine residues in HS1 implicated in actin stabilization. Thus, coordinated actions of the F-BAR and SH2 domains of Fes allow for coupling to FcεRI signaling and potential regulation the actin reorganization in mast cells.

Sign in / Sign up

Export Citation Format

Share Document