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Data show that protein tyrosine kinase p56(lck) (Lck) expression is higher in Th1 cells as compared to Th2 cells.
LCK nitration inhibits T cell activation, leading to reduced interleukin 2 (IL2) production and proliferation.
Mutation of the basic clusters in the CD28 cytoplasmic domain reduced the recruitment to the CD28-Lck complex of protein kinase Ctheta; (PKCtheta;), which serves as a key effector kinase in the CD28 signaling pathway.
A phosphosite within the SH2 Domain of Lck regulates its activation by CD45. A negative feedback loop that responds to signaling events tunes active Lck amounts and TCR sensitivity.
We show a striking 65% reduction in cellularity, preferential development of gammadelta versus alphabeta T cells, and increased expression of IL-7R in the thymus of mice expressing Cre under the proximal lck promoter (lck-cre(+) mice)
this work demonstrates a role for constitutive Lck activity in controlling antigen sensitivity
this study defines distinct and complementary requirements for proximal and distal lck promoters during T-cell development
Aurora A inhibition causes delocalized clustering of Lck at the immunological synapses and decreases its phosphorylation levels thus indicating Aurora A is required for maintaining Lck active during T-cell activation.
essential for thymic development in presence or absence of Cbl, ensuring MHC restriction of T cells
Lck-Dlx5 mice develop T-ALLs that consistently acquire overexpression of Myc and activation of Akt.
Lck-CD8 interaction is required for initial CD8 recruitment.
The kinase Itk and the adaptor TSAd change the specificity of the kinase Lck in T cells by promoting the phosphorylation of Tyr192.
CD4 is expressed in distinct nanoclusters and does not colocalize with T-cell receptor and active protein tyrosine kinase p56lck
lymphoid cell kinase is the crucial effector of beta1-integrin signalling in Schwann cells
Study concludes that the intracellular state of Lck Study conclude that the intracellular state of Lck determines the specificity of thymic selection and that Lck association with coreceptor proteins during thymic selection is the mechanism by which MHC restriction is imposed on a randomly generated alphabetaTCR repertoire.
LCK could be considered a target attenuated by the anti-aging effects of CR. Integrative analysis of cDNA microarray and interactome data are powerful tools for identifying target molecules that are involved in the aging process and modulated by CR.
Mechanistically, poly-G oligonucleotides directly induce the phosphorylation of Lck (an essential element of the T cell-signaling pathway), thereby enhancing production of IL-2 and CD8 T cell proliferation.
Specific pharmacological inhibition and genetic silencing indicated the involvement of Lck in the regulation of neuritic outgrowth.
Data show that activation of both tuned and untuned CD4 single-positive (SP) thymocytes is Lck-dependent.
results show that Lck plays an essential role in PC in both cellular and animal models of stroke.
The ionic CD3-epsilon -Lck interaction controls the phosphorylation level of the T-cell receptor.
a previously unappreciated role for PLC-gamma1 in the positive regulation of Zap-70 and T-cell receptor tyrosine phosphorylation. Conversely, PLC-gamma1 negatively regulated the phosphorylation of SLP-76-associated proteins, including previously established Lck substrate phosphorylation sites within this complex.
autophosphorylation of the LCK active-site loop is indispensable for its catalytic activity and LCK can stimulate its own activation by adopting a more open conformation, which can be modulated by point mutations, and CD4 and CD8, T-cell coreceptors, can enhance LCK activity
the central biological role of the novel IL-2-R/Lck/PLCgamma/PKCtheta;/alphaPIX/Rac1/PYGM signalling pathway is directly related to the control of fundamental cellular processes such as T cell migration and proliferation.
Possible models of regulation of Lck by Aurora-A during T cell activation are described in the review.
Data suggest that T cell activation through the TCR complex is accompanied by the de novo activation of T-lymphocyte specific protein tyrosine kinase p56lck (Lck) and that phosphorylation of Tyr(394) plays a role in Lck function that goes beyond inducing an open conformation of the kinase.
WASH has a pivotal role for regulation of NK cell cytotoxicity through Lck-mediated Y141 tyrosine phosphorylation.
The results have revealed a novel splicing homozygous mutation of LCK that may be responsible for the clinical phenotype of HPV infection from latency to invasive carcinoma.
this study show that Lck as a major signaling hub of CD147 in T cells
data indicate that HSP65 suppresses cholesterol efflux and increases cellular cholesterol content through an Lck-mediated pathway in T cells
LSKlow cells, which are derived from LSK cells in p18(-/-) mice, possess lymphoid differentiation ability and short-term repopulation capability.
These results suggest that PM lipids, including phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate, modulate interaction of Lck with its binding partners in the TCR signaling complex and its TCR signaling activities in a spatiotemporally specific manner via its SH2 domain.
this study shows that p56(lck), which is essential for activation of T cells through the T-cell receptor, is also critical for signal transduction through Toll-like receptors in T cells
Results demonstrate that Lck represses oxidative phosphorylation through competitive binding with mitochondrial CRIF1 in a kinase-independent manner.
introducing bulky side-chains into this patch (GGxxG to GVxxL) impairs the Lck-independent role of CD4 in T cell activation upon TCR engagement of agonist and weak agonist stimulation.
our results support a novel function of nuclear Lck in promoting human leukemic T cell survival through interaction with a tumor suppressor, CRIF1
TSAD binds to and co-localizes with Nck. Expression of TSAD increases both Nck-Lck and Nck-SLP-76 interaction in T cells.
LCK gene could be an useful candidate gene in selection for increasing litter size in pigs.
This gene is a member of the Src family of protein tyrosine kinases (PTKs). The encoded protein is a key signaling molecule in the selection and maturation of developing T-cells. It contains N-terminal sites for myristylation and palmitylation, a PTK domain, and SH2 and SH3 domains which are involved in mediating protein-protein interactions with phosphotyrosine-containing and proline-rich motifs, respectively. The protein localizes to the plasma membrane and pericentrosomal vesicles, and binds to cell surface receptors, including CD4 and CD8, and other signaling molecules. Multiple alternatively spliced variants, encoding the same protein, have been described.
lymphocyte protein tyrosine kinase
, lymphocyte-specific protein tyrosine kinase
, tyrosine-protein kinase Lck-like
, leukocyte C-terminal Src kinase
, lymphocyte cell-specific protein-tyrosine kinase
, proto-oncogene tyrosine-protein kinase LCK
, T-lymphocyte specific protein tyrosine kinase p56lck
, p56(LSTRA) protein-tyrosine kinase
, t cell-specific protein-tyrosine kinase
, tyrosine-protein kinase Lck
, tyrosine protein kinase
, tyrosine-protein kinase LCK