Ludwig, L.M.; Weihrauch, D.; Kersten, J.R.; Pagel, P.S.; Warltier, D.C., 2004: Protein kinase C translocation and Src protein tyrosine kinase activation mediate isoflurane-induced preconditioning in vivo: potential downstream targets of mitochondrial adenosine triphosphate-sensitive potassium channels and reactive oxygen species
BioAssay record AID 242624 submitted by ChEMBL: Inhibition of fluorescent (GpYEEI) binding to Src protein tyrosine kinase SH2 domain.
TY - JOUR. T1 - Csk-binding protein controls red blood cell development via regulation of Lyn tyrosine kinase activity. AU - Plani-Lam, Janice H. C.. AU - Slavova-Azmanova, Neli S.. AU - Kucera, Nicole. AU - Louw, Alison. AU - Satiaputra, Jiulia. AU - Singer, Peter. AU - Lam, Kong Peng. AU - Hibbs, Margaret L.. AU - Ingley, Evan. PY - 2017/2/1. Y1 - 2017/2/1. N2 - Erythropoiesis is controlled principally through erythropoietin (Epo) receptor signaling, which involves Janus kinase 2 (JAK2) and Lyn tyrosine kinase, both of which are important for regulating red blood cell (RBC) development. Negative regulation of Lyn involves C-Src kinase (Csk)-mediated phosphorylation of its C-terminal tyrosine, which is facilitated by the transmembrane adaptor Csk-binding protein (Cbp). Although Cbp has significant functions in controlling Lyn levels and activity in erythroid cells in vitro, its importance to primary erythroid cell development and signaling has remained unclear. To address this, we assessed the ...
TY - JOUR. T1 - Docking-based substrate recognition by the catalytic domain of a protein tyrosine kinase, C-terminal Src kinase (Csk). AU - Lee, Sungsoo. AU - Ayrapetov, Marina K.. AU - Kemble, David J.. AU - Parang, Keykavous. AU - Sun, Gongqin. PY - 2006/3/24. Y1 - 2006/3/24. N2 - Protein tyrosine kinases are key enzymes of mammalian signal transduction. Substrate specificity is a fundamental property that determines the specificity and fidelity of signaling by protein tyrosine kinases. However, how protein tyrosine kinases recognize the protein substrates is not well understood. C-terminal Src kinase (Csk) specifically phosphorylates Src family kinases on a C-terminal Tyr residue, which down-regulates their activities. We have previously determined that Csk recognizes Src using a substrate-docking site away from the active site. In the current study, we identified the docking determinants in Src recognized by the Csk substrate-docking site and demonstrated an interaction between the docking ...
Вид документа : Однотомное издание Шифр издания : K Автор(ы) : Pessa-Morikawa T. Заглавие : G proteins and Src-family protein tyrosine kinases in T lymphocytes:Regulation during differentation a.cell activation Выходные данные : Helsinki: Finn.soc.of sciences a.letters, 1993 Колич.характеристики :III,72 c: ил Серия: Commentationes phys.-math.et chem.-med., ISSN 0788-5717;N144 Примечания : ; Библиогр.:с.54-72 ISBN, Цена 951-653-253-5: Б.ц. ГРНТИ : ; 34.39.27 УДК : Ключевые слова (Своб.индексиров.): 0 ; протеин тирозинкиназы Перейти к источнику в Интернете: G proteins and Src-family protein tyrosine kinases in T lymphocytes:Regulation during differentation a.cell activation, Перейти к источнику в Интернете: , Перейти к источнику в Интернете: , ...
TY - JOUR. T1 - Inhibitory role of Src family tyrosine kinases on Ca2+-dependent insulin release. AU - Cheng, Haiying. AU - Straub, Susanne G.. AU - Sharp, Geoffrey W G. PY - 2007/3. Y1 - 2007/3. N2 - Both neurotransmitter release and insulin secretion occur via regulated exocytosis and share a variety of similar regulatory mechanisms. It has been suggested that Src family tyrosine kinases inhibit neurotransmitter release from neuronal cells (H. Ohnishi, S. Yamamori, K. Ono, K. Aoyagi, S. Kondo, and M. Takahashi. Proc Natl Acad Sci USA 98: 10930-10935, 2001). Thus the potential role of Src family kinases in the regulation of insulin secretion was investigated in this study. Two structurally different inhibitors of Src family kinases, SU-6656 and PP2, but not the inactive compound, PP3, enhanced Ca 2+-induced insulin secretion in both rat pancreatic islets and INS-1 cells in a concentration-dependent and time-dependent manner. Furthermore, Src family kinase-mediated insulin secretion appears to ...
We have demonstrated that in the H526 SCLC cell line, Lck activity is required for SCF-stimulated MAPK activation using two complementary techniques: (a) although activation of both Kit and MAPK were sensitive to inhibition by the tyrosine kinase inhibitor PP1, MAPK inhibition occurred at a lower PP1 concentration; this greater sensitivity to PP1 could be partially reversed by overexpression of Lck; and (b) inducible expression of a kinase-inactive DN Lck protein blocked SCF-mediated MAPK activation in a dose-dependent fashion. Although these observations run contrary to the dogma that receptor tyrosine kinases activate the Ras-MAPK pathway directly, they are consistent with a large body of data that demonstrates the importance of Src kinases in signaling from class-III RTKs, including the PDGFR, CSF-1R, and Kit. In murine fibroblasts expressing the PDGFR or the CSF-1R, interaction with their respective ligands recruits Src family kinases to the activated receptors and results in an increase in ...
The kinetics of CHC phosphorylation in activated T cells was slow compared with the total protein tyrosine phosphorylation in cell lysates (not depicted). This delay suggested that other signaling events are initiated before CHC phosphorylation. We had previously found that the activation of c-Src kinase or Lyn kinase, a Src kinase family member, was required for CHC phosphorylation after EGFR and BCR stimulation, respectively (20, 21). To address whether the activity of a Src family kinase was necessary for CHC phosphorylation in activated T cells, we treated Jurkat cells with various concentrations of the Src family kinase inhibitor PP1 before stimulation with soluble anti-CD3 Ab. At increasing concentrations of PP1, but not the serine/threonine kinase inhibitor H7, the level of inducible CHC phosphorylation was diminished (Fig. 2 A). Additionally, in the presence of PP1, the basal level of CHC phosphorylation in Jurkat cells before the induction of TCR internalization was also decreased, ...
Protein-tyrosine kinase C-terminal Src kinase (Csk) was originally purified as a kinase for phosphorylating Src and other Src family kinases. The phosphorylation of a C-terminal tyrosine residue of Src family kinases suppresses their kinase activity. Therefore, most physiological studies regarding Csk function have been focused on Csk as a negative regulator of Src family tyrosine kinases and as a potential tumor suppressor. Paradoxically, the protein levels of Csk were elevated in some human carcinomas. In this report, we show that eukaryotic elongation factor 2 (eEF2) is a new protein substrate of Csk and could locate in the nucleus ...
... and is currently a target of anti-invasive therapies. These outcomes indicate that although raised Src kinase activity is usually needed to focus on actin-associated meats to pre-invadopodia, controlled Src activity is certainly needed for invadopodia matrix and growth destruction activity. Our results explain a previously unappreciated function for proto-oncogenic Src in allowing the intrusive activity of constitutively energetic Src alleles. represents the true amount of cells analyzed within each experimental group. Antibodies and traditional western blotting Traditional western blotting of cell lysates was executed as referred to (Rothschild et al., 2006). The pursuing antibodies had been utilized: 4F11, Src clone GD11 (Upstate); -actin (Calbiochem); Living Shades GFP duplicate JL-8 (BD); Cort-pY421, Src-pY418 (Biosource); bird Src duplicate EC10 (Millipore) and Yes, Fyn (Cell Signaling). Plasmids The SrcCGFP ...
A wide range of extracellular signals are transduced by G protein-coupled receptors (GPCRs). When activated by ligands, GPCRs can activate associated heterotrimeric guanine nucleotide-binding proteins (G proteins), which in turn act on various effectors. Increasing evidence indicates that GPCRs also signal independently of heterotrimeric G proteins. Several GPCRs directly interact with Src-family kinases. Here, we discuss the evidence for direct interaction and activation of Src-family kinases by GPCRs and data that suggest that agonist dosage provides a mechanism by which GPCRs can switch between G protein-dependent and G protein-independent signaling.. ...
Constitutive STAT3 activation by tyrosine phosphorylation of mutated or amplified tyrosine kinases (pYSTAT3) is critical for cancer initiation, progression, invasion, and motility of carcinoma cells. We showed that AF1q is associated with STAT3 signaling in breast cancer cells. In xenograft models, enhanced AF1q expression activated STAT3 and promoted tumor growth and metastasis in immunodeficient NSG mice. The cytokine secretory phenotype of MDA-MB-231LN breast cancer cells with altered AF1q expression revealed changes in expression of platelet-derived growth factor subunit B (PDGF-B). AF1q-induced PDGF-B stimulated motility, migration, and invasion of MDA-MB-231LN cells, and AF1q up-regulated platelet-derived growth factor receptor (PDGFR) signaling. Further, AF1q-induced PDGFR signaling enhanced STAT3 activity through Src kinase activation, which could be blocked by the Src kinase inhibitor PP1. Moreover, AF1q up-regulated tyrosine kinase signaling through PDGFR signaling, which was blockable by
The non-receptor tyrosine kinase Src phosphorylates the newly discovered and described GTPase activating protein (GAP) ARHGAP42 that targets RhoA, among other Rho family GTPases, on tyrosine residue 376 which results in activation of ARHGAP42 which in turn de-activates GTP-bound (active) RhoA and correlates with increased cell motility that relies upon dynamic changes in the actin cytoskeleton and focal adhesions, changes involving RhoA signaling.
In the present study, we investigate the mechanism for the protein kinase A (PKA)-mediated activation of C-terminal Src kinase (Csk). Although isolated Csk kinase domain was phosphorylated at Ser364 by PKA to the same stoichiometry as wild-type Csk, significant activation of the isolated Csk kinase domain by PKA was observed only in the presence of the purified Src homology 3 domain (SH3 domain). Furthermore, the interaction between the SH3 and kinase domains was facilitated by PKA-mediated phosphorylation of the kinase domain, as evaluated by surface plasmon resonance. This suggests that an overall structural domain organization and interaction between the kinase and SH3 domains are important for the activity of Csk and its regulation by PKA.. ...
TY - JOUR. T1 - Structural elements and allosteric mechanisms governing regulation and catalysis of CSK-family kinases and their inhibition of Src-family kinases. AU - Ia, Kim K.. AU - Mills, Ryan D.. AU - Hossain, Mohammed I.. AU - Chan, Khai Chew. AU - Jarasrassamee, Boonyarin. AU - Jorissen, Robert. AU - Cheng, Heung Chin. PY - 2010/10/1. Y1 - 2010/10/1. N2 - C-terminal Src kinase (CSK) and CSK-homologous kinase (CHK) are endogenous inhibitors constraining the activity of the oncogenic Src-family kinases (SFKs) in cells. Both kinases suppress SFKs by selectively phosphorylating their consensus C-terminal regulatory tyrosine. In addition to phosphorylation, CHK can suppress SFKs by a unique non-catalytic inhibitory mechanism that involves tight binding of CHK to SFKs to form stable complexes. In this review, we discuss how allosteric regulators, phosphorylation, and inter-domain interactions interplay to govern the activity of CSK and CHK and their ability to inhibit SFKs. In particular, based ...
Ma Y.C., Huang X.Y.. Src tyrosine kinase is a critical signal transducer that modulates a wide variety of cellular functions. Misregulation of Src leads to cell transformation and cancer. Heterotrimeric guanine-nucleotide-binding proteins (G proteins) are another group of signaling molecules that transduce signals from cell-surface receptors to generate physiological responses. Recently, it was discovered that G alpha s and G alpha i could directly stimulate Src family tyrosine kinase activity. This novel regulation of Src tyrosine kinase by G proteins provides insights into the adenylyl cyclase-independent signaling mechanisms involved in ligand-induced receptor desensitization, internalization and other physiological processes.. Cell. Mol. Life Sci. 59:456-462(2002) [PubMed] [Europe PMC] ...
Ren X, Cao C, Zhu L, Yoshida K, Kharbanda S, Weichselbaum R, Kufe D. Lyn tyrosine kinase inhibits nuclear export of the p53 tumor suppressor. . 2002 Nov-Dec; 1(6):703-8 ...
The identification of small molecules that alter T cell interactions with APCs represents an intriguing therapeutic strategy for autoimmune diseases such as rheumatoid arthritis and systemic lupus erythematosus (SLE). Indeed, a recent study has highlighted the critical importance of T cell and APC contact duration in determining T cell fate in vivo and the development of T cell tolerance or activation (9). There are currently no known small molecules that reverse the T cell stop signal in clinical use, and the addition of such drugs to treat autoimmune diseases is particularly attractive given the high cost of biologic agents and the resultant burden on the healthcare system. In this study, we have identified at least three distinct classes of "reverse-stop" small molecules that impair TCR-induced T cell arrest but not random T cell motility: 1) Src family tyrosine kinase inhibitors, 2) microtubule depolymerizing agents, and 3) PGs. These compounds act in contrast with inhibitors of ...
Src tyrosine kinases transmit integrin-dependent signals pivotal for cell movement and proliferation. Here, we establish a mechanism for Src activation by integrins. c-Src is shown to bind constitutively and selectively to beta3 integrins through an interaction involving the c-Src SH3 domain and the …
c-Src and Lyn will be the only Src family kinases (SFKs) with established activity in osteoclasts (OCs). RANK Gandotinib ligand (RANKL)-induced differentiation attended by suppressed activation of the osteoclastogenic signaling molecules c-Jun and NF-κB. The anti-apoptotic properties of RANKL are also compromised in cells deleted of Fyn an event mediated by increased Bim expression and failed activation of Akt. The defective osteoclastogenesis of Fyn-/- OCs dampens bone resorption in vitro. Finally while Fyn deficiency does not regulate basal osteoclastogenesis in vivo it reduces that stimulated by RANKL by approximately 2/3. Thus Fyn is usually a pro-resorptive SFK which exerts its effects by prompting proliferation and differentiation while attenuating apoptosis of OC lineage cells. Keywords: Gandotinib Osteoclasts Fyn Src family kinase (SFK) M-CSF RANK ligand OCs are multinucleated hematopoietic cells with the unique capacity to degrade bone. They are generated under the aegis of M-CSF and ...
Src (proto-oncogene tyrosine-protein kinase) family is a family of non-receptor tyrosine kinases including nine members: Src, Yes, Fyn, and Fgr, forming the SrcA subfamily, Lck, Hck, Blk, and Lyn in the SrcB subfamily, and Frk in its own subfamily. In immune cells, Src-family kinases (SFKs) have been implicated as critical regulators of a large number of intracellular signaling pathways. Src-family kinases (SFKs) occupy a proximal position in numerous signaling transduction cascades including those emanating from the T and B cell antigen receptors, Fc receptors, growth factor receptors, cytokine receptors, and integrins.
Cross-linking of the neutrophil-beta 2- or beta 3-related leukocyte response integrins by extracellular matrix (ECM) proteins or monoclonal antibodies (mAb) stimulates cytoskeletal rearrangement leading to cell spreading and respiratory burst. Tyrosin phosphorylation of a variety of proteins and activation of the Src family kinases within polymorphonuclear leukocytes (PMN) have recently been implicated in the intracellular signaling pathways generated by leukocyte integrins (Yan, S.R., L. Fumagalli, and G Berton. 1995. J. Inflammation. 45:217-311.) To directly test whether these functional responses are dependent on the Src family kinases p59/61hck and p58c-fgr, we examined adhesion-dependent respiratory burst in PMNs isolated from hck -/-, fgr -/-, and hck -/- fgr -/- knockout mice. Purified bone marrow PMNS from wild-type mice released significant amounts of O2- when adherent to fibrinogen-, fibronectin-, or collagen-coated surfaces, in the presence of activating agents such as tumor necrosis ...
A new study by Marieke Meijer (FGA) published in EMBO Journal reveals a novel pathway for neurons to shut down synaptic transmission via tyrosine phosphorylation of Munc18-1.
Non-receptor tyrosine-protein kinase that plays an important role in the regulation of cell growth, differentiation, migration and immune response. Phosphorylates tyrosine residues located in the C-terminal tails of Src-family kinases (SFKs) including LCK, SRC, HCK, FYN, LYN or YES1. Upon tail phosphorylation, Src-family members engage in intramolecular interactions between the phosphotyrosine tail and the SH2 domain that result in an inactive conformation. To inhibit SFKs, CSK is recruited to the plasma membrane via binding to transmembrane proteins or adapter proteins located near the plasma membrane. Suppresses signaling by various surface receptors, including T-cell receptor (TCR) and B-cell receptor (BCR) by phosphorylating and maintaining inactive several positive effectors such as FYN or LCK (By similarity).
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases. Protein Tyrosine Kinase (PTK) family; C-terminal Src kinase (Csk) subfamily; catalytic (c) domain. The Csk subfamily is composed of Csk, Chk, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk subfamily kinases are cytoplasmic (or nonreceptor) tyr kinases containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr ...
Yao, Q., B. Q. Liu, H. Li, D. McGarrigle, B. W. Xing, M. T. Zhou, Z. Wang, J. J. Zhang, X. Y. Huang and L. Guo (2014). "C-terminal Src kinase (Csk)-mediated phosphorylation of eukaryotic elongation factor 2 (eEF2) promotes proteolytic cleavage and nuclear translocation of eEF2." J Biol Chem 289(18): 12666-78 ...
Treatment with 10 completely M PP2 for 1 hour Constantly blocked ERK phosphorylation in these lymphoma cells au He LY3 OIC, one hour Higher dose of PP2 for completelys Full blocking SFK activity T requires. 1 to M PP1 that are not sufficient to reduce the activity to t SFK block is not inhibited ERK phosphorylation. In line so that the growth of cells is not inhibited UCS 2 at this dose. Because ERK MAPK kinases Src PAR is embroidered and asked if JNK MAPK is also embroidered controlled by the Src kinase. PP2 not affect the phosphorylation of JNK in CH12, LY3 tested UCS 2 and Ly10 lines and two B-lymphoma cells, suggesting that the JNK pathway is not controlled Controlled by Src kinase. Dasatinib and has not decreased in the phosphorylation of JNK UCS 2 cells. PI-3-kinase / AKT survival pathway is activated in a variety of important cancer cells. In B cells, CD19 Lyn phosphorylates to activate PI-3 kinase / AKT in response to antigenic stimulation.. ...
We previously reported that endogenous ROS production by high glucose in diabetic GK islets is elevated compared with that in control Wistar islets and is effectively ameliorated by Src inhibition, suggesting that Src may be activated in GK islets (6). In the present study, we first investigated whether Src activity is altered in GK islets. Immunoblotting analysis revealed that the level of Src pY416, which indicates the level of Src activation, is higher in GK islets than that in Wistar islets, despite lower levels of total Src, Src pY527, and Csk. The lower level of total Src seems to be a consequence of Src activation. Targeted degradation of active forms of Src is brought about by ubiquitination (29). The protooncogene c-Cbl, recently found to be an E3 ubiquitin ligase, mediates ubiquitination of activated Src (30). These reports suggest that increased degradation of activated Src may result in a lower level of total Src in GK islets. In addition, a lower level of Csk might cause a lower ...
摘 要:BCR/ABL融合蛋白是慢性粒细胞白血病(CML)的分子标志,具有高激酶活性,其在疾病发生、发展中扮演了极其重要的角色。伊马替尼(Imatinib)靶向抑制BCR-ABL,为CML慢性期的一线治疗药。BCR/ABL与Src家族激酶(Src-family kinases, SFK)之间也存在相互活化作用,通过激活众多信号通路,导致CML向急变期发展,并导致伊马替尼耐药。对有关BCR/ABL与SFK两者的相互作用机制及其生物学效应的研究进行总结 ...
The present invention relates to the treatment of EGFR-mediated disease, particularly cancer by inhibiting or blocking EGFR and src in combination or simultaneously. The invention relates to treatment, prevention, or modulation of cancer, particularly EGFR-mediated disease, with one or more EGFR modulator and src inhibitor in combination. The invention further relates to the treatment of cancer with anti-EGFR antibodies and src inhibitors. Methods and compositions for treatment of cancer with the antibody anti-EGFR mAb806 in combination or series with a src inhibitor or src inhibitors are described.
Complete information for SYF2 gene (Protein Coding), SYF2 Pre-MRNA Splicing Factor, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
TNBC has been thought as an extremely aggressive and refractory malignancy (29). Currently, no targeted drug is approved to use in the treatment of TNBC in clinic (30). Though some targeted drugs have entered clinical trials, most of them just showed very limited efficacy against TNBC. For example, dasatinib, a SRC family kinase inhibitor, has been assessed in phase II clinical trial. As a single agent, dasatinib exhibited moderate efficacy in TNBC patients and the clinical response rate was just 9.3% (4/43; ref. 31). Another agent, sorafenib, a VEGFR/Raf inhibitor, has been reported to have modest activity as a single agent in metastatic breast cancer patients, which contained some TNBC patients (32). Interestingly, a recent study has demonstrated that combined use of dasatinib and sorafenib displayed an enhanced efficacy compared with sole use of either dasatinib or sorafenib in inhibiting TNBC cells (33). This study prompted an advantage of use agents concurrently targeting multi-targets in ...
AZD0424 is a potent orally available, potent (IC50 approximately 4 nM) inhibitor of Src and ABL1 kinases with additional activity against Src family kinase (SFK) members including Yes and Lck. AZD0424 was selective for SFKs and ABL1 kinase over C-terminal Src kinase (a negative regulator of Src) and a range of other kinase targets. The anti-cancer activity of AZD0424 is thought to be mediated primarily by anti-migratory and anti-invasive signalling and, as such, it is expected that in the late stage cancer setting strong signals of efficacy with this compound used as a single agent are unlikely, requiring it to be administered in combination with other anti-cancer agents.. In summary the study will be performed in four main stages:. ...
C-terminal Src kinase (CSK) functions as a negative regulator of T cell activation through inhibitory phosphorylation of LCK, so inhibitors of CSK are of interest as potential immuno-oncology agents ...
Wang, Z., Han, Q. Q., Zhou, M. T., Chen, X., and Guo, L. (2016) Protein turnover analysis in Salmonella Typhimurium during infection by dynamic SILAC, Topograph, and quantitative proteomics. J. Basic Microbiol. 56, 801-811. Yao, Q., Liu, B. Q., Li, H., McGarrigle, D., Xing, B. W., Zhou, M. T., Wang, Z., Zhang, J. J., Huang, X. Y., and Guo, L. (2014) C-terminal Src kinase (Csk)-mediated phosphorylation of eukaryotic elongation factor 2 (eEF2) promotes proteolytic cleavage and nuclear translocation of eEF2. J. Biol. Chem. 289, 12666-12678. ...
The inhibition obtained by the number of molecules in 1 µg rCCP1-CCP2-SP per ml was. thus said to be equivalent to the number of molecules in 1·76 (79 247/45 073) µg MASP-1 per ml. We added the rCCP1-CCP2-SP to 10% fetal calf serum before performing the dilutions in order to obtain a similar matrix and to obtain comparable slopes of the dilution curve of the standard plasma and the recombinant material (the antibodies employed do not cross-react with bovine MASP-1). To test for the specificity of the assay, purified rMAp44 or rMASP-3 (produced and purified as described in Degn et al. [21]) was added to the MASP-1 assay at a concentration of 10 µg/ml for rMAp44 Erismodegib ic50 and 2·5 µg/ml for rMASP-3 at the highest concentration and dilutions thereof. The addition of rMAp44 or rMASP-3 did not influence the signal. To characterize the assay further and to study the association of MASP-1 with other serum components, serum was subjected to gel. permeation chromatography (GPC) on a 1 × 30 ...
Supplementary Materials10549_2017_4442_MOESM1_ESM. blotting, luciferase reporter assays, TUNEL assays, analysis of the gene, and ChIP assays. Results NSC35446.HCl inhibited proliferation and induced apoptosis in antiestrogen resistant LCC9, T47DCO, MCF-7/RR, and LY2 cells but not in ER-negative breast malignancy cell lines. (mRNA and protein expression in LCC9 cells. NSC35446.HCl also inhibited NF-B activity and expression of NF-B target genes. analysis of the promoter recognized nine estrogen response element (ERE) half-sites and one ERE-like full-site. ChIP assays revealed that ER was recruited to the ERE-like full-site and five from the nine half-sites which ER recruitment was inhibited by NSC35446.HCl in T47DCO and. ...
Complete information for FGR gene (Protein Coding), FGR Proto-Oncogene, Src Family Tyrosine Kinase, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Considering these results, our failure to detect mutations in our cancer materials could mean that: (a) no c-src mutations were, in fact, present; and (b) activating genetic alterations had occurred in other regions of c-src outside exon 12 in the tumors we studied. According to the method described by Irby et al. (10) , the PCR products from tumor samples were sequenced manually, as well as by automated sequencers. In this method, there would be a possible risk for a technical artifact, such as artificial mutation, generated in the process of PCR amplification and for contamination.. c-src and structurally related members of the src family are non-receptor tyrosine kinases that reside within the cell, associated with cell membranes; they seem to transduce signals from transmembrane receptors to the cell interior (24) . Many intracellular pathways can be stimulated on src activation, inducing a variety of consequences including morphological changes and cell proliferation (25, 26, 27) . c-src ...
Structure of a large fragment of the c-Src tyrosine kinase shows that interactions among domains, stabilized by binding of the phosphorylated tail to the SH2 domain, lock the molecule in a conformation that simultaneously disrupts the kinase active site and sequesters the binding surfaces of the SH2 and SH3 domains. N lobe rotates 9 degress relative to its position in the cAPK Sidechain of Glu310 moves 12 A ...
CSK antibody [CSK-04] (c-src tyrosine kinase) for ICC/IF, IP, WB. Anti-CSK mAb (GTX14996) is tested in Human, Mouse samples. 100% Ab-Assurance.
Ellison, S., Mori, J., Barr, Alastair J. and Senis, Y.A. (2010) CD148 enhances platelet responsiveness to collagen by maintaining a pool of active Src family kinases. Journal of Thrombosis and Haemostasis, 8 (7). pp. 1575-1583. ISSN 1538-7933 ...
Mouse Monoclonal Anti-Lyn Antibody (LYN-01) [PerCP]. Validated: WB, ICC/IF, IP. Tested Reactivity: Human, Mouse, Rat. 100% Guaranteed.
LYN-1604 is a potential ULK1 agonist with IC50 of 1.66 μM against MDA-MB-231 cells and it binds to wild-type ULK1 with a binding affinity in the nanom... Quality confirmed by NMR & HPLC. See customer reviews, validations & product citations.
K05704 tyrosine-protein kinase Src [EC:2.7.10.2] , (RefSeq) SRC, ASV, SRC1, THC6, c-SRC, p60-Src; SRC proto-oncogene, non-receptor tyrosine ...
マウス・モノクローナル抗体 ab1890 交差種: Ms,Rat,Hu 適用: WB,IP,ICC,Flow Cyt,ICC/IF…Lyn抗体一覧…画像、プロトコール、文献などWeb上の情報が満載のアブカムの Antibody 製品。国内在庫と品質保証制度も充実。
SRC3兔多克隆抗体(ab10313)可与人样本反应并经WB, IP实验严格验证。中国75%以上现货,所有产品均提供质保服务,可通过电话、电邮或微信获得本地专属技术支持。
购买我们的重组人Src蛋白。Ab51424为有活性的全长蛋白,在大肠杆菌中生产并经过Functional Studies, SDS-PAGE实验验证。中国80%以上现货。
Malignant mesothelioma is an aggressive tumor arising from mesothelial cells of serous membranes. Src family kinases (SFKs) have a pivotal role in cell adhesion, proliferation, survival and apoptosis. Here, we examined the effect of SFK inhibitors in NCI-H2052, ACC-MESO-4 and NCI-H28 cells, mesothelioma cell lines and Met5A, a human non-malignant mesothelial cell line. We found that PP2, a selective SFK inhibitor, inhibited SFK activity and induced apoptosis mediated by caspase-8 in NCI-H28 but not Met5A, NCI-H2052 and ACC-MESO-4 cells. Src, Yes, Fyn and Lyn protein, which are members of the SFK, were expressed in these cell lines, whereas NCI-H28 cells were deficient in Fyn protein. Small interfering RNA (siRNA) targeting Fyn facilitated PP2-induced apoptosis mediated by caspase-8 in NCI-H2052 and ACC-MESO-4 cells. PP2 reduced Lyn protein levels and suppressed SFK activity in all mesothelioma cell lines. Lyn siRNA induced caspase-8 activation and apoptosis in NCI-H28 cells but not in NCI-H2052 ...
TY - JOUR. T1 - A common signaling pathway via Syk and Lyn tyrosine kinases generated from capping of the sialomucins CD34 and CD43 in immature hematopoietic cells. AU - Tada, Jun Ichi. AU - Omine, Mitsuhiro. AU - Suda, Toshio. AU - Yamaguchi, Naoto. PY - 1999/6/1. Y1 - 1999/6/1. N2 - The sialomucin CD34 is a useful marker for hematopoietic stem/progenitor cells. However, the role of CD34 remains poorly understood. Here we investigate the functions of CD34 and another sialomucin CD43 coexpressed on hematopoietic stem/progenitor cells. Stimulation of undifferentiated hematopoietic KG1a cells with anti-CD34 or anti-CD43 induced homotypic cytoadhesion, accompanied by formation of a long-lived cap of CD34 and CD43 respectively, which colocalized with F-actin. Stimulation with either antibody specifically increased tyrosine phosphorylation of the identical set of proteins of Lyn, Syk, pp60, pp69, and pp77 at the capping site. These events were similar to those observed in monocytic U937 cells ...