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Literatura académica sobre el tema "Kinase Syk"

Autor: Grafiati

Publicado: 29 de marzo de 2025

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Artículos de revistas sobre el tema "Kinase Syk"

Makhoul, Stephanie, Stephanie Dorschel, Stepan Gambaryan, Ulrich Walter y Kerstin Jurk. "Feedback Regulation of Syk by Protein Kinase C in Human Platelets". International Journal of Molecular Sciences 21, n.º 1 (25 de diciembre de 2019): 176. http://dx.doi.org/10.3390/ijms21010176.

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The spleen tyrosine kinase (Syk) is essential for immunoreceptor tyrosine-based activation motif (ITAM)-dependent platelet activation, and it is stimulated by Src-family kinase (SFK)-/Syk-mediated phosphorylation of Y352 (interdomain-B) and Y525/526 (kinase domain). Additional sites for Syk phosphorylation and protein interactions are known but remain elusive. Since Syk S297 phosphorylation (interdomain-B) was detected in platelets, we hypothesized that this phosphorylation site regulates Syk activity via protein kinase C (PKC)-and cyclic adenosine monophosphate (cAMP)-dependent pathways. ADP, the GPVI-agonist convulxin, and the GPIbα-agonist echicetin beads (EB) were used to stimulate human platelets with/without effectors. Platelet aggregation and intracellular messengers were analyzed, along with phosphoproteins, by immunoblotting using phosphosite-specific antibodies or phos-tags. ADP, convulxin, and EB upregulated Syk S297 phosphorylation, which was inhibited by iloprost (cAMP pathway). Convulxin-stimulated Syk S297 phosphorylation was stoichiometric, transient, abolished by the PKC inhibitor GF109203X, and mimicked by the PKC activator PDBu. Convulxin/EB stimulated Syk S297, Y352, and Y525/526 phosphorylation, which was inhibited by SFK and Syk inhibitors. GFX and iloprost inhibited convulxin/EB-induced Syk S297 phosphorylation but enhanced Syk tyrosine (Y352/Y525/526) and substrate (linker adaptor for T cells (LAT), phospholipase γ2 (PLC γ2)) phosphorylation. GFX enhanced convulxin/EB-increases of inositol monophosphate/Ca2+. ITAM-activated Syk stimulates PKC-dependent Syk S297 phosphorylation, which is reduced by SFK/Syk/PKC inhibition and cAMP. Inhibition of Syk S297 phosphorylation coincides with enhanced Syk activation, suggesting that S297 phosphorylation represents a mechanism for feedback inhibition in human platelets.

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Zhang, Pengyu, Fiorella A. Solari, Johan W. M. Heemskerk, Marijke J. E. Kuijpers, Albert Sickmann, Ulrich Walter y Kerstin Jurk. "Differential Regulation of GPVI-Induced Btk and Syk Activation by PKC, PKA and PP2A in Human Platelets". International Journal of Molecular Sciences 24, n.º 9 (24 de abril de 2023): 7776. http://dx.doi.org/10.3390/ijms24097776.

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Bruton’s tyrosine kinase (Btk) and spleen tyrosine kinase (Syk) are major signaling proteins in human platelets that are implicated in atherothrombosis and thrombo-inflammation, but the mechanisms controlling their activities are not well understood. Previously, we showed that Syk becomes phosphorylated at S297 in glycoprotein VI (GPVI)-stimulated human platelets, which limits Syk activation. Here, we tested the hypothesis that protein kinases C (PKC) and A (PKA) and protein phosphatase 2A (PP2A) jointly regulate GPVI-induced Btk activation in platelets. The GPVI agonist convulxin caused rapid, transient Btk phosphorylation at S180 (pS180↑), Y223 and Y551, while direct PKC activation strongly increased Btk pS180 and pY551. This increase in Btk pY551 was also Src family kinase (SFK)-dependent, but surprisingly Syk-independent, pointing to an alternative mechanism of Btk phosphorylation and activation. PKC inhibition abolished convulxin-stimulated Btk pS180 and Syk pS297, but markedly increased the tyrosine phosphorylation of Syk, Btk and effector phospholipase Cγ2 (PLCγ2). PKA activation increased convulxin-induced Btk activation at Y551 but strongly suppressed Btk pS180 and Syk pS297. PP2A inhibition by okadaic acid only increased Syk pS297. Both platelet aggregation and PLCγ2 phosphorylation with convulxin stimulation were Btk-dependent, as shown by the selective Btk inhibitor acalabrutinib. Together, these results revealed in GPVI-stimulated platelets a transient Syk, Btk and PLCγ2 phosphorylation at multiple sites, which are differentially regulated by PKC, PKA or PP2A. Our work thereby demonstrated the GPVI–Syk–Btk signalosome as a tightly controlled protein kinase network, in agreement with its role in atherothrombosis.

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Xu, Rong, Rony Seger y Israel Pecht. "Cutting Edge: Extracellular Signal-Regulated Kinase Activates Syk: A New Potential Feedback Regulation of Fcε Receptor Signaling". Journal of Immunology 163, n.º 3 (1 de agosto de 1999): 1110–14. http://dx.doi.org/10.4049/jimmunol.163.3.1110.

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Abstract The protein tyrosine kinase Syk is an essential element in several cascades coupling Ag receptors to cell responses. Syk and the mitogen-activated protein kinase extracellular signal-regulated kinase 1 (ERK1) were found to form a tight complex in both resting and Ag-stimulated rat mucosal-type mast cells (rat basophilic leukemia 2H3 cell line RBL-2H3). A direct serine phosphorylation and activation of Syk by ERK was observed in in vitro experiments. Moreover the mitogen-activated protein kinase/extracellular signal-regulated protein kinase (ERK) kinase (MEK) inhibitors markedly decreased the Ag-induced phosphorylation of the tyrosyl residues of Syk and its activation as well as suppressed the degranulation of the cells. These results suggest a positive feedback regulation of Syk by ERK in the cascade coupling the type 1 Fcε receptor to the secretory response of mast cells; hence, the existence of a novel type of cross-talk between protein serine/threonine kinases and protein tyrosine kinases is suggested.

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Makhoul, Stephanie, Elena Kumm, Pengyu Zhang, Ulrich Walter y Kerstin Jurk. "The Serine/Threonine Protein Phosphatase 2A (PP2A) Regulates Syk Activity in Human Platelets". International Journal of Molecular Sciences 21, n.º 23 (25 de noviembre de 2020): 8939. http://dx.doi.org/10.3390/ijms21238939.

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Distinct membrane receptors activate platelets by Src-family-kinase (SFK)-, immunoreceptor-tyrosine-based-activation-motif (ITAM)-dependent stimulation of spleen tyrosine kinase (Syk). Recently, we reported that platelet activation via glycoprotein (GP) VI or GPIbα stimulated the well-established Syk tyrosine (Y)-phosphorylation, but also stoichiometric, transient protein kinase C (PKC)-mediated Syk serine(S)297 phosphorylation in the regulatory interdomain-B, suggesting possible feedback inhibition. The transient nature of Syk S297 phosphorylation indicated the presence of an unknown Syk pS297 protein phosphatase. In this study, we hypothesize that the S-protein phosphatase 2A (PP2A) is responsible for Syk pS297 dephosphorylation, thereby affecting Syk Y-phosphorylation and activity in human washed platelets. Using immunoblotting, we show that specific inhibition of PP2A by okadaic acid (OA) alone leads to stoichiometric Syk S297 phosphorylation, as analyzed by Zn2+-Phos-tag gels, without affecting Syk Y-phosphorylation. Pharmacological inhibition of Syk by PRT060318 or PKC by GF109203X only minimally reduced OA-induced Syk S297 phosphorylation. PP2A inhibition by OA preceding GPVI-mediated platelet activation induced by convulxin extended Syk S297 phosphorylation but inhibited Syk Y-phosphorylation. Our data demonstrate a novel biochemical and functional link between the S-protein phosphatase PP2A and the Y-protein kinase Syk in human platelets, and suggest that PP2A represents a potential enhancer of GPVI-mediated Syk activity caused by Syk pS297 dephosphorylation.

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Coates, Matthew S., Eric W. F. W. Alton, Garth W. Rapeport, Jane C. Davies y Kazuhiro Ito. "Pseudomonas aeruginosa induces p38MAP kinase-dependent IL-6 and CXCL8 release from bronchial epithelial cells via a Syk kinase pathway". PLOS ONE 16, n.º 2 (1 de febrero de 2021): e0246050. http://dx.doi.org/10.1371/journal.pone.0246050.

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Pseudomonas aeruginosa (Pa) infection is a major cause of airway inflammation in immunocompromised and cystic fibrosis (CF) patients. Mitogen-activated protein (MAP) and tyrosine kinases are integral to inflammatory responses and are therefore potential targets for novel anti-inflammatory therapies. We have determined the involvement of specific kinases in Pa-induced inflammation. The effects of kinase inhibitors against p38MAPK, MEK 1/2, JNK 1/2, Syk or c-Src, a combination of a p38MAPK with Syk inhibitor, or a novel narrow spectrum kinase inhibitor (NSKI), were evaluated against the release of the proinflammatory cytokine/chemokine, IL-6 and CXCL8 from BEAS-2B and CFBE41o- epithelial cells by Pa. Effects of a Syk inhibitor against phosphorylation of the MAPKs were also evaluated. IL-6 and CXCL8 release by Pa were significantly inhibited by p38MAPK and Syk inhibitors (p<0.05). Phosphorylation of HSP27, but not ERK or JNK, was significantly inhibited by Syk kinase inhibition. A combination of p38MAPK and Syk inhibitors showed synergy against IL-6 and CXCL8 induction and an NSKI completely inhibited IL-6 and CXCL8 at low concentrations. Pa-induced inflammation is dependent on p38MAPK primarily, and Syk partially, which is upstream of p38MAPK. The NSKI suggests that inhibiting specific combinations of kinases is a potent potential therapy for Pa-induced inflammation.

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Yan, S. R., M. Huang y G. Berton. "Signaling by adhesion in human neutrophils: activation of the p72syk tyrosine kinase and formation of protein complexes containing p72syk and Src family kinases in neutrophils spreading over fibrinogen." Journal of Immunology 158, n.º 4 (15 de febrero de 1997): 1902–10. http://dx.doi.org/10.4049/jimmunol.158.4.1902.

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Abstract Src family kinases are implicated in signaling by integrins in polymorphonuclear neutrophils (PMN). To identify proteins present in complexes with Src family kinases, we subjected p58(c-fgr) or p53/56(lyn) immunoprecipitates from Triton X-100 lysates of PMN incubated on fibrinogen-coated surfaces to in vitro kinase assays. Assays on p58(c-fgr) or p53/56(lyn) immunoprecipitates from Triton lysates of PMN induced to spread over fibrinogen in response to TNF-alpha showed that several proteins form complexes with Src family kinases and can be phosphorylated in vitro. Immunoblot analysis showed that the p72(syk) tyrosine kinase is one of these proteins. Formation of protein complexes containing Src family kinases and p72(syk) required PMN spreading because p72(syk) was not detected in p58(c-fgr) or p53/56(lyn) immunoprecipitates from PMN, which were stimulated with TNF-alpha, in suspension. In addition, induction of PMN spreading with Mn2+ in the absence of TNF-alpha promoted the formation of protein complexes containing Src family kinases and p72(syk). We also found that p72(syk)-autophosphorylating kinase activity was enhanced, and a fraction of p72(syk) was translocated to a Triton-insoluble cytoskeletal fraction in PMN induced to spread over fibrinogen by TNF-alpha or Mn2+. In vitro kinase assays on CD18 (beta 2 integrin subunit) immunoprecipitates from Triton lysates of spread PMN showed that several proteins formed complexes with CD18 and could be phosphorylated in vitro. Immunoblot analysis of CD18 immunoprecipitates allowed us to identify p72(syk) as one of these proteins. These findings show that PMN spreading is accompanied by activation of p72(syk) and formation of multimolecular complexes in which Src family kinases and p72(syk) colocalize.

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Pasquet, Jean-Max, Romain Gioia, Claire Drullion, Valerie Lagarde, Cedric Leroy, Serge Roche, Bruno Cardinaud y Francois-Xavier Mahon. "Tyrosine Kinase Proteins profiling of Nilotinib Resistant Chronic Myelogenous Leukemia Cells Unravels a Tyrosine Kinase-Mediated Bypass." Blood 114, n.º 22 (20 de noviembre de 2009): 2175. http://dx.doi.org/10.1182/blood.v114.22.2175.2175.

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Abstract Abstract 2175 Poster Board II-152 Targeting the tyrosine kinase activity of Bcr-Abl is an attractive therapeutic strategy in Chronic Myeloid Leukemia (CML) and in Bcr-Abl positive Acute Lymphoblastic Leukemia. Whereas imatinib, a selective inhibitor of Bcr-Abl tyrosine kinase, is now used in frontline therapy for CML, second generation inhibitors such as nilotinib or dasatinib have been developed for the treatment of imatinib-resistant or –intolerant disease. We have shown that one of the mechanisms of resistance to nilotinib is an increasing expression of the p53/56 Lyn kinase, both at mRNA and protein level in cell lines. This result was confirmed in vivo in nilotinib-resistant CML patients (Mahon et al. Cancer Res., 2008, 68(23):9809-16.). To elucidate Lyn mediated-nilotinib resistance, a phosphoproteomic study was performed by Stable Isotope Labelling with Amino acid in Cell culture (SILAC) which highlights the potential role of downstream tyrosine kinases. Among different candidate proteinsThe Spleen tyrosine kinase Syk and the UFO family receptor tyrosine kinase Axl were the most relevant in the nilotinib resistant cell line as compared to the sensitive counterpart. Syk hyperphosphorylation was confirmed in the nilotinib resistant cell line using western blot at least on tyrosine residues Y323 and Y525/526, two critical tyrosine residues respectively involved in Lyn-mediated Syk phosphorylation and autophosphorylation-associated Syk activation. Lyn interacts with Syk as detected in Syk immunoprecipitates in nilotinib resistant cells. Furthermore, Syk-Lyn interaction is inhibited by dasatinib suggesting the requirement of Lyn kinase activity and Syk phosphorylation. Targeting Syk expression in nilotinib resistant cells by siRNA or tyrosine kinase activity by pharmacological inhibitors leads respectively to a partial (35%) or to a full restoration of nilotinib sensitivity. Moreover, the identification of Axl by SILAC is correlated to a 9 fold increase of its level of expression in the resistant cell line and the inhibition of Axl tyrosine kinase activity decreases proliferation of both nilotinib sensitive and resistant CML cells. All together these results disclose a new pathway for tyrosine kinase inhibitors resistance in CML involving at least the two Lyn downstream tyrosine kinases Syk and Axl. Disclosures: Mahon: Amgen: Honoraria; Novartis Pharma: Consultancy, Honoraria, Research Funding; Alexion: Consultancy, Honoraria.

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MELANDER, Fredrik, Tommy ANDERSSON y Karim DIB. "Fgr but not Syk tyrosine kinase is a target for beta2 integrin-induced c-Cbl-mediated ubiquitination in adherent human neutrophils". Biochemical Journal 370, n.º 2 (1 de marzo de 2003): 687–94. http://dx.doi.org/10.1042/bj20021201.

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An early and critical event in β2 integrin signalling during neutrophil adhesion is activation of Src tyrosine kinases and Syk. In the present study, we report Src kinase-dependent β2 integrin-induced tyrosine phosphorylation of Cbl occurring in parallel with increased Cbl-associated tyrosine kinase activity. These events concurred with activation of Fgr and, surprisingly, also with dissociation of this Src tyrosine kinase from Cbl. Moreover, the presence of the Src kinase inhibitor PP1 in an in vitro assay had only a limited effect on the Cbl-associated kinase activity. These results suggest that an additional active Src-dependent tyrosine kinase associates with Cbl. The following observations imply that Syk is such a kinase: (i) β2 integrins activated Syk in a Src-dependent manner, (ii) Syk was associated with Cbl much longer than Fgr was, and (iii) the Syk inhibitor piceatannol (3,4,3′,5′-tetrahydroxy-trans-stilbene) abolished the Cbl-associated kinase activity in an in vitro assay. Effects of the mentioned interactions between these two kinases and Cbl may be related to the finding that Cbl is a ubiquitin E3 ligase. Indeed, we detected β2 integrin-induced ubiquitination of Fgr that, similar to the phosphorylation of Cbl, was abolished in cells pretreated with PP1. However, the ubiquitination of Fgr did not cause any apparent degradation of the protein. In contrast with Fgr, Syk was not modified by the E3 ligase. Thus Cbl appears to be essential in β2 integrin signalling, first by serving as a matrix for a subsequent agonist-induced signalling interaction between Fgr and Syk, and then by mediating ubiquitination of Fgr which possibly affects its interaction with Cbl.

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Jiang, Aimin, Andrew Craxton, Tomohiro Kurosaki y Edward A. Clark. "Different Protein Tyrosine Kinases Are Required for B Cell Antigen Receptor–mediated Activation of Extracellular Signal–Regulated kinase, c-Jun NH2-terminal Kinase 1, and p38 Mitogen-activated Protein Kinase". Journal of Experimental Medicine 188, n.º 7 (5 de octubre de 1998): 1297–306. http://dx.doi.org/10.1084/jem.188.7.1297.

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B cell antigen receptor (BCR) cross-linking activates three distinct families of nonreceptor protein tyrosine kinases (PTKs): src-family kinases, Syk, and Btk; these PTKs are responsible for initiating downstream events. BCR cross-linking in the chicken DT40 B cell line also activates three distinct mitogen-activated protein kinases (MAPKs): extracellular signal–regulated kinase (ERK)2, c-jun NH2-terminal kinase (JNK)1, and p38 MAPK. To dissect the functional roles of these PTKs in MAPK signaling, activation of MAPKs was examined in various PTK-deficient DT40 cells. BCR-mediated activation of ERK2, although maintained in Lyn-deficient cells, was abolished in Syk-deficient cells and partially inhibited in Btk-deficient cells, indicating that BCR-mediated ERK2 activation requires Syk and that sustained ERK2 activation requires Btk. BCR-mediated JNK1 activation was maintained in Lyn-deficient cells but abolished in both Syk- and Btk-deficient cells, suggesting that JNK1 is activated via a Syk- and Btk-dependent pathway. Consistent with this, BCR-mediated JNK1 activation was dependent on intracellular calcium and phorbol myristate acetate–sensitive protein kinase Cs. In contrast, BCR-mediated p38 MAPK activation was detected in all three PTK-deficient cells, suggesting that no single PTK is essential. However, BCR-mediated p38 MAPK activation was abolished in Lyn/Syk double deficient cells, demonstrating that either Lyn or Syk alone may be sufficient to activate p38 MAPK. Our data show that BCR-mediated MAPK activation is regulated at the level of the PTKs.

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Dangelmaier, Carol A., Patricia G. Quinter, Jianguo Jin, Alexander Y. Tsygankov, Satya P. Kunapuli y James L. Daniel. "Rapid ubiquitination of Syk following GPVI activation in platelets". Blood 105, n.º 10 (15 de mayo de 2005): 3918–24. http://dx.doi.org/10.1182/blood-2004-09-3689.

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AbstractSpleen tyrosine kinase (Syk) activation is a key intermediate step in the activation of platelets by the physiologic agonist collagen. We have found that Syk is rapidly ubiquitinated upon activation of platelets by collagen, collagen-related peptide (CRP), and convulxin. The Src family kinase inhibitors prevented Syk phosphorylation and its ubiquitination, indicating that the process is downstream of Src kinases. The ubiquitination of Syk did not cause degradation of the protein as evidenced by the lack of effect of proteasomal and lysosomal inhibitors. We separated ubiquitinated Syk from its nonubiquitinated counterpart and used an in vitro kinase assay to compare their activities. We found that the ubiquitinated Syk appeared to be about 5-fold more active. Using a phosphospecific antibody to Syk (Tyr525/Tyr526) that measures activated Syk, we found that most (60%-75%) of the active Syk is in the ubiquitinated fraction. This result explains the apparent high specific activity of ubiquitinated Syk. In c-Cbl–deficient mice, Syk is not ubiquitinated, implicating c-Cbl as the E3 ligase involved in Syk ubiquitination. Furthermore, Syk is not dephosphorylated in these mice. We propose that c-Cbl plays a regulatory role in glycoprotein VI (GPVI)/Fc receptor γ (FcRγ)-chain–dependent platelet activation through its interaction with Syk.

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Tesis sobre el tema "Kinase Syk"

Garcia, Emilien. "Rôle de la tyrosine kinase SYK dans la régulation du processus métastatique du mélanome". Thesis, Université Côte d'Azur (ComUE), 2016. http://www.theses.fr/2016AZUR4154/document.

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La progression tumorale en cancer métastatique implique la perte de fonctions oncosuppressives, comme c'est le cas dans le mélanome. Une migration cellulaire aberrante est caractéristique de la progression du mélanome. SYK (Spleen tyrosine kinase) est une tyrosine kinase cytoplasmique impliquée dans la suppression tumorale du cancer du sein et du mélanome. Dans la peau, SYK est exprimée dans les mélanocytes mais est fréquemment réprimée épigénétiquement dans le mélanome. Nous avions pu montré que cette perte était associée à un échappement de la sénescence. Qu'elle puisse réguler la migration des cellules tumorales et la formation des métastases reste peu connu. Dans mes travaux j'ai utilisé des approches gain et perte de fonction pour analyser l'effet de SYK sur les mélanomes humains et murins. Respectivement, la réexpression et l'extinction de SYK diminue et augmente la migration, l'invasion et les métastases des cellules de mélanome. L'extinction de SYK induit notamment un phénotype et une signature mésenchymateuse. Notre étude dévoile ce rôle pour SYK dans la répression d'une adhérence dépendante des intégrines, points de tractions et plateforme de signalisation de la migration, et souligne l'importance la perte de SYK dans la formation de métastases. Pour clarifier le rôle de SYK dans la progression du mélanome, j'ai généré un modèle murin de KO conditionnel de SYK spécifique des mélanocytes concomitants à une perte de Pten et de l'activation de BrafV600E. Des résultats préliminaires suggèrent que la perte de SYK n'accélère pas la formation de mélanome dans ce contexte mutationnel mais mène à une invasion plus profonde des cellules tumorales dans le derme
The progression of tumors to metastatic disease involves the loss of metastatic suppressor functions, as it is the case in melanoma. Thus, aberrant cell migration is a key feature of melanoma progression, and is required for metastasis. SYK (Spleen tyrosine kinase) is a cytoplasmic tyrosine kinase that has been implicated in tumor suppression of breast cancer and melanoma. In skin cells, SYK is found expressed in melanocytes but SYK is frequently downregulated in melanoma by epigenetic silencing. We showed previously that its loss has been associated with senescence escape. Whether it also regulates tumor cell migration and subsequent metastasis remains poorly understood. In this work we used gain- and loss-of-function approaches to analyze SYK’s effects on metastatic abilities of human and murine melanoma cells. Respectively, the reexpression or knockdown of SYK results in decreased or increased migration, invasion and metastasis of melanoma cells. Notably, SYK knockdown cells displayed a mesenchymal-like phenotype with upregulation of mesenchymal markers. Our study unveils a novel role for SYK in suppressing integrin-mediated adhesion, both a points of traction and a signaling platform during cell migration, and outlines the importance of SYK inactivation in acquisition of a metastatic phenotype. To clarify the role of SYK in melanoma formation and progression, we have generated a conditional Syk KO mouse model in melanoma based on melanocyte-specific Pten loss and BrafV600E activating mutation. Preliminary results suggest that Syk loss does not accelerate Pten/Braf-driven melanoma formation but leads to deep invasion of Braf/Pten tumor cells into the dermis

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Pechloff, Konstanze. "Conditional in vivo expression of the fusion kinase ITK-SYK". Diss., Ludwig-Maximilians-Universität München, 2013. http://nbn-resolving.de/urn:nbn:de:bvb:19-159471.

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Nys, J. "Role of the Syk tyrosine kinase in mature B cell function". Thesis, University College London (University of London), 2010. http://discovery.ucl.ac.uk/20243/.

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Signal transduction through the antigen receptor of B cells (BCR) is crucial in controlling their development and maintenance, and is also needed for B cell immune responses. Syk, a protein tyrosine kinase, has already been implicated in signalling downstream of the BCR. Mice deficient for Syk show a developmental block at the immature to mature B cell stage such that no mature B cells are generated. Thus it has not been possible to use these targeted mice to study the role of Syk in the activation of mature B cells or in antigen-driven B cell responses. To get around this, I used mice with an inducible conditional knock out (CoKO) of Syk to generate mature B cells lacking Syk. This has allowed me to study the role of Syk in mature B cell activation and its involvement in the immune response. In this work I show that B cells from Syk CoKO mice are unable to respond to BCR stimulation. I also addressed the requirement in Syk for T-dependent immune responses, looking at both primary and secondary responses. The primary response was Syk-dependent, while, surprisingly, the secondary response seems to be Syk-independent. Finally, I investigated the role of Syk downstream of TLR receptors. Unexpectedly, Syk CoKO B cells were unresponsive to TLR4 stimulation. This defect is B cell autonomous and may be due to reduced signaling through the Akt/Gsk-3/cMyc pathway, downstream of the BCR.

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Garcia, Emilien. "Rôle de la tyrosine kinase SYK dans la régulation du processus métastatique du mélanome". Electronic Thesis or Diss., Université Côte d'Azur (ComUE), 2016. http://www.theses.fr/2016AZUR4154.

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Saen, Michaël Bastien. "La tyrosine kinase Syk influence négativement la progression du cycle cellulaire à travers la phosphorylation de la kinase Cdk1". Montpellier 2, 2009. http://www.theses.fr/2009MON20200.

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La tyrosine kinase cytoplasmique Syk a longtemps été étudiée dans les cellules hématopoïétiques en tant qu'acteur de la réponse immunitaire. Notre laboratoire a montré, pour la première fois, une expression de Syk dans les cellules et tissus mammaires humains sains et faiblement tumorigéniques, alors qu'elle est absente ou peu exprimée dans les cellules et carcinomes mammaires invasifs. La transfection de Syk dans une lignée de cancer du sein fortement tumorigénique, abolit sa capacité tumorale et métastastique chez la souris athymique, conférant à Syk un rôle de suppresseur de tumeurs. Curieusement, la surexpression de Syk par transfection provoque des défauts de division cellulaire, et induit une mort cellulaire, évoquant la catastrophe mitotique. De plus notre laboratoire a montré que Syk est localisée et catalytiquement active au niveau des centrosomes, et que son expression y est régulée de façon spatio-temporelle au cours du cycle cellulaire. Néanmoins, les mécanismes moléculaires ainsi que les effecteurs de Syk responsables de son activité anti-oncogénique demeurent inconnus. Dans cette thèse nous montrons que Syk pourrait agir de façon négative sur le déroulement de la division cellulaire à travers la phosphorylation d'une protéine clef de la mitose: la kinase Cdk1. Nous avons observé que Syk interagit avec le complexe Cdk1/cycline B1 et phosphoryle Cdk1 sur différents résidus tyrosine aux centrosomes dont la tyrosine 15, connue pour influencer négativement le déroulement de la mitose. Etonnamment, la surexpression transitoire de Syk provoque une accumulation des cellules en phase G1 du cycle cellulaire. Enfin, nous démontrons que des agents anticancéreux provoquant du stress génotoxique et bloquant le cycle cellulaire, induisent la phosphorylation de Cdk1 sur tyrosine dépendant de l'activation de Syk. Ces fonctions nouvelles de Syk contribueront à une meilleure compréhension de son activité anti-oncogénique dans les cellules de cancer du sein
The non-receptor Syk tyrosine kinase has mainly been studied in haematopoietic cells in which it plays a key role in the immune-response signalling. Our laboratory demonstrated for the first time that Syk is expressed also in normal human breast cells and tissue and low-tumorigenic breast cancer cell lines, whereas its expression is low or undetectable in invasive breast carcinoma tissue and cell lines. Transfection of Syk in a highly tumorigenic breast cancer cell line suppressed its tumorigenic and metastatic capacity in athymic mice, suggesting that Syk acts as a tumour suppressor. Surprisingly, overexpression of transfected Syk provokes abnormal cell division and a non-apoptotic cell death, reminiscent of mitotic catastrophe. Furthermore, our laboratory demonstrated that Syk is localized and catalytically active at the centrosomes, in which Syk expression is controlled in a spatio-temporal manner. Nevertheless, the molecular mechanisms and the Syk effectors responsible for its anti-oncogenic activity remain unknown. In this PhD thesis, we demonstrate that Syk could negatively affect cell division through the phosphorylation of a key protein involved in the control of mitosis: the Cdk1 kinase. We observed that Syk interacts with the Cdk1/cyclin B1 complex and that it phosphorylates Cdk1 on different tyrosine residues, amongst which we identified the tyrosine 15 residue, known to negatively affect the progression of mitosis. Surprisingly, transient Syk overexpression induced an accumulation of cells in the G1 cell cycle phase. Finally, we demonstrate that anti-cancer drugs that provoke genotoxic stress and a cell cycle block induce phosphorylation of Cdk1 on tyrosine and this in a Syk activation-dependent manner. These novel aspects of Syk function will undeniably contribute to a better understanding of its onco-suppressive activity in breast cancer cells

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Schweighoffer, Edina. "The role of Syk protein tyrosine kinase in B cell development and function". Thesis, Open University, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.250493.

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Mayanglambam, Azad. "Regulation of Protein Kinases (Syk and PKC zeta) in platelets". Diss., Temple University Libraries, 2010. http://cdm16002.contentdm.oclc.org/cdm/ref/collection/p245801coll10/id/91635.

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Physiology
Ph.D.
Platelets are crucial components of the hemostatic machinery of the body. When the endothelial continuity is disrupted due to injury or atherosclerotic plaque rupture, one of the earliest responses to arrest the bleeding is the adhesion of circulating platelets to the exposed subendothelial collagen matrix. Subsequent intracellular signaling mediated downstream of various receptor systems leads to alpha IIb beta 3 activation, thromboxane generation, ADP release, etc., culminating in platelet clot or thrombus formation. The protein kinase family of enzymes mediates a significant number of these intracellular signaling events that culminate in platelet activation. These enzymes can be broadly classified into two classes- tyrosine kinases and serine/threonine kinases. Syk (spleen tyrosine kinase) is an important non-receptor tyrosine kinase present in platelets and plays an important role downstream of GPVI-FcR gamma chain receptor complex activation. We studied the effects of curcumin (diferuloylmethane), which is the active ingredient found in the herbal remedy and food spice turmeric, on the GPVI-mediated platelet activation. We have found that it significantly inhibits the kinase activity of Syk without affecting its phosphorylation. Pre-incubating the platelets with curcumin for only a minute resulted in a concentration-dependent inhibition of aggregation and secretion, with approximately 75% inhibition observed at 50 mM curcumin. Additionally, the activation-dependent phosphorylation of tyrosines 753/759 on PLC gamma2 and phosphorylation of tyrosine 191 on the transmembrane scaffold protein LAT, were inhibited (p<0.05). However, the phosphorylation of the activation loop tyrosines 525/526 on Syk and of the tyrosine 145 on intracellular adaptor molecule SLP-76 were not significantly affected. Furthermore, the inhibitory action of curcumin on the catalytic activity of Syk was independent of any of its effects on the thromboxane generation because all our studies were performed using aspirin-treated platelets. PKC zeta is an atypical member of the PKC family of serine/threonine kinases. In this study, we have confirmed that it is expressed in human platelets and is constitutively phosphorylated at the activation loop threonine 410 as well as the turn motif threonine 560, which is an autophosphorylation site. Phosphorylation at these two residues has been shown to be important for its kinase activity. Furthermore, agonist-mediated platelet aggregation under stirring condition results in dephosphorylation of the Thr410 residue, which can be prevented by blocking integrin alpha IIb beta 3 by its antagonist SC-57101 (p<0.01). The dephosphorylation of Thr410 can also be prevented by okadaic acid, a Ser/Thr protein phosphatase inhibitor, at concentrations above 100 nM. However, in PP1c gamma null mice, we did not observe any effect on the dephosphorylation, suggesting that other isoforms of PP1 or other classes of the phosphatases could be responsible for this phenomenon, at least in these knockout mice. The basal phosphorylation of Thr560, however, remained unaffected by agonist stimulation, integrin activation, integrin blockade, okadaic acid treatment and in the PP1c gamma null mice. It can be speculated that PKC zeta may be constitutively active under basal resting conditions and acts as a negative regulator of platelet activation or functional responses. The Thr560 autophosphorylation signal alone may not be sufficient to sustain its full enzymatic activity.
Temple University--Theses

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Le, Roux Delphine. "Régulation des interactions entre endosomes et cytosquelette pendant la présentation antigénique : un rôle pour la protéine tyrosine kinase Syk". Paris 6, 2006. http://www.theses.fr/2006PA066472.

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Fargier, Guillaume. "Comportement dynamique au centrosome de la tyrosine kinase Syk, un nouveau suppresseur de tumeur dans le sein : étude par microscopie à haute résolution". Montpellier 2, 2009. http://www.theses.fr/2009MON20241.

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Très étudiée pour son rôle dans la signalisation des immuno-récepteurs, la tyrosine kinase Syk agirait comme suppresseur de tumeur et de métastase dans l'épithélium mammaire. Le mécanisme de cette activité anti-oncogénique reste inconnu. En plus de la localisation cytoplasmique, Syk est localisée aux extensions membranaires et au centrosome où elle est catalytiquement active, avec une variation de la concentration au cours du cycle cellulaire. Les localisations de mutants de Syk dans la cellule dépendent du type du site tyrosine muté d'une part, et les effecteurs potentiels de Syk reconnus par analyse protéomique d'autre part, font penser à un code de phosphorylation qui dépendrait du résidu tyrosine activé pour cibler la kinase à des sites sub-cellulaires différents. Afin de caractériser la dynamique des échanges de Syk entre compartiments subcellulaires et surtout dans le centrosome, nous avons employé des approches d'imagerie à haute résolution sur cellules vivantes de cancer du sein transfectées par des formes sauvage ou mutantes de DsRed-Syk. L'approche de FRAP et l'utilisation d'une chimère photo-activable (PA-GFP-Syk) montrent que Syk est recrutée activement au centrosome, avec un τ de 18,54 ± 3,63 sec. L'utilisation d'inhibiteurs de polymérisation de microtubules ou du moteur moléculaire dynéine/dynactine, la visualisation par TIRF des déplacements de particules de Syk à la base des cellules, la co-localisation par immunofluorescence, l'observation confirmée par modélisation d'une dérive directionnelle de PA-GFP-Syk après activation, tout indique que cytosquelette microtubulaire et moteur moléculaire sont nécessaires pour le recrutement de Syk au centrosome
Initially studied for its role in immunoreceptor-mediated downstream signalling, the tyrosine kinase Syk acts like a tumor and metastasis suppressor within breast cancer cells. The mechanism of its anti-oncogenic activity remains, however, to be identified. In addition to its cytoplasmic localization, Syk is also visualized at plasma membrane extensions and at the centrosome in which it exhibits a catalytic activity and is tightly regulated along the cell cycle. Considering both the action sites of potential effectors as identified by proteomic approach and differently targeted DsRed-Syk following the tyrosine residue mutated, we hypothesize a phosphorylation code targeting the kinase at different sub-cellular compartments depending on the tyrosine residue activated. In order to determine whether a dynamic exchange occurs between the subcellular compartments, we applied different imaging techniques on living breast cancer cells transiently expressing wild-type and mutant fluorescent Syk chimeras. Fluorescence Recovery After Photobleaching (FRAP) with DsRed-Syk and photoactivatable GFP-Syk clearly evidenced rapid exchanges at the centrosomes with a recruitment τ of 18,54 ± 3,63 sec. Treatments affecting the microtubule skeleton or the molecular motor dynein, TIRF imaging of Syk clusters, antibody co-localization, directional drift of activated PA-GFP-Syk corroborated by mathematical modelling, together show that the tubulin cytoskeleton and the microtubule motor dynein/dynactin are necessary for Syk recruitment at the centrosome

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Yamamoto, Noriyuki. "Development of a selective inhibitor for Syk tyrosine kinase and investigation of its pharmacological activities". 京都大学 (Kyoto University), 2003. http://hdl.handle.net/2433/148369.

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Libros sobre el tema "Kinase Syk"

Chen, Linyun. Exploring the structure and functions of Sak, a gene encoding a serine/threonine kinase. Ottawa: National Library of Canada, 1996.

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Senin, Viktor. Syn faraona: [fantasticheskai︠a︡ povestʹ]. Sankt-Peterburg: Amfora, 2006.

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Thom, James Alexander. Panther in the sky. New York: Ballantine Books, 1990.

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Thom, James Alexander. Panther in the sky: A Novel. New York: Ballantine Books, 1989.

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Kanbe, Mamoru. Sora no woto: Sound of the sky. Hackensack, NJ: Bayview Entertainment, 2013.

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Nowacki, Bronisław. Przemysł I: Syn Władysława Odonica, książę wielkopolski, 1220/1221-1257. Poznań: Wydawn. WBP, 2003.

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Miller, Linda Lael. Big Sky River: The Parable (Big Sky) series. 2^a ed. Don Mills, Canada: Harlequin HQN, 2012.

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Kim, Sang-hŏn. Tongnye suchʻo. Ŭirye munhae sok. Kogŭm sangnye idongŭi. Pusan Kwangyŏksi: Minjok Munhwa, 2008.

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Golightly, Walton. AmaZulu: Being the many divers adventures of the Induna & the boy among the People of the Sky in the time of Shaka kaSenzangakhona, King of Kings. Cape Town: Kwela Books, 2007.

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Fleischmann, Roy. Signalling pathway inhibitors. Oxford University Press, 2013. http://dx.doi.org/10.1093/med/9780199642489.003.0081.

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Oral, small-molecule signalling pathway inhibitors, including ones that inhibit the JAK and SyK pathways, are currently in development for the treatment of rheumatoid arthritis (RA). Tofacitinib is an orally administered small-molecule inhibitor that targets the intracellular Janus kinase 3 and 1 (JAK1/3) molecules to a greater extent than JAK2 while baricitinib (formerly INCB028050) predominantly inhibits JAK1/2. Many of the proinflammatory cytokines implicated in the pathogenesis of RA utilize cell signalling that involves the JAK-STAT pathways and therefore inhibition of JAK-STAT signalling, by targeting multiple RA-associated cytokine pathways, has the potential to simultaneously reduce inflammation, cellular activation, and proliferation of key immune cells. Fostamatinib disodium is an orally available inhibitor of spleen tyrosine kinase (SyK), which is a cytoplasmic tyrosine kinase that is an important mediator of immunoreceptor signalling in mast cells, macrophages, neutrophils, and B cells. Interruption of SyK signalling may interrupt production of tumour necrosis factor (TNF) and metalloproteinase and therefore affect RA disease activity. Tofacitinib has been investigated in multiple phase 2 and phase 3 trials which have investigated its efficacy (clinical, functional, and radiographic) and safety in patients who have failed disease-modifying anti-inflammatory drugs (DMARDs) as monotherapy or in combination with DMARDs, compared to an inhibitor of tumour necrosis factor alpha (TNFα‎) and in patients who have failed TNFα‎ inhibitors. The efficacy of fostamatinib and baricitinib has been investigated in phase 2 trials; both are in large phase 3 clinical programmes. Each of these medications has demonstrated efficacy; their safety profile has been shown to be different from each other and from currently approved biological agents. This chapter discusses what is currently known and understood about their efficacy and safety.

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Capítulos de libros sobre el tema "Kinase Syk"

Mueller, Susette C. y Peter J. Coopman. "Syk Tyrosine Kinase". En Encyclopedia of Cancer, 1–5. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-27841-9_5616-3.

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Mueller, Susette C. y Peter J. Coopman. "Syk Tyrosine Kinase". En Encyclopedia of Cancer, 4424–27. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-662-46875-3_5616.

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Denyer, Jane y Vipul Patel. "Syk kinase inhibitors". En New Drugs and Targets for Asthma and COPD, 283–88. Basel: KARGER, 2010. http://dx.doi.org/10.1159/000320832.

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Mueller, Susette C. y Peter J. Coopman. "Syk Tyrosine Kinase". En Encyclopedia of Cancer, 3589–92. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16483-5_5616.

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Deckert, Marcel y Sophie Tartare-Deckert. "Senescence Escape in Melanoma: Role of Spleen Tyrosine Kinase SYK". En Tumor Dormancy, Quiescence, and Senescence, Volume 2, 227–37. Dordrecht: Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-7726-2_22.

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Siraganian, Reuben P., Juan Zhang y Teruaki Kimura. "Regulation and Function of Protein Tyrosine Kinase Syk in FcεRI-Mediated Signaling". En Signal Transduction in Mast Cells and Basophils, 115–33. New York, NY: Springer New York, 1999. http://dx.doi.org/10.1007/978-1-4612-2154-8_10.

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Pavan, Isadora Carolina Betim, Fernando Riback Silva, Ana Paula Morelli y Fernando Moreira Simabuco. "S6K (S6 Kinase)". En Encyclopedia of Signaling Molecules, 4814–23. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101816.

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Pavan, Isadora Carolina Betim, Fernando Riback Silva, Ana Paula Morelli y Fernando Moreira Simabuco. "S6K (S6 Kinase)". En Encyclopedia of Signaling Molecules, 1–10. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_101816-1.

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Della-Morte, David, Donatella Pastore, Barbara Capuani, Francesca Pacifici y Davide Lauro. "SGK-1 (Serum- and Glucocorticoid-Inducible Kinase-1)". En Encyclopedia of Signaling Molecules, 4914–22. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101807.

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Della-Morte, David, Donatella Pastore, Barbara Capuani, Francesca Pacifici y Davide Lauro. "SGK-1 (Serum- and Glucocorticoid-Inducible Kinase-1)". En Encyclopedia of Signaling Molecules, 1–9. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_101807-1.

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Actas de conferencias sobre el tema "Kinase Syk"

Tuemmler, Conny, Gianina Dumitriu, Julia Cserna, Ugo L. Moens, Per Kogner, John Inge Johnsen y Baldur Sveinbjørnsson. "Abstract 2465: Spleen tyrosine kinase (SYK) in neuroblastoma tumorigenesis". En Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-2465.

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Lallah Missimana, Jeanne Pierrette, Magnus Diller, Rebecca Hasseli, Stefan Rehart, Ulf Müller-Ladner y Elena Neumann. "THU0042 EFFECT OF SPLEEN TYROSIN KINASE (SYK)-INHIBITORS ON RHEUMATOID ARTHRITIS SYNOVIAL FIBROBLASTS". En Annual European Congress of Rheumatology, EULAR 2019, Madrid, 12–15 June 2019. BMJ Publishing Group Ltd and European League Against Rheumatism, 2019. http://dx.doi.org/10.1136/annrheumdis-2019-eular.4865.

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Gaillard, Stephanie, Alexander Stoeck, Ben Davidson, Tian-Li Wang y Ie-Ming Shih. "Abstract 815: The role of spleen tyrosine kinase (SYK) in paclitaxel resistant ovarian cancer". En Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-815.

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Bijli, Kaiser M., Fabeha Fazal, Mohammad Minhajuddin y Arshad Rahman. "Protein Tyrosine Kinase Syk Regulates ICAM-1 Expression And PMN Sequestration In Mouse Lungs". En American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a2671.

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Danen, Erik. "Abstract 4117: Syk is a candidate kinase target for the treatment of advanced prostate cancer". En Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-4117.

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Saen, Michael, Anne Morel, Romain Larive, Serge Urbach, Patrick Jouin, May C. Morris, Vjekoslav Dulic, Paul Mangeat y Peter J. Coopman. "Abstract 2959: The Syk tyrosine kinase negatively affects cell cycle progression through phosphorylation of the Cdk1 kinase in response to DNA damage". En Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-2959.

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Sappal, Jessica J., Matthew Theisen, Zhongmin Xiang, Stephen Tirrell, Rudy Christmas, Jie Yu, Mengkun Zhang y Karuppiah Kannan. "Abstract 3844: TAK-659, a SYK kinase inhibitor, demonstrates preclinical antitumor activity in solid tumor models". En Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-3844.

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Kim, Seon Uk, Hyun Jung Yoo, Shin Eui Kang, Ji Soo Park, Ra Ham Kim, Jin Kyun Park, Eun Young Lee y Yeong Wook Song. "AB0126 ANTI-INFLAMMATORY EFFECTS OF SPLEEN TYROSINE KINASE (SYK) INHIBITOR, PICEATANNOL, ON FIBROBLAST-LIKE SYNOVIOCYTE IN RHEUMATOID ARTHRITIS". En Annual European Congress of Rheumatology, EULAR 2019, Madrid, 12–15 June 2019. BMJ Publishing Group Ltd and European League Against Rheumatism, 2019. http://dx.doi.org/10.1136/annrheumdis-2019-eular.6696.

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Coates, MS, K. Ito, EWFW Alton y JC Davies. "M3 Pseudomonas aeruginosa induces inflammation in bronchial epithelial cells via the p38 MAP and Syk tyrosine kinase pathways". En British Thoracic Society Winter Meeting 2019, QEII Centre, Broad Sanctuary, Westminster, London SW1P 3EE, 4 to 6 December 2019, Programme and Abstracts. BMJ Publishing Group Ltd and British Thoracic Society, 2019. http://dx.doi.org/10.1136/thorax-2019-btsabstracts2019.411.

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Hua, Kevin L., Michelle Pan, Minoo Rafati y Anurag Singh. "Abstract A02: SYK kinase inhibition causes autophagy pathway activation via suppression of mTORC1 in KRAS-mutant pancreatic cancer cells". En Abstracts: AACR Special Conference on Targeting PI3K/mTOR Signaling; November 30-December 8, 2018; Boston, MA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1557-3125.pi3k-mtor18-a02.

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Informes sobre el tema "Kinase Syk"

Meyer, Erik. Night skies data report: Photometric assessment of night sky quality at Sequoia and Kings Canyon National Parks. National Park Service, 2025. https://doi.org/10.36967/2308859.

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This report characterizes night sky conditions in Sequoia and Kings Canyon National Parks (SEKI) using measurements made in the park unit and models of regional conditions based on satellite data. Calibrated night sky imagery was obtained to characterize the night sky at 5 sites. These ground-based observations were collected on 8 nights from 2004-06-12 to 2009-07-21. Satellite data from 2022 was used to create a map of predicted night sky conditions in and around the park. The sky overhead remains pristine with an average zenith brightness of 21.63 mag/arcsec2. We estimate more than 91% of stars were visible throughout the data collection period, providing an excellent opportunity to observe the natural night sky from the park during cloudless, new moon conditions. The whole sky over SEKI is 18%–74% (mean=53%) brighter than average natural levels, indicating impaired dark sky conditions on average. In SEKI, we classified the sky as Bortle Class 4: rural/suburban transition, based on the visibility of astronomical objects. The average naked eye limiting magnitude (NELM) is 6.75, which is approaching near pristine under average conditions. Our Sky Quality Meter (SQM) measurements average 21.74 mag/arcsec2, indicating the zenith is darker than what we can accurately measure with an SQM. Fairly obvious light-pollution domes are apparent over population centers in several directions. The zodiacal light is clearly evident but doesn’t even extend halfway to the zenith at the beginning or end of twilight. The Milky Way well above the horizon is still impressive but lacks all but the most obvious structure. The main impacts on SEKI’s night sky quality were the light domes from Los Angeles, Fresno, Visalia, Bakersfield, Porterville, Clovis, Tulare, Las Vegas, and Hanford. These light domes were observed along the horizon, with a few nearing the natural brightness of the Milky Way.

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Mohler, James L. Dependency on Src-Family Kinases (SFK) for Recurrence of Androgen-Independent Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, agosto de 2012. http://dx.doi.org/10.21236/ada566915.

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Patumraj, Suthiluk y Sheepsumon Viboolvorakul. Protective effects of exercise training against vascular and neuronal dysfunction in aging brain. Department of Physiology, Faculty of Medicine, Chulalongkorn University, 2019. https://doi.org/10.58837/chula.res.2019.11.

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During advancing age, reduction of microvessels in the brain contributes insufficiency tissue perfusion. Mounting evidence indicates that microvascular deterioration in aged brain relates to oxidative stress. Nuclear factor erythroid-related factor 2 (Nrf2) plays an important role in cellular antioxidant defense. Regular physical exercise is well known to have beneficial effect to brain health, including promoted blood flow and augmented angiogenesis, in aging individuals. However, the underlying mechanism of regular physical exercise in improvement of brain microvascular density during advancing age has not been fully elucidated. This study aimed to investigate the underlying mechanism of exercise training in improvement of microvascular density associated with PI3K/Akt/Nrf2 pathway in aged rat brain. Male Wistar rats were divided into three groups; sedentary-young (SY), sedentary-age (SA) and trained-age (TA). Exercise program included swimming exercise for eight weeks. Expression of CD31 (as indicator of microvascular density) and Nrf2 were evaluated by immunohistochemistry staining. Activity of Nrf2, protein levels of phosphatidylinositol-4,5-biphosphate 3-kinase (PI3K) and phosphorylated-protein kinase B (p-Akt) in isolated brain microvessels were assessed by immunoassay. Aging (SA) induced significant reduction of brain microvascular density and expression of Nrf2, PI3K and p-Akt proteins, as well as Nrf2 activity, comparing to those of SY group. The eight-week exercise training significantly improved brain microvascular density and upregulated Nrf2, PI3K and p-Akt proteins as well as activated Nrf2 activity, than that of the age group without exercise (SA). In conclusion, exercise training can improve brain microvascular deterioration associated with PI3K/Akt/Nrf2 pathway in aging rats.

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Coplin, David, Isaac Barash y Shulamit Manulis. Role of Proteins Secreted by the Hrp-Pathways of Erwinia stewartii and E. herbicola pv. gypsophilae in Eliciting Water-Soaking Symptoms and Initiating Galls. United States Department of Agriculture, junio de 2001. http://dx.doi.org/10.32747/2001.7580675.bard.

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Many bacterial pathogens of plants can inject pathogenicity proteins into host cells using a specialized type III secretion system encoded by hrpgenes. This system deliver effector proteins, into plant cells that function in both susceptible and resistant interactions. We have found that the virulence of Erwinia stewartii(Es; syn. Pantoea stewartii) and Erwinia herbicola pv. gypsophilae (Ehg, syn. Pantoea agglomerans), which cause Stewart's wilt of corn and galls on Gypsophila, respectively, depends on hrpgenes. The major objectives of this project were: To increase expression of hrpgenes in order to identify secreted proteins; to identify genes for proteins secreted by the type-III systems and determine if they are required for pathogenicity; and to determine if the secreted proteins can function within eukaryotic cells. We found that transcription of the hrp and effector genes in Es and Ehg is controlled by at least four genes that constitute a regulatory cascade. Environmental and/or physiological signaling appears to be mediated by the HrpX/HrpY two component system, with HrpX functioning as a sensor-kinase and HrpY as a response regulator. HrpYupregulateshrpS, which encodes a transcriptional enhancer. HrpS then activates hrpL, which encodes an alternate sigma factor that recognizes "hrp boxes". All of the regulatory genes are essential for pathogenicity, except HrpX, which appears only to be required for induction of the HR in tobacco by Es. In elucidating this regulatory pathway in both species, we made a number of significant new discoveries. HrpX is unusual for a sensor-kinase because it is cytoplasmic and contains PAS domains, which may sense the redox state of the bacterium. In Es, a novel methyl-accepting protein may function upstream of hrpY and repress hrp gene expression in planta. The esaIR quorum sensing system in Es represses hrp gene expression in Es in response to cell-density. We have discovered six new type III effector proteins in these species, one of which (DspE in Ehg and WtsE in Es) is common to both pathogens. In addition, Es wtsG, which is a homolog of an avrPpiB from P. syringae pv. pisi, and an Ehg ORF, which is a homolog of P. syringae pv. phaseolicola AvrPphD, were both demonstrated to encode virulence proteins. Two plasmidborne, Ehg Hop proteins, HsvG and PthG, are required for infection of gypsophilia, but interestingly, PthG also acts as an Avr elicitor in beets. Using a calmodulin-dependent adenylate cyclase (cyaA) reporter gene, we were successful in demonstrating that an HsvG-CyaA fusion protein can be transferred into human HeLa cells by the type-III system of enteropathogenic E. coli. This is a highly significant accomplishment because it is the first direct demonstration that an effector protein from a plant pathogenic bacterium is capable of being translocated into a eukaryotic cell by a type-III secretion system. Ehg is considered a limiting factor in Gypsophila production in Israel and Stewart’s Wilt is a serious disease in the Eastern and North Central USA, especially on sweet corn in epidemic years. We believe that our basic research on the characterization of type III virulence effectors should enable future identification of their receptors in plant cells. This may lead to novel approaches for genetically engineering resistant plants by modifying their receptors or inactivating effectors and thus blocking the induction of the susceptible response. Alternatively, hrp gene regulation might also provide a target for plant produced compounds that interfere with recognition of the host by the pathogen. Such strategies would be broadly applicable to a wide range of serious bacterial diseases on many crops throughout the USA and Israel.

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Morrison, Mark y Joshuah Miron. Molecular-Based Analysis of Cellulose Binding Proteins Involved with Adherence to Cellulose by Ruminococcus albus. United States Department of Agriculture, noviembre de 2000. http://dx.doi.org/10.32747/2000.7695844.bard.

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At the beginning of this project, it was clear that R. albus adhered tightly to cellulose and its efficient degradation of this polysaccharide was dependent on micromolar concentrations of phenylacetic acid (PAA) and phenylpropionic acid (PPA). The objectives for our research were: i) to identify how many different kinds of cellulose binding proteins are produced by Ruminococcus albus; ii) to isolate and clone the genes encoding some of these proteins from the same bacterium; iii) to determine where these various proteins were located and; iv) quantify the relative importance of these proteins in affecting the rate and extent to which the bacterium becomes attached to cellulose. BARD support has facilitated a number of breakthroughs relevant to our fundamental understanding of the adhesion process. First, R. albus possesses multiple mechanisms for adhesion to cellulose. The P.I.'s laboratory has discovered a novel cellulose-binding protein (CbpC) that belongs to the Pil-protein family, and in particular, the type 4 fimbrial proteins. We have also obtained genetic and biochemical evidence demonstrating that, in addition to CbpC-mediated adhesion, R. albus also produces a cellulosome-like complex for adhesion. These breakthroughs resulted from the isolation (in Israel and the US) of spontaneously arising mutants of R. albus strains SY3 and 8, which were completely or partially defective in adhesion to cellulose, respectively. While the SY3 mutant strain was incapable of growth with cellulose as the sole carbon source, the strain 8 mutants showed varying abilities to degrade and grow with cellulose. Biochemical and gene cloning experiments have been used in Israel and the US, respectively, to identify what are believed to be key components of a cellulosome. This combination of cellulose adhesion mechanisms has not been identified previously in any bacterium. Second, differential display, reverse transcription polymerase chain reaction (DD RT-PCR) has been developed for use with R. albus. A major limitation to cellulose research has been the intractability of cellulolytic bacteria to genetic manipulation by techniques such as transposon mutagenesis and gene displacement. The P.I.'s successfully developed DD RT- PCR, which expanded the scope of our research beyond the original objectives of the project, and a subset of the transcripts conditionally expressed in response to PAA and PPA have been identified and characterized. Third, proteins immunochemically related to the CbpC protein of R. albus 8 are present in other R. albus strains and F. intestinalis, Western immunoblots have been used to examine additional strains of R. albus, as well as other cellulolytic bacteria of ruminant origin, for production of proteins immunochemically related to the CbpC protein. The results of these experiments showed that R. albus strains SY3, 7 and B199 all possess a protein of ~25 kDa which cross-reacts with polyclonal anti-CbpC antiserum. Several strains of Butyrivibrio fibrisolvens, Ruminococcus flavefaciens strains C- 94 and FD-1, and Fibrobacter succinogenes S85 produced no proteins that cross-react with the same antiserum. Surprisingly though, F. intestinalis strain DR7 does possess a protein(s) of relatively large molecular mass (~200 kDa) that was strongly cross-reactive with the anti- CbpC antiserum. Scientifically, our studies have helped expand the scope of our fundamental understanding of adhesion mechanisms in cellulose-degrading bacteria, and validated the use of RNA-based techniques to examine physiological responses in bacteria that are nor amenable to genetic manipulations. Because efficient fiber hydrolysis by many anaerobic bacteria requires both tight adhesion to substrate and a stable cellulosome, we believe our findings are also the first step in providing the resources needed to achieve our long-term goal of increasing fiber digestibility in animals.

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