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Relevant bibliographies by topics / Mast cells Protein-tyrosine kinase

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Academic literature on the topic 'Mast cells Protein-tyrosine kinase'

Author: Grafiati

Published: 4 June 2021

Last updated: 3 February 2022

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Journal articles on the topic "Mast cells Protein-tyrosine kinase"

1

Kitaura, Jiro, Koichi Asai, Mari Maeda-Yamamoto, Yuko Kawakami, Ushio Kikkawa, and Toshiaki Kawakami. "Akt-Dependent Cytokine Production in Mast Cells." Journal of Experimental Medicine 192, no. 5 (September 5, 2000): 729–40. http://dx.doi.org/10.1084/jem.192.5.729.

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Cross-linking of FcεRI induces the activation of three protein tyrosine kinases, Lyn, Syk, and Bruton's tyrosine kinase (Btk), leading to the secretion of a panel of proinflammatory mediators from mast cells. This study showed phosphorylation at Ser-473 and enzymatic activation of Akt/protein kinase B, the crucial survival kinase, upon FcεRI stimulation in mouse mast cells. Phosphorylation of Akt is regulated positively by Btk and Syk and negatively by Lyn. Akt in turn can regulate positively the transcriptional activity of interleukin (IL)-2 and tumor necrosis factor (TNF)-α promoters. Transcription from the nuclear factor κB (NF-κB), nuclear factor of activated T cells (NF-AT), and activator protein 1 (AP-1) sites within these promoters is under the control of Akt activity. Accordingly, the signaling pathway involving IκB-α, a cytoplasmic protein that binds NF-κB and inhibits its nuclear translocation, appears to be regulated by Akt in mast cells. Catalytic activity of glycogen synthase kinase (GSK)-3β, a serine/threonine kinase that phosphorylates NF-AT and promotes its nuclear export, seems to be inhibited by Akt. Importantly, Akt regulates the production and secretion of IL-2 and TNF-α in FcεRI-stimulated mast cells. Altogether, these results revealed a novel function of Akt in transcriptional activation of cytokine genes via NF-κB, NF-AT, and AP-1 that contributes to the production of cytokines.

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2

Nechushtan, Hovav, Michael Leitges, Cellina Cohen, Gillian Kay, and Ehud Razin. "Inhibition of degranulation and interleukin-6 production in mast cells derived from mice deficient in protein kinase Cβ." Blood 95, no. 5 (March 1, 2000): 1752–57. http://dx.doi.org/10.1182/blood.v95.5.1752.005k18_1752_1757.

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The antigen-mediated activation of mast cells by means of IgE antibodies bound to the cell surface leads to direct interactions between FcɛRI receptor cytoplasmic domains and various intracellular proteins. These interactions initiate diverse signal-transduction pathways, and the activation of these pathways results in the immediate release of proinflammatory agents. A delayed response also occurs and includes the release of various cytokines. It is clear that the activation of kinases is a requirement for the exocytosis observed in mast cells. In addition to the tyrosine phosphorylation of the affected system by soluble tyrosine kinases, activity of protein kinase C (PKC) results in serine or threonine phosphorylation of multiple protein substrates. In this study, we found that mast cells derived from PKCβ-deficient mice produce less interleukin 6 in response to IgE-Ag. The inhibition of exocytosis in the PKCβ-deficient mast cells occurred whether the stimuli were due to the aggregation of the mast cell surface FcɛRI or to the calcium ionophore, ionomycin. However, no significant changes were observed in the proliferative response of the mast cells to interleukin 3 (IL-3) or in their apoptotic rate after IL-3 depletion.

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Tam, See-Ying, Mindy Tsai, Masao Yamaguchi, Koji Yano, Joseph H. Butterfield, and Stephen J. Galli. "Expression of Functional TrkA Receptor Tyrosine Kinase in the HMC-1 Human Mast Cell Line and in Human Mast Cells." Blood 90, no. 5 (September 1, 1997): 1807–20. http://dx.doi.org/10.1182/blood.v90.5.1807.

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Abstract Nerve growth factor (NGF ) can influence mast cell development and function in murine rodents by interacting with its receptors on mast cells. We now report the identification of mRNA transcripts of full-length tyrosine kinase-containing trkA, trkB, and trkC neurotrophin receptor genes in HMC-1 human mast cell leukemia cells. Although HMC-1 cells lacked p75 mRNA, they expressed transcripts for the exon-lacking splice variant of trkA (trkAI), truncated trkB (trkB.T1), and truncated trkC. By flow cytometry, HMC-1 cells exhibited expression of TrkA, TrkB, and TrkC receptor proteins containing full-length tyrosine kinase domains. NGF stimulation of HMC-1 cells induced tyrosine phosphorylation of TrkA protein, increased expression of the early response genes c-fos and NGF1-A, and activation of ERK-mitogen–activated protein (MAP) kinase, results which indicate that TrkA receptors in HMC-1 cells are fully functional. Highly purified populations of human lung mast cells expressed mRNAs for trkA, trkB and trkC, whereas preparations of human umbilical cord blood-derived mast cells expressed mRNAs for trkA and trkC, but not trkB. Moreover, preparations of human umbilical cord blood-derived immature mast cells not only expressed mRNA transcript and protein for TrkA, but exhibited significantly higher numbers of chymase-positive cells after the addition of NGF to their culture medium for 3 weeks. In addition, HMC-1 cells expressed mRNAs for NGF, brain-derived neurotrophic factor (BDNF ), and neurotrophin-3 (NT-3), the cognate ligands for TrkA, TrkB, and TrkC, whereas NGF and BDNF transcripts were detectable in human umbilical cord blood mast cell preparations. Taken together, our findings show that human mast cells express a functional TrkA receptor tyrosine kinase and indicate that NGF may be able to promote certain aspects of mast cell development and/or maturation in humans. Our studies also raise the possibility that human mast cells may represent a potential source for neurotrophins.

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Dastych, Jaroslaw, Dennis Taub, Mary C. Hardison, and Dean D. Metcalfe. "Tyrosine kinase-deficient Wvc-kit induces mast cell adhesion and chemotaxis." American Journal of Physiology-Cell Physiology 275, no. 5 (November 1, 1998): C1291—C1299. http://dx.doi.org/10.1152/ajpcell.1998.275.5.c1291.

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W/Wvmice are deficient in tissue mast cells, and mast cells cultured from these mice do not proliferate in response to the c-kit ligand, stem cell factor (SCF). In this paper, we report that mouse bone marrow cultured mast cells derived from W/Wvmice do adhere to fibronectin in the presence of SCF and exhibit chemotaxis to SCF, and we explore this model for the understanding of c-kit-mediated signaling pathways. Both in vitro and in vivo (in intact cells) phosphorylation experiments demonstrated a low residual level of W/Wvc-kit protein phosphorylation. SCF-induced responses in W/Wvmast cells were abolished by the tyrosine kinase inhibitor herbimycin A and by the phospatidylinositol 3-kinase (PI 3-kinase) inhibitor wortmannin but were not affected by protein kinase C inhibitors. These observations are consistent with the conclusions that Wvc-kit initiates a signaling process that is PI 3-kinase dependent and that mutated Wvc-kit retains the ability to initiate mast cell adhesion and migration.

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Craig, Andrew W. B., and Peter A. Greer. "Fer Kinase Is Required for Sustained p38 Kinase Activation and Maximal Chemotaxis of Activated Mast Cells." Molecular and Cellular Biology 22, no. 18 (September 15, 2002): 6363–74. http://dx.doi.org/10.1128/mcb.22.18.6363-6374.2002.

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ABSTRACT Mast cells play important roles in inflammation and immunity and express the high-affinity immunoglobulin E receptor (FcεRI) and the receptor protein-tyrosine kinase Kit. Aggregation of FcεRI via antigen binding elicits signals leading to the release of preformed inflammatory mediators as well as de novo-synthesized lipid mediators and cytokines and to elevated cell adhesion and migration. Here, we report that in mouse bone marrow-derived mast cells, Fer kinase is activated downstream of activated FcεRI and activated Kit receptor, and this activation is abolished in cells homozygous for a kinase-inactivating mutation in Fer (fer DR/DR ). Interestingly, the highly related Fps/Fes kinase is also activated upon FcεRI aggregation. This report represents the first description of a common signaling pathway activating Fer and Fps/Fes. While Fer-deficient cells showed similar activation of the Erk mitogen-activated protein (MAP) kinases, p38 MAP kinase activation was less sustained than that in wild-type cells. Although no major defects were observed in degranulation, leukotriene biosynthesis, and cytokine secretion, Fer-deficient cells displayed increased adhesion and decreased motility upon activation of FcεRI and the Kit receptor. The restoration of Fer kinase activity in fer DR/DR mast cells resulted in prolonged p38 kinase activation and increased antigen-mediated cell migration of sensitized mast cells. Thus, Fer is required for maximal p38 kinase activation to promote the chemotaxis of activated mast cells. Further studies with mast cells derived from fps/fes-deficient mice will be required to provide insight into the role of Fps/Fes in mast cell activation.

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6

Kawakami, Y., L. Yao, T. Miura, S. Tsukada, O. N. Witte, and T. Kawakami. "Tyrosine phosphorylation and activation of Bruton tyrosine kinase upon Fc epsilon RI cross-linking." Molecular and Cellular Biology 14, no. 8 (August 1994): 5108–13. http://dx.doi.org/10.1128/mcb.14.8.5108.

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Tyrosine phosphorylation of several cellular proteins is one of the earliest signaling events induced by cross-linking of the high-affinity receptor for immunoglobulin E (Fc epsilon RI) on mast cells or basophils. Tyrosine kinases activated during this process include the Src family kinases, Lyn, c-Yes, and c-Src, and members of another subfamily, Syk and PTK72 (identical or highly related to Syk). Recently, some of us described two novel tyrosine kinases, Emb and Emt, whose expression was limited to subsets of hematopoietic cells, including mast cells. Emb turned out to be identical to Btk, a gene product defective in human X-linked agammaglobulinemia and in X-linked immunodeficient (xid) mice. Here we report that Fc epsilon RI cross-linking induced rapid phosphorylation on tyrosine, serine, and threonine residues and activation of Btk in mouse bone marrow-derived mast cells. A small fraction of Btk translocated from the cytosol to the membrane compartment following receptor cross-linking. Tyrosine phosphorylation of Btk was not induced by either a Ca2+ ionophore (A23187), phorbol 12-myristate 13-acetate, or a combination of the two reagents. Co-immunoprecipitation between Btk and receptor subunit beta or gamma was not detected. The data collectively suggest that Btk is not associated with Fc epsilon but that its activation takes place prior to protein kinase C activation and plays a novel role in the Fc epsilon RI signaling pathway.

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Kawakami, Y., L. Yao, T. Miura, S. Tsukada, O. N. Witte, and T. Kawakami. "Tyrosine phosphorylation and activation of Bruton tyrosine kinase upon Fc epsilon RI cross-linking." Molecular and Cellular Biology 14, no. 8 (August 1994): 5108–13. http://dx.doi.org/10.1128/mcb.14.8.5108-5113.1994.

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Tyrosine phosphorylation of several cellular proteins is one of the earliest signaling events induced by cross-linking of the high-affinity receptor for immunoglobulin E (Fc epsilon RI) on mast cells or basophils. Tyrosine kinases activated during this process include the Src family kinases, Lyn, c-Yes, and c-Src, and members of another subfamily, Syk and PTK72 (identical or highly related to Syk). Recently, some of us described two novel tyrosine kinases, Emb and Emt, whose expression was limited to subsets of hematopoietic cells, including mast cells. Emb turned out to be identical to Btk, a gene product defective in human X-linked agammaglobulinemia and in X-linked immunodeficient (xid) mice. Here we report that Fc epsilon RI cross-linking induced rapid phosphorylation on tyrosine, serine, and threonine residues and activation of Btk in mouse bone marrow-derived mast cells. A small fraction of Btk translocated from the cytosol to the membrane compartment following receptor cross-linking. Tyrosine phosphorylation of Btk was not induced by either a Ca2+ ionophore (A23187), phorbol 12-myristate 13-acetate, or a combination of the two reagents. Co-immunoprecipitation between Btk and receptor subunit beta or gamma was not detected. The data collectively suggest that Btk is not associated with Fc epsilon but that its activation takes place prior to protein kinase C activation and plays a novel role in the Fc epsilon RI signaling pathway.

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8

Kinashi, T., JA Escobedo, LT Williams, K. Takatsu, and TA Springer. "Receptor tyrosine kinase stimulates cell-matrix adhesion by phosphatidylinositol 3 kinase and phospholipase C-gamma 1 pathways." Blood 86, no. 6 (September 15, 1995): 2086–90. http://dx.doi.org/10.1182/blood.v86.6.2086.bloodjournal8662086.

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Receptor tyrosine kinases are known to be important in growth and differentiation. We have recently found that c-kit, the tyrosine kinase receptor for steel factor, also regulates cell-matrix adhesion. Because Steel factor helps regulate cell migration and localization, this may be an important biologic function. Integrin adhesiveness is regulated within minutes by c-kit. The signaling pathways for tyrosine kinase stimulation of integrin adhesiveness and their relation to pathways that regulate growth and differentiation over much longer time periods remain uncharacterized. We have studied the effector pathways by which receptor tyrosine kinases regulate cell-matrix adhesion using wild-type and mutant forms of the platelet-derived growth factor (PDGF) receptor, which is closely related to c-kit. The PDGF receptor expressed in mast cells is as potent as c-kit in stimulating adhesion to fibronectin. We show that induction of adhesion is regulated through two independent pathways of phosphatidylinositol 3 kinase (PI3K) and phospholipase C- gamma 1 (PLC gamma)-protein kinase C by elimination of autophosphorylation sites required for activation of PI3K and PLC gamma or in combination with downregulation of protein kinase C or wortmannin. By contrast, a receptor mutated in both the PI3K and PLC gamma association sites can still stimulate mast cell growth, indicating a crucial role of these effector molecules in regulating adhesion rather than cell growth.

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9

Rottapel, R., M. Reedijk, D. E. Williams, S. D. Lyman, D. M. Anderson, T. Pawson, and A. Bernstein. "The Steel/W transduction pathway: kit autophosphorylation and its association with a unique subset of cytoplasmic signaling proteins is induced by the Steel factor." Molecular and Cellular Biology 11, no. 6 (June 1991): 3043–51. http://dx.doi.org/10.1128/mcb.11.6.3043.

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The W/c-kit and Steel loci respectively encode a receptor tyrosine kinase (Kit) and its extracellular ligand, Steel factor, which are essential for the development of hematopoietic, melanocyte, and germ cell lineages in the mouse. To determine the biochemical basis of the Steel/W developmental pathway, we have investigated the response of the Kit tyrosine kinase and several potential cytoplasmic targets to stimulation with Steel in mast cells derived from normal and mutant W mice. In normal mast cells, Steel induces Kit to autophosphorylate on tyrosine and bind to phosphatidylinositol 3'-kinase (PI3K) and phospholipase C-gamma 1 but not detectably to Ras GTPase-activating protein. Additionally, we present evidence that Kit tyrosine phosphorylation acts as a switch to promote complex formation with PI3K. In mast cells from mice homozygous for the W42 mutant allele, Kit is not tyrosine phosphorylated and fails to bind PI3K following Steel stimulation. In contrast, in the transformed mast cell line P815, Kit is constitutively phosphorylated and binds to PI3K in the absence of ligand. These results suggest that Kit autophosphorylation and its physical association with a unique subset of cytoplasmic signaling proteins are critical for mammalian development.

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Rottapel, R., M. Reedijk, D. E. Williams, S. D. Lyman, D. M. Anderson, T. Pawson, and A. Bernstein. "The Steel/W transduction pathway: kit autophosphorylation and its association with a unique subset of cytoplasmic signaling proteins is induced by the Steel factor." Molecular and Cellular Biology 11, no. 6 (June 1991): 3043–51. http://dx.doi.org/10.1128/mcb.11.6.3043-3051.1991.

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The W/c-kit and Steel loci respectively encode a receptor tyrosine kinase (Kit) and its extracellular ligand, Steel factor, which are essential for the development of hematopoietic, melanocyte, and germ cell lineages in the mouse. To determine the biochemical basis of the Steel/W developmental pathway, we have investigated the response of the Kit tyrosine kinase and several potential cytoplasmic targets to stimulation with Steel in mast cells derived from normal and mutant W mice. In normal mast cells, Steel induces Kit to autophosphorylate on tyrosine and bind to phosphatidylinositol 3'-kinase (PI3K) and phospholipase C-gamma 1 but not detectably to Ras GTPase-activating protein. Additionally, we present evidence that Kit tyrosine phosphorylation acts as a switch to promote complex formation with PI3K. In mast cells from mice homozygous for the W42 mutant allele, Kit is not tyrosine phosphorylated and fails to bind PI3K following Steel stimulation. In contrast, in the transformed mast cell line P815, Kit is constitutively phosphorylated and binds to PI3K in the absence of ligand. These results suggest that Kit autophosphorylation and its physical association with a unique subset of cytoplasmic signaling proteins are critical for mammalian development.

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Dissertations / Theses on the topic "Mast cells Protein-tyrosine kinase"

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Lin, Tzu-yin. "The world according to mast cells the role of Kit in normal and neoplastic canine mast cells /." Columbus, Ohio : Ohio State University, 2007. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1189098916.

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Bennett, Haley Lorraine Garvan Institute of Medical Research Faculty of Medicine UNSW. "Co-operation between the docking protein GAB2 and the protein tyrosine kinase src in human mammary epithelial cells." Awarded by:University of New South Wales, 2008. http://handle.unsw.edu.au/1959.4/39486.

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The Gab2 docking protein is a target of several oncogenic protein tyrosine kinases and potentiates activation of the Ras/extracellular signal regulated kinase and phosphatidylinositol 3-kinase (PI3-kinase) pathways. The prototypical member of the Src family of protein tyrosine kinases, c-Src, phosphorylates Gab2 and both proteins are overexpressed in breast cancers. However, whether overexpression of these two proteins contributes to mammary tumourigenesis had not been previously investigated. Pharmacological inhibition of c-Src in breast cancer cell lines reduced Gab2 tyrosine phosphorylation while overexpression of these two proteins increased this effect, demonstrating a contribution of c-Src to Gab2 tyrosine phosphorylation in breast cancer cells. The biological effects of Gab2 and c-Src overexpression were determined in a three-dimensional cell culture model using the human mammary epithelial cell line MCF-10A. When cultured on a basement membrane, MCF10A cells form acini that model mammary lobules in vivo. Overexpression of Gab2 in MCF10As conferred increased acinar size and independence of the morphogenetic program from exogenous EGF. While overexpression of c-Src alone did not affect acinar morphogenesis, it potentiated the EGF-independent acinar growth induced by Gab2 overexpression. As enhanced c-Src kinase activity is often observed in breast cancer, the effect of Gab2 co-expression with active Src constructs was next determined. Expression of v-Src or c-SrcY527F altered acinar morphology and the resulting structures were categorised as spheroidal, discohesive or dispersed, according to the degree of phenotypic disruption. Gab2 co-expression shifted the proportion of structures towards the dispersed phenotype. This shift reflects a negative role for Gab2 at adherens junctions in the context of active Src expression, as in monolayer cells Gab2 significantly decreased E-cadherin-based adhesive strength without altering the surface expression of this adhesion molecule. Furthermore, Gab2 associated with the E-cadherin complex. The ability of Gab2 to weaken the strength of cell-cell contacts in active Src-expressing cells may be due to enhanced activation of PI3-kinase signalling at adherens junctions, as the potentiating effects of Gab2 in both monolayer and three-dimensional cultures were dependent upon Gab2 recruitment of the p85 subunit of PI3-kinase. Finally, Gab2 increased migration and invasion of v-Src-expressing cells in transwell assays, however these effects were p85-independent. This is the first study to demonstrate Gab2 co-operation with various forms of Src to augment proliferative, invasive and migratory signals, as well as revealing a novel mechanism whereby Gab2 may promote metastatic spread. This study thus demonstrates multiple roles for Gab2 in contributing to breast cancer progression.

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Zhang, Deyong, and 張德勇. "The regulation of cardiac potassium channels by protein tyrosine kinases." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2008. http://hub.hku.hk/bib/B41508294.

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Zhang, Deyong. "The regulation of cardiac potassium channels by protein tyrosine kinases." Click to view the E-thesis via HKUTO, 2008. http://sunzi.lib.hku.hk/hkuto/record/B41508294.

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Ekman, Niklas. "The Bmx tyrosine kinase : a signal mediator in hematopoietic and endothelial/epithelial cells." Helsinki : University of Helsinki, 2003. http://ethesis.helsinki.fi/julkaisut/mat/bioti/vk/ekman/.

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Jiang, Liying. "Exposure of endothelial cells to shear stress stimulates protein tryosine phosphorylation." Thesis, Georgia Institute of Technology, 1996. http://hdl.handle.net/1853/25421.

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Edling, Charlotte. "Receptor tyrosine kinase c-Kit signalling in hematopoietic progenitor cells." Doctoral thesis, Umeå : Umeå University, 2006. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-888.

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8

Gavériaux, Claire. "Etude de l'interaction entre l'immunoglobuline e et son recepteur de forte affinite : mise au point d'un nouvel essai immunoenzymatique sur cellules, le celisa, importance de la n-glycosylation et de l'activation de la proteine kinase c dans l'expresion fonctionnelle de ce recepteur." Université Louis Pasteur (Strasbourg) (1971-2008), 1988. http://www.theses.fr/1988STR13014.

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9

Heinonen, Juhana E. "Molecular dissection of Bruton's tyrosine kinase signaling in hematopoietic cells using RNAi /." Stockholm : Karolinska institutet, 2007. http://diss.kib.ki.se/2007/978-91-7357-320-7/.

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Kerner, James David. "The significance of Bruton tyrosine kinase in multiple stages of B lymphopoiesis /." Thesis, Connect to this title online; UW restricted, 1996. http://hdl.handle.net/1773/8347.

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Books on the topic "Mast cells Protein-tyrosine kinase"

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Schmidt, Holger. NMR-Lösungsstruktur der humanen Hck SH3-Domäne im Komplex mit einem artifiziellen, hochoffinen Peptid-Liganden. Jülich: Forschungszentrum Jülich, Zentralbibliothek, 2006.

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Danielian, Sylvia. Protéines tyrosine kinases et signalisation cellulaire: Le modèle des lymphocytes T. Paris: Editions INSERM, 1993.

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Tran, Thi Tuyen. Analyse der Bindungsspezifität der humanen Lck-SH3-Domäne anhand artifizieller und physiologischer Peptid-Liganden und strukturelle Charakterisierung dieser Peptide im Komplex mit SH3-Domänen. Jülich: Forschungszentrum Jülich, Zentralbibliothek, 2005.

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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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Murayama, Kaoru. Purification and identification of a 100 kDa protein, which is tyrosine-phosphorylated by EGF stimulation in SFME cells. 1997.

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Book chapters on the topic "Mast cells Protein-tyrosine kinase"

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Kawakami, Toshiaki, Libo Yao, and Yuko Kawakami. "Tec Family Protein Tyrosine Kinases and Their Interaction with Protein Kinase C." In Signal Transduction in Mast Cells and Basophils, 274–85. New York, NY: Springer New York, 1999. http://dx.doi.org/10.1007/978-1-4612-2154-8_19.

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Siraganian, Reuben P., Juan Zhang, and Teruaki Kimura. "Regulation and Function of Protein Tyrosine Kinase Syk in FcεRI-Mediated Signaling." In 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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Swann, Patrick G., Sandra Odom, and Juan Rivera. "Protein Kinase C and Early Mast Cell Signals." In Signal Transduction in Mast Cells and Basophils, 152–70. New York, NY: Springer New York, 1999. http://dx.doi.org/10.1007/978-1-4612-2154-8_12.

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Geldman, Alexander, and Catherine J. Pallen. "Protein Tyrosine Phosphatases in Mast Cell Signaling." In Mast Cells, 269–86. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-1568-2_17.

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Benhamou, Marc. "FcεRI-Induced Protein Tyrosine Phosphorylation." In IgE Receptor (FcεRI) Function in Mast Cells and Basophils, 33–54. Berlin, Heidelberg: Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-662-22022-1_3.

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Swieter, Mark. "Protein Tyrosine Phosphatases in Signaling Through the FcεRI on Mast Cells and Basophils." In IgE Receptor (FcεRI) Function in Mast Cells and Basophils, 127–37. Berlin, Heidelberg: Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-662-22022-1_7.

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Jimenez de Asua, L., and M. Goin. "Prostaglandin F2α (PGF2α) Triggers Protein Kinase C (PKC) and Tyrosine Kinase Activity in Cultured Mammalian Cells." In Advances in Experimental Medicine and Biology, 531–38. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4615-5325-0_72.

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Lindschau, C., H. Haller, P. Quass, and A. Distler. "Downregulation of protein kinase C is associated with phenotypic changes and enhanced proliferation of vascular smooth muscle cells." In Tyrosine Phosphorylation/Dephosphorylation and Downstream Signalling, 223–26. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-78247-3_27.

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Hemmer, W., M. Skarli, H. M. Eppenberger, and T. Wallimann. "Phosphorylation of Creatine Kinase in Myogenic Cells: Effects of Okadaic Acid and other Agents Affecting Cellular Protein Phosphorylation." In Tyrosine Phosphorylation/Dephosphorylation and Downstream Signalling, 235–40. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-78247-3_30.

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Beaven, Michael A., and Tatiana Kassessinoff. "Role of Phospholipases, Protein Kinases and Calcium in FcεRI-Induced Secretion." In IgE Receptor (FcεRI) Function in Mast Cells and Basophils, 55–73. Berlin, Heidelberg: Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-662-22022-1_4.

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Conference papers on the topic "Mast cells Protein-tyrosine kinase"

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WU, LONG-MEI, KAZUO UEDA, YUJI HIRANO, TETSUSHI FURUKAWA, and MASAYASU HIRAOKA. "HERG POTASSIUM CHANNEL IS REGULATED BY PROTEIN TYROSINE KINASE (PTK) IN HUMAN EMBRYONIC KIDNEY CELLS." In Proceedings of the 31st International Congress on Electrocardiology. WORLD SCIENTIFIC, 2005. http://dx.doi.org/10.1142/9789812702234_0009.

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Day, Evan K., and Matthew J. Lazzara. "Abstract B28: Mitogen-activated protein kinase-driven Sprouty2 expression mediates resistance to receptor tyrosine kinase-targeted therapeutics in glioblastoma cells." In Abstracts: Fourth AACR International Conference on Frontiers in Basic Cancer Research; October 23-26, 2015; Philadelphia, PA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.fbcr15-b28.

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Day, Evan K., and Matthew J. Lazzara. "Abstract 2111: Mitogen-activated protein kinase-driven Sprouty2 expression mediates resistance to receptor tyrosine kinase-targeted therapeutics in glioblastoma cells." In 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.am2016-2111.

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Irie, HY, SH Park, I. Katsyv, W. Zhang, and A. Nayak. "Abstract P3-04-13: Protein tyrosine kinase 6 (PTK6) promotes survival of endocrine therapy-resistant ER+ breast cancer cells." In Abstracts: 2016 San Antonio Breast Cancer Symposium; December 6-10, 2016; San Antonio, Texas. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.sabcs16-p3-04-13.

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Yu, Shuai, He Huang, Anton Iliuk, Wen-Horng Wang, Weiguo Andy Tao, Carol B. Post, and Robert L. Geahlen. "Abstract 542: Syk inhibits the activity of protein kinase A by phosphorylating tyrosine 330 of the catalytic subunit in breast cancer cells." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-542.

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Chakedis, Jeffery M., Randall French, Michele Babicky, Dawn Jaquish, Haleigh Howard, Evangeline Mose, Jaclyn Miyamoto, Zakk Walterscheid, Patrick Holman, and Andrew M. Lowy. "Abstract A72: Protein isoforms of the RON tyrosine kinase receptor transform human pancreatic ductal epithelial cells and induce acinar to ductal metaplasia." In Abstracts: AACR Special Conference on Pancreatic Cancer: Innovations in Research and Treatment; May 18-21, 2014; New Orleans, LA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.panca2014-a72.

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Mohamed, JS, and AM Boriek. "Stretch-Activated RhoA/ROCK Signaling Regulates TGF-beta1 Expression and Its Promoter Activity Via Protein-Tyrosine Kinase and Phosphatidylinositol 3-Kinase Dependent Pathway in Airway Smooth Muscle Cells." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a5608.

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Hayashi, Yujiro, Michael R. Bardsley, Yoshitaka Toyomasu, Takahiro Taguchi, Brian P. Rubin, Monique Carter, Abhijit Ramachandran, and Tamas Ordog. "Abstract 1035: Crenolanib, a highly selective platelet-derived growth factor receptor α/β (PDGFRA/B) tyrosine kinase inhibitor, destabilizes ETV1 protein inKIT-mutant gastrointestinal stromal tumor (GIST) cells." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-1035.

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Paolo, Julie A. Di, Astrid Clarke, Hong Rong, and Emma Rousseau. "Abstract 4205: Mass-spectroscopy phosphorylation profiling identified differential activation of signaling molecules via spleen tyrosine kinase in B-cell receptor signaling and stromal cell stimulation in DLBCL and CLL cells that are inhibited by GS-9973." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-4205.

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Kedei, Noemi, Sudipto Das, Thorkell Andresson, and Peter M. Blumberg. "Abstract 215: Characterization by mass spectrometry of protein kinase C substrates differentially phosphorylated in LNCaP cells in response to phorbol ester and bryostatin 1 treatment." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-215.

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