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Relevant bibliographies by topics / Rac1 signalling

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Academic literature on the topic 'Rac1 signalling'

Author: Grafiati

Published: 10 January 2023

Last updated: 29 January 2023

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Journal articles on the topic "Rac1 signalling"

1

Whalley, Katherine. "RAC1 signalling remodels dendrites." Nature Reviews Neuroscience 13, no. 6 (May 10, 2012): 361. http://dx.doi.org/10.1038/nrn3261.

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Payapilly, Aishwarya, and Angeliki Malliri. "Compartmentalisation of RAC1 signalling." Current Opinion in Cell Biology 54 (October 2018): 50–56. http://dx.doi.org/10.1016/j.ceb.2018.04.009.

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Takenaka, Nobuyuki, Yukio Sumi, Keiko Matsuda, Junko Fujita, Tetsuya Hosooka, Tetsuya Noguchi, Atsu Aiba, and Takaya Satoh. "Role for RalA downstream of Rac1 in skeletal muscle insulin signalling." Biochemical Journal 469, no. 3 (July 23, 2015): 445–54. http://dx.doi.org/10.1042/bj20150218.

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The small GTPase RalA is required for Rac1-mediated glucose uptake and activated by Rac1 in mouse skeletal muscle fibres. This might be the first demonstration of the involvement of RalA in Rac1-mediated insulin signalling in mature skeletal muscle.

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Dilasser, Florian, Lindsay Rose, Dorian Hassoun, Martin Klein, Morgane Rousselle, Carole Brosseau, Christophe Guignabert, et al. "Essential role of smooth muscle Rac1 in severe asthma-associated airway remodelling." Thorax 76, no. 4 (February 4, 2021): 326–34. http://dx.doi.org/10.1136/thoraxjnl-2020-216271.

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BackgroundSevere asthma is a chronic lung disease characterised by inflammation, airway hyperresponsiveness (AHR) and airway remodelling. The molecular mechanisms underlying uncontrolled airway smooth muscle cell (aSMC) proliferation involved in pulmonary remodelling are still largely unknown. Small G proteins of the Rho family (RhoA, Rac1 and Cdc42) are key regulators of smooth muscle functions and we recently demonstrated that Rac1 is activated in aSMC from allergic mice. The objective of this study was to assess the role of Rac1 in severe asthma-associated airway remodelling.Methods and resultsImmunofluorescence analysis in human bronchial biopsies revealed an increased Rac1 activity in aSMC from patients with severe asthma compared with control subjects. Inhibition of Rac1 by EHT1864 showed that Rac1 signalling controlled human aSMC proliferation induced by mitogenic stimuli through the signal transducer and activator of transcription 3 (STAT3) signalling pathway. In vivo, specific deletion of Rac1 in SMC or pharmacological inhibition of Rac1 by nebulisation of NSC23766 prevented AHR and aSMC hyperplasia in a mouse model of severe asthma. Moreover, the Rac1 inhibitor prevented goblet cell hyperplasia and epithelial cell hypertrophy whereas treatment with corticosteroids had less effect. Nebulisation of NSC23766 also decreased eosinophil accumulation in the bronchoalveolar lavage of asthmatic mice.ConclusionThis study demonstrates that Rac1 is overactive in the airways of patients with severe asthma and is essential for aSMC proliferation. It also provides evidence that Rac1 is causally involved in AHR and airway remodelling. Rac1 may represent as an interesting target for treating both AHR and airway remodelling of patients with severe asthma.

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Fan, Minghua, Yongping Xu, Fanzhen Hong, Xiaolin Gao, Gang Xin, Haijie Hong, Lihua Dong, and Xingbo Zhao. "Rac1/β-Catenin Signalling Pathway Contributes to Trophoblast Cell Invasion by Targeting Snail and MMP9." Cellular Physiology and Biochemistry 38, no. 4 (2016): 1319–32. http://dx.doi.org/10.1159/000443076.

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Background/Aims: Preeclampsia is an idiopathic and serious complication during gestation in which placental trophoblast cells differentiate into several functional subtypes, including highly invasive extravillous trophoblasts (EVTs). Although the cause and pathogenesis of preeclampsia have remained unclear, numerous studies have suggested that the inadequacy of EVT invasion leads to imperfect uterine spiral artery remodelling, which plays a crucial role in the development of preeclampsia. Rac1, or Ras-related C3 botulinum toxin substrate 1, was found to be a key regulator of the migration, invasion uand apoptosis of various tumour cells. Because EVTs share similar invasive and migratory biological behaviours with malignant cells, this study aimed to determine whether the Rac1 signalling pathway affects trophoblast invasion and is thus involved in the pathogenesis of preeclampsia. Methods: We measured the activity of Rac1 and its downstream targets, β-catenin, Snail and MMP9 in placental tissues from patients experiencing a normal pregnancy and those with preeclampsia. Furthermore, we treated HTR-8/SVneo cells with a shRNA Rac1 vector and the β-catenin inhibitor IWP-2 and explored Rac1 signalling pathway activation as well as the effects of Snail and β-catenin on trophoblast invasion. Results: In placental samples from patients experiencing a normal pregnancy and those with preeclampsia, active Rac1 levels and MMP9 protein and mRNA levels were significantly decreased in term pregnancy samples compared to early pregnancy samples. Lower levels were found in preeclampsia samples than in normal term pregnancy samples, and these levels significantly declined in severe preeclampsia samples compared with mild preeclampsia samples. Further analyses demonstrated that both Rac1 shRNA and the β-catenin inhibitor significantly suppressed MMP9 and Snail activation in trophoblasts, thus impairing trophoblast invasion. Notably, silencing Rac1 down-regulated the expression of β-catenin in HTR-8/SVneo cells, demonstrating that β-catenin is a downstream effector of Rac1 in trophoblast invasion. Conclusion: Our data suggest that Rac1-mediated activation of β-catenin might regulate Snail and MMP9 expression subsequently promoting trophoblast invasion in pregnancy.

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Tkachuk, Natalia, Hermann Haller, Inna Dumler, and Ioulia Kiian. "Urokinase-induced migration of human vascular smooth muscle cells requires coupling of the small GTPases RhoA and Rac1 to the Tyk2/PI3-K signalling pathway." Thrombosis and Haemostasis 89, no. 05 (2003): 904–14. http://dx.doi.org/10.1055/s-0037-1613478.

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SummaryUrokinase-type plasminogen activator (uPA) facilitates cell migration by localizing proteolisys on the cell surface and by inducing intracellular signalling pathways. In human vascular smooth muscle cell (VSMC) uPA stimulates migration via the uPA receptor (uPAR) signalling complex containing the Janus kinase Tyk2 and phosphatidylinositol 3-kinase (PI3-K). We report that active GTP-bound forms of small GTPases RhoA and Rac1, but not Cdc42, are directly associated with Tyk2 and PI3-K in an uPA/uPAR-dependent fashion. Endogenous RhoA, but not Rac1 or Cdc42, was significantly activated in response to uPA. RhoA activation was abolished by cell treatment with two unrelated, structurally distinct, specific inhibitors of PI3-K, wortmannin, and LY294002. Downstream of RhoA, phosphorylation of myosin light chain (MLC) was dramatically upregulated by uPA in a Rho kinase- and PI3-K-dependent manner. Thus, selective Rho kinase inhibitor Y27632 and PI3-K inhibitors wortmannin and LY294002 prevented the uPA-induced stimulation of MLC phosphorylation. Rho kinase inhibition also decreased uPA-stimulated VSMC migration as observed in a Boyden chamber. VSMC immunocytochemical staining demonstrated redistribution of RhoA and Rac1 active forms to the newly formed leading edge of migrating cell. VSMC microinjection with antibodies to either Rho or Rac1 decreased uPA-stimulated cell migration, indicating the involvement of both GTPases in the migration process. Our results provide evidence that the small GTPases RhoA and Rac1, together with Rho kinase, are necessary to mediate the uPA/uPAR-directed migration via the Tyk2/PI3-K signalling complex in human VSMC.

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Neagoe, Raluca A. I., Elizabeth E. Gardiner, David Stegner, Bernhard Nieswandt, Steve P. Watson, and Natalie S. Poulter. "Rac Inhibition Causes Impaired GPVI Signalling in Human Platelets through GPVI Shedding and Reduction in PLCγ2 Phosphorylation." International Journal of Molecular Sciences 23, no. 7 (March 29, 2022): 3746. http://dx.doi.org/10.3390/ijms23073746.

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Rac1 is a small Rho GTPase that is activated in platelets upon stimulation with various ligands, including collagen and thrombin, which are ligands for the glycoprotein VI (GPVI) receptor and the protease-activated receptors, respectively. Rac1-deficient murine platelets have impaired lamellipodia formation, aggregation, and reduced PLCγ2 activation, but not phosphorylation. The objective of our study is to investigate the role of Rac1 in GPVI-dependent human platelet activation and downstream signalling. Therefore, we used human platelets stimulated using GPVI agonists (collagen and collagen-related peptide) in the presence of the Rac1-specific inhibitor EHT1864 and analysed platelet activation, aggregation, spreading, protein phosphorylation, and GPVI clustering and shedding. We observed that in human platelets, the inhibition of Rac1 by EHT1864 had no significant effect on GPVI clustering on collagen fibres but decreased the ability of platelets to spread or aggregate in response to GPVI agonists. Additionally, in contrast to what was observed in murine Rac1-deficient platelets, EHT1864 enhanced GPVI shedding in platelets and reduced the phosphorylation levels of PLCγ2 following GPVI activation. In conclusion, Rac1 activity is required for both human and murine platelet activation in response to GPVI-ligands, but Rac1’s mode of action differs between the two species.

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Williams, M. J. "Rac1 signalling in the Drosophila larval cellular immune response." Journal of Cell Science 119, no. 10 (May 15, 2006): 2015–24. http://dx.doi.org/10.1242/jcs.02920.

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Moshfegh, Yasmin, Jose Javier Bravo-Cordero, Veronika Miskolci, John Condeelis, and Louis Hodgson. "A Trio–Rac1–Pak1 signalling axis drives invadopodia disassembly." Nature Cell Biology 16, no. 6 (May 25, 2014): 571–83. http://dx.doi.org/10.1038/ncb2972.

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Chiu, Tim T., Thomas E. Jensen, Lykke Sylow, Erik A. Richter, and Amira Klip. "Rac1 signalling towards GLUT4/glucose uptake in skeletal muscle." Cellular Signalling 23, no. 10 (October 2011): 1546–54. http://dx.doi.org/10.1016/j.cellsig.2011.05.022.

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More sources

Dissertations / Theses on the topic "Rac1 signalling"

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Quist, Sven Roy. "Role of Rac1 signalling in epidermal tumour formation." Thesis, University of Cambridge, 2014. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.708007.

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Al-Abri, Abdulrahim. "Investigating the effect of PIP4K2a overexpression in insulin signalling in L6 myotubes." Thesis, University of Manchester, 2018. https://www.research.manchester.ac.uk/portal/en/theses/investigating-the-effect-of-pip4k2a-overexpression-in-insulin-signalling-in-l6-myotubes(1dd2d1dd-c765-4830-9b66-cf32a64d7de9).html.

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Insulin signalling is an essential process in humans by which the level of plasma glucose is maintained within the physiologically healthy range. Insulin activates the phosphoinositide 3 kinase (PI3K) signalling pathway that generates the phospholipid messenger PtdIns(3,4,5)P3, which in turn enhances the activity of two important proteins, AKT and Rac1. This then leads to increase the presence of the glucose transporter 4 (GLUT4) at the plasma membrane that enhances the intake of glucose, particularly in skeletal muscle cells and adipocytes. Insulin signalling also triggers interconversion of several other phosphoinositides (PIs) which play pivotal roles in different steps of glucose regulation. PtdIns5P is an important PI that is robustly increased after insulin treatment in the skeletal muscle cell line, L6 myotubes. Many of PtdIns5P`s functions are not fully understood. To gain more knowledge of the role of PtdIns5P in insulin signalling in muscle cells, the PtdIns5P kinase phosphatidylinositol-5-phosphate 4-kinase a (PIP4K2a) was over-expressed in L6 myotubes as a way of removing PtdIns5P, and the consequences in insulin signalling were studied. Although PtdIns5P is converted by PIP4K2a to PtdIns(4,5)P2 which is a precursor of the potent PI PtdIns(3,4,5)P3, previous studies revealed that the increase in PtdIns(3,4,5)P3 induced by insulin in control cells is diminished in cells overexpressing PIP4K2a, for unknown reasons. Additionally, although the phosphorylation of the serine/threonine protein kinase AKT was not affected in these L6 cells, glucose uptake was attenuated. The current study investigates the possible causes of attenuating glucose uptake in PIP4K overexpressing myotubes by examining the small GTPase Rac1 which plays an important role in the cytoskeleton re-arrangement that is necessary for GLUT4 translocation. Furthermore, the possible roles of PI phosphatases that may cause the disturbance on the levels of PIs in response to insulin were evaluated. Additionally, the potential role of PtdIns5P in Rac1 activation in L6 myotubes was further investigated by delivering synthetic PtdIns5P using a carrier-based delivery approach. The results showed that the attenuation of glucose uptake documented in previous studies occurred as a result of a defect in the process of translocating GLUT4 from intracellular storage to the plasma membrane. Rac1 activity was significantly reduced in cells expressing PIP4K2a. Quantifying the level of PIs suggested that PIP4K2a expression increases the removal of PtdIns(3,4,5)P3 by the PI 5-phosphatase, SKIP. Silencing the expression of SKIP by siRNA restored the level of PtdIns(3,4,5)P3 but Rac1 activity and the attenuation GLUT4 translocation were not rescued possibly as a result of removing PtdIns5P by PIP4K2a. On the other hand, exogenous delivery of PtdIns5P in L6 myotubes activates both Rac1 and GLUT4 translocation in the absence of insulin. However, activating GLUT4 translocation by the exogenous PtdIns5P requires PI3K activity since redistribution of GLUT4 to the plasma membrane is inhibited by the PI3K inhibitor, wortmannin. Removing PtdIns5P reduces Rac1 activity and stimulates SKIP that inhibits PtdIns(3,4,5)P3 increase which attenuates GLUT4 translocation and hence glucose uptake. These results emphasise the critical role played by PtdIns5P which seems to serve as a regulator of insulin signalling, both directly and/or by regulating other enzymes involved in the metabolism of PIs.

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Schenck, Annette. "CYFIP, a protein family implicated in neuronal connectivity, links Rac1 GTPase signalling to the fragile X mental retardation protein." Université Louis Pasteur (Strasbourg) (1971-2008), 2003. http://www.theses.fr/2003STR13175.

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Le syndrome de l'X Fragile, qui constitue la forme la plus fréquente de retard mental héréditaire, est du à l'absence de FMRP, une protéine de liaison à l'ARN qui régulerait la traduction au niveau synaptique. Afin de mieux comprendre le role de FMRP, nous avons réalisé un criblage double-hybride dans la levure pour identifier certains de ses interacteurs. Deux protéines ont été isolées, CYFIP1 et CYFIP2 (Cytoplasmic FMRP Interacting Proteins 1/2). Ces deux protéines cytoplasmiques sont hautement homologues mais interagissent différement avec les deux autres protéines de la famille FXR, FXR1P et FXR2P. Le site de liaison à CYFIP recouvre le site d'homo- et d'hétérodimérisation de FMRP, suggérant que la liaison à CYFIP pourrait moduler l'activité de FMRP. D'autre part, l'interaction entre CYFIP1 et Rac1 a été démontrée précédemment. Rac1, une protéine de la famille des Rho GTPase, est un des principaux régulateurs de la réorganisation du cytosquelette d'actine et joue un role clé dans la maturation et la maintenance des épines dendritiques, structures synaptiques riches en actine anormalement développées chez les patients X-Fragile et dans les souris invalidées pour FMRP. De nombreux gènes des voies Rho/Rac étant impliqués dans des retards mentaux, Rac1, CYFIP1 et FMRP pourraient participer à une voie commune contrôlant la morphogénèse synaptique et le fonctionnement cognitif. Pour valider cette hypothèse in vivo, nous avons choisi Drosophila melanogaster comme organisme modèle. Nous avons découvert que CYFIP y est très exprimé dans le système nerveux embryonnaire, et s'accumule notamment dans les axones centraux et aux jonctions neuro-musculaires (JNM). Des mutations de CYFIP causent des défauts de croissance, de ramification et de connexion des axones et conduisent à une morphologie anormale des synapses des JNM. Ainsi, l'absence de CYFIP provoque des défauts similaires à ceux précedemment décrits chez les mutants dFMR1 et/ou dRac1. L'analyse des interactions génétiques et biochimiques entre ces trois protéines suggère que, lorsque la voie est activée, dRac1 inhibe CYFIP qui régule à son tour négativement dFMR1
Fragile X Syndrome is the most frequent form of hereditary mental retardation and caused by the absence of FMRP, an RNA binding protein that seems to regulate local protein translation at synapses. To better understand the physiological function of FMRP, we conducted a yeast two-hybrid screen to determine interacting proteins. We identified CYFIP1 and CYFIP2 (Cytoplasmic FMRP Interacting Proteins 1/2), two highly homologous cytoplasmic proteins, which show a different pattern of interaction with the two FMRP-related proteins FXR1P and FXR2P. The CYFIP binding site of FMRP overlaps with its homo- and heteromerisation domain, suggesting that binding to CYFIP may modulate FMRP function. Importantly, CYFIP1 has been previously reported to interact with Rac1. Rac1, a Rho GTPase, is a key regulator of actin cytoskeleton remodelling with a well-established role in maturation and maintenance of dendritic spines, which are actin-rich synaptic structures that are abnormally developed in Fragile X patients and FMRP null mice. Since several genes of Rac/Rho signalling pathways are implicated in mental retardation, our work suggested that Rac1, CYFIP and FMRP work in a common pathway determining synapse morphogenesis and cognitive function. To address this hypothesis in vivo, we have chosen the fruitfly Drosophila melanogaster as a genetic model organism. Drosophila CYFIP, a previously undescribed gene, is highly expressed in the embryonic nervous system, where it strongly accumulates in central axons and at the neuromuscular junction (NMJ). CYFIP mutations induce defects in axon growth, branching and pathfinding and result in abnormal synapse morphology at the neuromuscular junction. Hence, loss of CYFIP involves defects that have been previously described in dFMR1 and/or dRac1 mutants. Analyses of biochemical and genetic interactions amongst these three proteins suggest that upon activation, dRac1 acts antagonistically on CYFIP, which in turn negatively regulates dFMR1

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Newcombe, Anthony Richard. "The biochemical role of the small G protein Rac1 in cell signalling pathways : interaction with RhoGDI and the phagocyte NADPH oxidase component, p67'p'h'o'x." Thesis, University College London (University of London), 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.342224.

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Verma, Sunil Kumar. "Studies on the signalling of the small GTPase Rap1." Thesis, University of Oxford, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.491743.

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RaplA (Krev-l) is a member of the Ras superfamily of small GTP-binding proteins and has highest homology to Ras. Rapl behaves as an antagonist of oncogenic K-Ras activity in NIH3T3 cells and of polyoma middle-T antigen in Rat-2 cells. It inhibits transformation of human prostate cancer cells, hamster pancreatic adenocarcinoma cells and of ethylcarbamate induced lung adenomas in transgenic mice. However, it does not prevent Ras induced transformation in human HT1080, EJ30 or SW48 cells. Rapl also plays a critical role in regulation of normal morphogenesis in the eye disk and the ovary during embryo development. Recently, Rapl has been implicated in integrin-mediated . adhesion through RapL and modulation of the actin cytoskeleton through RIAM. The downstream effectors through which Rapl mediates its diverse effects are largely unknown. Screening the human genome based upon structural and functional information from the known effectors of Rapl such as RapL, RaIGDS, RIAM and Kritl, a series of potential effectors of Rapl have been identified. Using classical and modem biochemical approaches, it has been established that RASSFlA, a well-known tumour suppressor of human carcinogenesis, is a novel effector of RaplA - linking RaplA to microtubules. Moreover, Rapl association influences the effect of RASSFIA on microtubule behaviour. It is shown that interaction between RASSFIA and RaplA is modulated by RASSFIA phosphorylation. In silica analyses on RASSFIA predicted various putative phosphorylation sites and associated protein kinases within and outside the RA domain of RASSFIA. The sites S197 and S203 within the RA domain of RASSFIA were established as novel PKC phosphorylation sites by in vitro and in vivo assays. These two sites were, however, not responsible for the regulated interaction of RASSFIA with RaplA. This study provides important new insights into the signalling of RaplA indicating that regulated association with RASSFIA links RaplA to microtubules and that the RaplA-RASSFIA interaction plays a role in microtubule dynamics.

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Ogg, Erinn-Lee. "The role of Tiam1/Rac signalling in the centriole cycle." Thesis, University of Manchester, 2016. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.684817.

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The mitotic spindle is a structure that facilitates the equal segregation of DNA into two daughter cells during mitosis. The centrosomes organise the mitotic spindle in to a bipolar conformation, and this arrangement is essential for maintaining faithful chromosome segregation. Deviations in centrosome number alter the structure of the spindle and this can promote multipolar cell divisions and large scale aneuploidy. Therefore centrosome number is tightly regulated in normal cells to prevent interference with bipolar spindle assembly and faithful chromosome segregation. Tumour cells often have supernumerary centrosomes. To prevent interference with bipolar spindle assembly extra centrosomes are clustered in to a bipolar spindle arrangement – preventing a multipolar cell division and intolerable levels of aneuploidy. However centrosome clustering can promote lagging chromosomes during anaphase, a major contributor to chromosomal instability. Chromosomal instability has been shown to enhance the malignant potential of tumour cells. Therefore it is important to understand the mechanisms involved in regulating centrosome number and how these become deregulated in cancer. Centrosome number is regulated by the centrioles, small barrel shaped organelles found within the core of the centrosome. We have identified Tiam1, a Rac specific guanine nucleotide exchange factor, as a novel regulator the centriole cycle. Tiam1 knockdown is sufficient to promote the assembly of multiple aberrant centriole structures in human tumour cell lines. These aberrant centriole structures behave like functional centrioles and correlate with an increase in lagging chromosomes at anaphase – suggesting these structures are capable of promoting chromosomal instability in human tumour cell lines. Moreover we have shown that Tiam1 regulates centriole number by preventing centriole re-duplication events and significantly this effect is independent of Rac activation. We have also identified MCM5 as a novel Tiam1 interactor. MCM5 has been identified in the literature as a regulator of centrosome re-duplication. Therefore we propose that Tiam1 and MCM5 co-operate to prevent centriole re-duplication in human tumour cell lines. These findings identify Tiam1 as a potential prognostic marker of centriole amplification and chromosomal instability in human tumours.

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Smith, Harvey W. "Signalling from uPAR to the Activation of the Small GTPase Rac." Thesis, Institute of Cancer Research (University Of London), 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.499157.

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Rigas, Anastasia Catherine. "The role of the scaffolding protein RACK1 in the androgen receptor signalling pathway." Thesis, University of Newcastle Upon Tyne, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.413937.

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Schönherr, Christina. "Anaplastic Lymphoma Kinase mutations and downstream signalling." Doctoral thesis, Umeå universitet, Institutionen för molekylärbiologi (Medicinska fakulteten), 2012. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-54562.

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The oncogene Anaplastic Lymphoma Kinase (ALK) is a Receptor Tyrosine Kinase (RTK) and was initially discovered as the fusion protein NPM (nucleophosmin)-ALK in a subset of Anaplastic Large Cell Lymphomas (ALCL). Since then more fusion proteins have been identified in a variety of cancers. Further, overexpression of ALK due to gene amplification has been observed in many malignancies, amongst others neuroblastoma, a pediatric cancer. Lately, activating point mutations in the kinase domain of ALK have been described in neuroblastoma patients and neuroblastoma cell lines. In contrast, the physiological function of ALK is still unclear, but ALK is suggested to play a role in the normal development and function of the nervous system. By employing cell culture based approaches, including a tetracycline-inducible PC12 cell system and the in vivo D. melanogaster model system, we aimed to analyze the downstream signalling of ALK and its role in neuroblastoma. First, we wished to analyze whether ALK is able to activate the small GTPase Rap1 contributing to differentiation/proliferation processes. Activated ALK recruits a complex of the GEF C3G and CrkL and activates C3G by tyrosine phosphorylation. This activated complex is able to activate Rap1 resulting either in neurite outgrowth in PC12 cells or proliferation of neuroblastoma cells suggesting a potential role in the oncogenesis of neuroblastoma driven by gain-of-function mutant ALK. Next, we could show that seven investigated ALK mutations with a high probability of being oncogenic (G1128A, I1171N, F1174L, F1174S, R1192P, F1245C and R1275Q), are true gain-of-function mutations, respond differently to ALK inhibitors and have different transforming ability. Especially the F1174S mutation correlates with aggressive disease development. However, the assumed active germ line mutation I1250T is in fact a kinase dead mutation and suggested to act as a dominant-negative receptor. Finally, ALK mutations are most frequently observed in MYCN amplified tumours correlating with a poor clinical outcome. Active ALK regulates mainly the initiation of MYCN transcription in human neuroblastoma cell lines. Further, ALK gain-of-function mutants and MYCN synergize in transforming NIH3T3 cells. Overall, somatic mutations appear to be more aggressive than germ line mutations, implying a different impact on neuroblastoma. Further, successful application of ALK inhibitors suggests a promising future for the development of patient-specific treatments for neuroblastoma patients.

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Dalton, Lucy Ellen. "The in vivo role of RAC signalling in melanoma progression using zebrafish as a model organism." Thesis, University of Manchester, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.509863.

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Book chapters on the topic "Rac1 signalling"

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Buoso, E., Mm Serafini, M. Galasso, M. Ronfani, L. Poloni, C. Lanni, E. Corsini, and M. Racchi. "Role of Cortisol and Dehydroepiandrosterone on RACK1/PKC Signalling and Consequences in Immunosenescence." In Handbook of Immunosenescence, 1515–42. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-319-99375-1_116.

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Buoso, E., Mm Serafini, M. Galasso, M. Ronfani, L. Poloni, C. Lanni, E. Corsini, and M. Racchi. "Role of Cortisol and Dehydroepiandrosterone on RACK1/PKC Signalling and Consequences in Immunosenescence." In Handbook of Immunosenescence, 1–28. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-64597-1_116-1.

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Wells, H. G. "The Last Message Cavor Sent to the Earth." In The First Men in the Moon, edited by Simon J. James. Oxford University Press, 2017. http://dx.doi.org/10.1093/owc/9780198705048.003.0026.

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In this unsatisfactory manner the penultimate message of Cavor dies out. One seems to see him away there in the blue obscurity amidst his apparatus intently signalling us to the last, all unaware of the curtain of confusion that drops between us; all unaware, too, of the final dangers that even then must have been creeping upon him. His disastrous want of vulgar common sense had utterly betrayed him. He had talked of war, he had talked of all the strength and irrational violence of men, of their insatiable aggressions, their tireless futility of conflict. He had filled the whole moon world with this impression of our race, and then I think it is plain that he made the most fatal admission that upon himself alone hung the possibility—at least for a long time — of any further men reaching the moon. The line the cold, inhuman reason of the moon would take seems plain enough to me, and a suspicion of it, and then perhaps some sudden sharp realisation of it, must have come to him. One imagines him going about the moon with the remorse of this fatal indiscretion growing in his mind. During a certain time I am inclined to guess the Grand Lunar was deliberating the new situation, and for all that time Cavor may have gone as free as ever he had gone. But obstacles of some sort prevented his getting to his electro-magnetic apparatus again after that message I have just given. For some days we received nothing. Perhaps he was having fresh audiences, and trying to evade his previous admissions. Who can hope to guess?

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