Relevant bibliographies by topics / Apoptosis signal-regulating kinase 1

Academic literature on the topic 'Apoptosis signal-regulating kinase 1'

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Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Apoptosis signal-regulating kinase 1"

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Kim, Albert H., Gus Khursigara, Xuan Sun, Thomas F. Franke, and Moses V. Chao. "Akt Phosphorylates and Negatively Regulates Apoptosis Signal-Regulating Kinase 1." Molecular and Cellular Biology 21, no. 3 (February 1, 2001): 893–901. http://dx.doi.org/10.1128/mcb.21.3.893-901.2001.

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ABSTRACT The Akt family of serine/threonine-directed kinases promotes cellular survival in part by phosphorylating and inhibiting death-inducing proteins. Here we describe a novel functional interaction between Akt and apoptosis signal-regulating kinase 1 (ASK1), a mitogen-activated protein kinase kinase kinase. Akt decreased ASK1 kinase activity stimulated by both oxidative stress and overexpression in 293 cells by phosphorylating a consensus Akt site at serine 83 of ASK1. Activation of the phosphoinositide 3-kinase (PI3-K)/Akt pathway also inhibited the serum deprivation-induced activity of endogenous ASK1 in L929 cells. An association between Akt and ASK1 was detected in cells by coimmunoprecipitation. Phosphorylation by Akt inhibited ASK1-mediated c-Jun N-terminal kinase and activating transcription factor 2 activities in intact cells. Finally, activation of the PI3-K/Akt pathway reduced apoptosis induced by ASK1 in a manner dependent on phosphorylation of serine 83 of ASK1. These results provide the first direct link between Akt and the family of stress-activated kinases.
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Wilson, Kathryn S., Hanna Buist, Kornelija Suveizdyte, John T. Liles, Grant R. Budas, Colin Hughes, Margaret R. MacLean, et al. "Apoptosis signal-regulating kinase 1 inhibition in in vivo and in vitro models of pulmonary hypertension." Pulmonary Circulation 10, no. 2 (April 2020): 204589402092281. http://dx.doi.org/10.1177/2045894020922810.

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Pulmonary arterial hypertension, group 1 of the pulmonary hypertension disease family, involves pulmonary vascular remodelling, right ventricular dysfunction and cardiac failure. Oxidative stress, through activation of mitogen-activated protein kinases is implicated in these changes. Inhibition of apoptosis signal-regulating kinase 1, an apical mitogen-activated protein kinase, prevented pulmonary arterial hypertension developing in rodent models. Here, we investigate apoptosis signal-regulating kinase 1 in pulmonary arterial hypertension by examining the impact that its inhibition has on the molecular and cellular signalling in established disease. Apoptosis signal-regulating kinase 1 inhibition was investigated in in vivo pulmonary arterial hypertension and in vitro pulmonary hypertension models. In the in vivo model, male Sprague Dawley rats received a single subcutaneous injection of Sugen SU5416 (20 mg/kg) prior to two weeks of hypobaric hypoxia (380 mmHg) followed by three weeks normoxia (Sugen/hypoxic), then animals were either maintained for three weeks on control chow or one containing apoptosis signal-regulating kinase 1 inhibitor (100 mg/kg/day). Cardiovascular measurements were carried out. In the in vitro model, primary cultures of rat pulmonary artery fibroblasts and rat pulmonary artery smooth muscle cells were maintained in hypoxia (5% O2) and investigated for proliferation, migration and molecular signalling in the presence or absence of apoptosis signal-regulating kinase 1 inhibitor. Sugen/hypoxic animals displayed significant pulmonary arterial hypertension compared to normoxic controls at eight weeks. Apoptosis signal-regulating kinase 1 inhibitor decreased right ventricular systolic pressure to control levels and reduced muscularised vessels in lung tissue. Apoptosis signal-regulating kinase 1 inhibition was found to prevent hypoxia-induced proliferation, migration and cytokine release in rat pulmonary artery fibroblasts and also prevented rat pulmonary artery fibroblast-induced rat pulmonary artery smooth muscle cell migration and proliferation. Apoptosis signal-regulating kinase 1 inhibition reversed pulmonary arterial hypertension in the Sugen/hypoxic rat model. These effects may be a result of intrinsic changes in the signalling of adventitial fibroblast.
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Tobiume, Kei. "Characterization of Mouse Apoptosis Signal-regulating Kinase 1." JOURNAL OF THE STOMATOLOGICAL SOCIETY,JAPAN 65, no. 1 (1998): 42–52. http://dx.doi.org/10.5357/koubyou.65.42.

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Hattori, Kazuki, and Hidenori Ichijo. "Apoptosis signal-regulating kinase 1 in regulated necrosis." Cell Cycle 17, no. 1 (January 2, 2018): 5–6. http://dx.doi.org/10.1080/15384101.2017.1397330.

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Weijman, Johannes F., Abhishek Kumar, Sam A. Jamieson, Chontelle M. King, Tom T. Caradoc-Davies, Elizabeth C. Ledgerwood, James M. Murphy, and Peter D. Mace. "Structural basis of autoregulatory scaffolding by apoptosis signal-regulating kinase 1." Proceedings of the National Academy of Sciences 114, no. 11 (February 27, 2017): E2096—E2105. http://dx.doi.org/10.1073/pnas.1620813114.

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Apoptosis signal-regulating kinases (ASK1–3) are apical kinases of the p38 and JNK MAP kinase pathways. They are activated by diverse stress stimuli, including reactive oxygen species, cytokines, and osmotic stress; however, a molecular understanding of how ASK proteins are controlled remains obscure. Here, we report a biochemical analysis of the ASK1 kinase domain in conjunction with its N-terminal thioredoxin-binding domain, along with a central regulatory region that links the two. We show that in solution the central regulatory region mediates a compact arrangement of the kinase and thioredoxin-binding domains and the central regulatory region actively primes MKK6, a key ASK1 substrate, for phosphorylation. The crystal structure of the central regulatory region reveals an unusually compact tetratricopeptide repeat (TPR) region capped by a cryptic pleckstrin homology domain. Biochemical assays show that both a conserved surface on the pleckstrin homology domain and an intact TPR region are required for ASK1 activity. We propose a model in which the central regulatory region promotes ASK1 activity via its pleckstrin homology domain but also facilitates ASK1 autoinhibition by bringing the thioredoxin-binding and kinase domains into close proximity. Such an architecture provides a mechanism for control of ASK-type kinases by diverse activators and inhibitors and demonstrates an unexpected level of autoregulatory scaffolding in mammalian stress-activated MAP kinase signaling.
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Nishida, Kazuhiko, and Kinya Otsu. "The Role of Apoptosis Signal-Regulating Kinase 1 in Cardiomyocyte Apoptosis." Antioxidants & Redox Signaling 8, no. 9-10 (September 2006): 1729–36. http://dx.doi.org/10.1089/ars.2006.8.1729.

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Fujisawa, Takao. "Therapeutic application of apoptosis signal-regulating kinase 1 inhibitors." Advances in Biological Regulation 66 (December 2017): 85–90. http://dx.doi.org/10.1016/j.jbior.2017.10.004.

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Kawarazaki, Yosuke, Hidenori Ichijo, and Isao Naguro. "Apoptosis signal-regulating kinase 1 as a therapeutic target." Expert Opinion on Therapeutic Targets 18, no. 6 (March 24, 2014): 651–64. http://dx.doi.org/10.1517/14728222.2014.896903.

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Mizuguchi, Junichiro, Eiko Takada, and Masae Furuhata. "Apoptosis signal-regulating kinase (ASK)-1 mediates apoptosis in B cells (34.6)." Journal of Immunology 182, no. 1_Supplement (April 1, 2009): 34.6. http://dx.doi.org/10.4049/jimmunol.182.supp.34.6.

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Abstract Engagement of membrane immunoglobulin (mIg) on B cells results in reduction of the mitochondrial membrane potential (ƒ¢ƒμm) and apoptosis, which plays a crucial role in the regulation of immune responses. In this study, we show that the apoptosis signal-regulating kinase 1 (ASK1)-JNK1 signaling pathway participates in mIg-induced apoptosis in normal B cells as well as WEHI-231 B lymphoma cells. Stimulation of WEHI-231 cells with anti-IgM induces phosphorylation and subsequent activation of ASK1, leading to JNK activation. Anti-IgM stimulation produces superoxide anions (O2-), accompanied by loss of ƒ¢ƒμm and an increase in cells with sub-G1 DNA content. Anti-IgM-induced O2- production, loss of ƒ¢ƒμm, and increase in the sub-G1 fraction were all reduced substantially in WEHI-231 cells overexpressing a dominant-negative form of ASK1, compared with control vector alone. The mIg-mediated O2- production, loss of ƒ¢ƒμm, and increase in the sub-G1 fraction were partially abrogated by the reactive oxygen species scavenger N-acetyl-L-cysteine (NAC). Similarly to WEHI-231 B lymphoma cells, the mIg-mediated apoptotic features were moderately compromised in mouse ASK1-deficient B cells. Taken together, these results suggest that mIg engagement induces JNK activation through ASK1 activation, resulting in production of O2- that leads to loss of ƒ¢ƒμm and finally to apoptosis.
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Zou, Xianghong, Tateki Tsutsui, Dipankar Ray, James F. Blomquist, Hidenori Ichijo, David S. Ucker, and Hiroaki Kiyokawa. "The Cell Cycle-Regulatory CDC25A Phosphatase Inhibits Apoptosis Signal-Regulating Kinase 1." Molecular and Cellular Biology 21, no. 14 (July 15, 2001): 4818–28. http://dx.doi.org/10.1128/mcb.21.14.4818-4828.2001.

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ABSTRACT CDC25A phosphatase promotes cell cycle progression by activating G1 cyclin-dependent kinases and has been postulated to be an oncogene because of its ability to cooperate with RAS to transform rodent fibroblasts. In this study, we have identified apoptosis signal-regulating kinase 1 (ASK1) as a CDC25A-interacting protein by yeast two-hybrid screening. ASK1 activates the p38 mitogen-activated protein kinase (MAPK) and c-Jun NH2-terminal protein kinase–stress-activated protein kinase (JNK/SAPK) pathways upon various cellular stresses. Coimmunoprecipitation studies demonstrated that CDC25A physically associates with ASK1 in mammalian cells, and immunocytochemistry with confocal laser-scanning microscopy showed that these two proteins colocalize in the cytoplasm. The carboxyl terminus of CDC25A binds to a domain of ASK1 adjacent to its kinase domain and inhibits the kinase activity of ASK1, independent of and without effect on the phosphatase activity of CDC25A. This inhibitory action of CDC25A on ASK1 activity involves diminished homo-oligomerization of ASK1. Increased cellular expression of wild-type or phosphatase-inactive CDC25A from inducible transgenes suppresses oxidant-dependent activation of ASK1, p38, and JNK1 and reduces specific sensitivity to cell death triggered by oxidative stress, but not other apoptotic stimuli. Thus, increased expression of CDC25A, frequently observed in human cancers, could contribute to reduced cellular responsiveness to oxidative stress under mitogenic or oncogenic conditions, while it promotes cell cycle progression. These observations propose a mechanism of oncogenic transformation by the dual function of CDC25A on cell cycle progression and stress responses.
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Dissertations / Theses on the topic "Apoptosis signal-regulating kinase 1"

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Chibon, Frédéric. "Étude des altérations génétiques des sarcomes indifférenciés : mise en relation des anomalies identifiées et de la différenciation tumorale." Paris 7, 2002. http://www.theses.fr/2002PA077050.

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Pillai, Prajit P. "Role of Protein Kinase C-iota in Neuroblastoma and the Effect of ICA-1, a Novel Protein Kinase C-iota Inhibitor on the Proliferation and Apoptosis of Neuroblastoma Cells." Scholar Commons, 2011. http://scholarcommons.usf.edu/etd/3292.

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Protein Kinase C-iota (PKC-é), an atypical protein kinase C isoform manifests its potential as an oncogene by targeting various aspects of cancer cells such as growth, invasion and survival. PKC-é confers resistance to drug-induced apoptosis in cancer cells. The acquisition of drug resistance is a major obstacle to good prognosis in neuroblastoma. The focus of the dissertation was three-fold: First to study the role of PKC-é in the proliferation of neuroblastoma. Secondly, to identify the efficacy of [4-(5-amino-4-carbamoylimidazol-1-yl)-2,3-dihydroxycyclopentyl] methyl dihydrogen phosphate (ICA-1) as a novel PKC-é inhibitor in neuroblastoma cell proliferation and apoptosis. Finally, to analyze whether PKC-é could self-regulate its expression. Cyclin dependent kinase 7 (Cdk7) phosphorylates cyclin dependent kinases (cdks) and promotes cell proliferation. Our data shows that PKC-é is an in-vitro Cdk7 kinase and that neuroblastoma cells proliferate via a PKC-é/Cdk7/cdk2 cell signaling pathway. ICA-1 specifically inhibits the activity of PKC-é but not that of PKC-zeta (PKC-æ), the closely related atypical PKC family member. The IC50 for the kinase activity assay was approximately 0.1µM which is 1000 times less than that of aurothiomalate, a known PKC-é inhibitor. The phosphorylation of Cdk7 by PKC-é was potently inhibited by ICA-1. ICA-1 mediates its antiproliferative effects on neuroblastoma cells by inhibiting the PKC-é/Cdk7/cdk2 signaling pathway. ICA-1 (0.1µM) inhibited the in-vitro proliferation of BE(2)-C neuroblastoma cells by 58% (P=0.01). Additionally, ICA-1 also induced apoptosis in neuroblastoma cells. Interestingly, ICA-1 did not affect the proliferation of normal neuronal cells suggesting its potential as chemotherapeutic with low toxicity. Hence, our results emphasize the potential of ICA-1 as a novel PKC-é inhibitor and chemotherapeutic agent for neuroblastoma. Bcr-Abl has been shown to regulate the activation of the transcription factor ELK-1 which in turn regulates the expression of PKC-é. Alternatively, we hypothesize that PKC-é can self regulate its expression by indirectly regulating the activity of Elk-1 in an ERK1 dependent manner. Our preliminary data shows that there was robust increase in the expression as well as association of PKC-é and Elk-1 in actively proliferating neuroblastoma cells suggesting a potential role of PKC-é in regulating the activity of Elk-1. Analysis of the subcellular fractions also presented a similar increase in the association between PKC-é and Elk-1 in the nuclear fraction of actively proliferating cells as compared to cytoplasm. Interestingly, the nuclear expression of PKC-é was also found to be higher in these cells, suggesting that PKC-é translocated to the nucleus in actively proliferating cells and regulated the transcriptional activity of Elk-1. However, our data from in-vitro kinase activity demonstrated that PKC-é was not an Elk-1 kinase but that it increased the phosphorylation of Elk-1 in the presence of ERK1, an upstream kinase of Elk-1 in the Bcr-Abl mediated regulatory pathway of PKC-é. This suggested that ERK1 was integral to the self-regulatory activity of PKC-é. In conclusion, we hypothesize that the self-regulatory mechanism of PKC-é is initiated by the translocation PKC-é into the nucleus where it activates ERK1. This promotes the activation of its downstream target Elk-1 which subsequently upregulates the expression of PKC-é
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Poser, Steven Walter. "Coincident signaling of cAMP with phosphatidylinositol 3' kinase and mitogen activated protein kinase signal transduction cascades : a role in regulating gene exression during development and synaptic plasticity /." Thesis, Connect to this title online; UW restricted, 2001. http://hdl.handle.net/1773/10633.

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Li, Li-Fu, and 李立夫. "Apoptosis Signal-Regulated Kinase 1 and c-Jun N-terminal Kinase Regulated Ventilation-Induced Inflammatory Cytokine and Lung Apoptosis." Thesis, 2005. http://ndltd.ncl.edu.tw/handle/98554179740295415443.

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博士
長庚大學
臨床醫學研究所
93
Positive pressure ventilation with large tidal volumes has been shown to cause release of cytokines, including macrophage inflammatory protein-2 (MIP-2), a functional equivalent of human Interleukin (IL)-8. The mechanisms regulating ventilation-induced cytokine production are unclear. We designed three experiments to explore the mechanisms underlying ventilator-induced lung injury. We hypothesized that high tidal volume ventilation-induced IL-8 or MIP-2 production and lung apoptosis are dependent on the activation of apoptosis signal-regulated kinase 1 (ASK1) and c-Jun N-terminal kinase (JNK). We exposed A549 cells, a type II-like alveolar epithelial cell line, to cyclic stretch at 20 cycles/minute for 5 minutes to two hours and C57BL/6 mice to high tidal volume (30 ml/kg) or low tidal volume (6 ml/kg) mechanical ventilation for 5 hours. Cyclic stretch induced IL-8 protein production, IL-8 mRNA expression and JNK activation, but only transient activation of p38 and ERK1/2. High tidal volume ventilation induced neutrophil migration into the lung, airway epithelial apoptosis, MIP-2 protein production, MIP-2 mRNA expression, and activation of ASK1, JNK, and activator protein-1 (AP-1) DNA binding. Inhibition of stretch-induced JNK activation by adenovirus- mediated gene transfer of SEK-1 (KR), a dominant inhibitory mutant of SEK-1, the immediate upstream activator of the JNKs, and pharmacological JNK inhibitor II SP600125, blocked IL-8 mRNA expression and attenuated IL-8 production. Inhibition of p38 and ERK1/2 did not affect stretch-induced IL-8 production. Stretch-induced activation nuclear factor (NF)-kB and AP-1 was blocked by NF-kB inhibitor and JNK inhibitor, respectively. NF-IL-6 site was not essential for cyclic stretch-induced IL-8 promoter activity. Stretch also induced NF-kB-inducing kinase (NIK) activation, and inhibition of NF-kB attenuated IL-8 mRNA expression and IL-8 production. Large tidal volume ventilation of JNK knockout mice, and pharmacological JNK inhibition with SP600125 and ASK1 inhibition with thioredoxin attenuated neutrophil sequestration, and blocked MIP-2 mRNA expression, MIP-2 production, airway epithelial cell apoptosis, activation of JNK and AP-1 DNA binding. We conclude that lung cell stretch in vitro and in vivo, results in increased neutrophil sequestration, apoptotic cell death, and increased IL-8 or MIP-2 production, which were, at least in part, dependent, on the ASK1/JNK pathway.
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Chang, Chia-Kai, and 張家凱. "The Role of Apoptosis Signal Regulated Kinase 1 in Peptidoglycan-Induced Cyclooxygenase-2 Expression in RAW 264.7 Macrophages." Thesis, 2005. http://ndltd.ncl.edu.tw/handle/50372115705052938243.

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碩士
臺北醫學大學
藥理學研究所
93
Abstract The Ras/Raf-1/extracellular signal-regulated kinase (ERK) pathway is known to be involved in peptidoglycan (PGN)-induced nuclear factor-B (NF-B) activation and cyclooxygenase-2 (COX-2) expression in RAW 264.7 macrophages (J. Biol. Chem. 2004, 297: 20889-20897). In this study, we further investigated the roles of apoptosis signal regulated kinase 1 (ASK1), c-jun N-terminal kinase (JNK), activator protein-1 (AP-1), and CCAAT/enhancer binding protein  (C/EBP) in PGN-induced COX-2 expression. The PGN-induced COX-2 expression was attenuated by the ASK1 dominant negative mutant (ASK1DN), a JNK inhibitor (SP600125), the JNK1 dominant negative mutant (JNK1DN), the JNK2DN, and the AP-1 inhibitor (curcumin). PGN induced the recruitment of TNFR-associated factor 6 (TRAF6) and ASK1 to toll-like receptor 2 (TLR2) in a time-dependent manner. Treatment of RAW 264.7 macrophages with PGN caused time-dependent dissociation of 14-3-3 with ASK1 and dephosphorylation of ASK1 which resulted in activations of ASK1 and further activates JNK and c-jun. The PGN-induced JNK activation was inhibited by ASK1DN and SP600125. Stimulation of cells with PGN activated the formation of AP-1 specific-DNA protein complex and AP-1-luciferase activity. The PGN-mediated increase in AP-1-luciferase activity was inhibited by SP600125, and curcumin. Treatment of macrophages with PGN caused time-dependent C/EBP expression. Stimulation of cells with PGN caused the formation of C/EBP-specific DNA-protein complex. Furthermore, PGN-induced increase in COX-2-luciferase activity was inhibited by cells transfected with the C/EBP site mutation of COX-2-construct. Our data demonstrated that PGN induced the recruitment of TRAF6 to TLR2 to activate the ASK1/JNK/AP-1 pathway, which in turn initiates CEBP expression and activation, and ultimately induces COX-2 expression in RAW 264.7 macrophages.
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Ling, Ling. "Investigarion of Activated Phosphaidylinositol 3’ Kinase Signaling in Stem Cell Self-renewal and Tumorigenesis." Thesis, 2012. http://hdl.handle.net/1807/32815.

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The phosphatidylinositol 3' kinase (PI3K) pathway is involved in many cellular processes including cell proliferation, survival, and glucose transport, and is implicated in various disease states such as cancer and diabetes. Though there have been numerous studies dissecting the role of PI3K signaling in different cell types and disease models, the mechanism by which PI3K signaling regulates embryonic stem (ES) cell fate remains unclear. It is believed that in addition to proliferation and tumorigenicity, PI3K activity might also be important for self-renewal of ES cells. Paling et al. (2004) reported that the inhibition of PI3K led to a reduction in the ability of leukemia inhibitory factor (LIF) to maintain self-renewal causing cells to differentiate. Studies in our lab have revealed that ES cells completely lacking GSK-3 remain undifferentiated compared to wildtype ES cells. GSK-3 is negatively regulated by PI3K suggesting that PI3K may play a vital role in maintaining pluripotency in ES cells through GSK-3. By using a modified Flp recombinase system, we expressed activated alleles of PDK-1 and PKB to create stable, isogenic ES cell lines to further study the role of the PI3K signaling pathway in stem cell fate determination. In vitro characterization of the transgenic cell lines revealed a strong tendency towards maintenance of pluripotency, and this phenotype was found to be independent of canonical Wnt signal transduction. To assess growth and differentiation capacity in vivo, the ES cell lines were grown as subcutaneous teratomas. The constitutively active PDK-1 and PKB ES cell lines were able to form all three germ layers when grown in this manner – in contrast to ES cells engineered to lack GSK-3. The resulting PI3K pathway activated cells exhibited a higher growth rate which resulted in large teratomas. In summary, PI3K signaling is sufficient to maintain self-renewal and survival of stem cells. Since this pathway is frequently mutationally activated in cancers, its effect on suppressing differentiation may contribute to its oncogenicity.
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Busch, F., A. Mobasheri, P. Shayan, C. Lueders, R. Stahlmann, and M. Shakibaei. "Resveratrol modulates interleukin-1beta-induced phosphatidylinositol 3-kinase and nuclear factor kappaB signaling pathways in human tenocytes." 2012. http://hdl.handle.net/10454/5903.

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Resveratrol, an activator of histone deacetylase Sirt-1, has been proposed to have beneficial health effects due to its antioxidant and anti-inflammatory properties. However, the mechanisms underlying the anti-inflammatory effects of resveratrol and the intracellular signaling pathways involved are poorly understood. An in vitro model of human tenocytes was used to examine the mechanism of resveratrol action on IL-1beta-mediated inflammatory signaling. Resveratrol suppressed IL-1beta-induced activation of NF-kappaB and PI3K in a dose- and time-dependent manner. Treatment with resveratrol enhanced the production of matrix components collagen types I and III, tenomodulin, and tenogenic transcription factor scleraxis, whereas it inhibited gene products involved in inflammation and apoptosis. IL-1beta-induced NF-kappaB and PI3K activation was inhibited by resveratrol or the inhibitors of PI3K (wortmannin), c-Src (PP1), and Akt (SH-5) through inhibition of IkappaB kinase, IkappaBalpha phosphorylation, and inhibition of nuclear translocation of NF-kappaB, suggesting that PI3K signaling pathway may be one of the signaling pathways inhibited by resveratrol to abrogate NF-kappaB activation. Inhibition of PI3K by wortmannin attenuated IL-1beta-induced Akt and p65 acetylation, suggesting that p65 is a downstream component of PI3K/Akt in these responses. The modulatory effects of resveratrol on IL-1beta-induced activation of NF-kappaB and PI3K were found to be mediated at least in part by the association between Sirt-1 and scleraxis and deacetylation of NF-kappaB and PI3K. Overall, these results demonstrate that activated Sirt-1 plays an essential role in the anti-inflammatory effects of resveratrol and this may be mediated at least in part through inhibition/deacetylation of PI3K and NF-kappaB.
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Mok, Sue-Ann. "Retrograde signaling mechanisms of nerve growth factor regulating the survival and apoptosis of sympathetic neurons." Phd thesis, 2009. http://hdl.handle.net/10048/447.

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The survival of several neuron populations during development, including sympathetic neurons, is strictly regulated by neurotrophins such as nerve growth factor (NGF) released from innervation targets. NGF activates its receptor, TrkA, at axon terminals, to generate signals that are transmitted retrogradely to cell bodies to induce signaling cascades regulating survival. A general view of this process is that NGF generates retrograde survival signals that, when delivered to cell bodies, induce downstream survival signaling that prevents apoptosis. A retrograde survival signal proposed to be necessary for sympathetic neuron survival consists of endosomes containing NGF and phosphorylated TrkA. For this signal, phosphorylated TrkA arriving at cell bodies is required to initiate survival signaling. Studies have tested the necessity of TrkA phosphorylation in the cell bodies for survival: results from different studies contradict each other. Moreover, the Trk inhibitor, K252a, used in these studies, has reported non-specific effects. Using an alternate Trk inhibitor, Gö6976, data presented in this thesis demonstrates that NGF can promote survival by retrograde signaling that does not require TrkA phosphorylation in the cell bodies. These retrograde signals may be composed of signaling molecules activated downstream of TrkA in axons since pro-survival molecules downstream of TrkA, Akt and CREB, were found activated in the cell bodies/proximal axons. Data presented in this thesis also reveals a fundamentally different mechanism for how NGF promotes sympathetic neuron survival: a retrograde apoptotic signal that is suppressed by NGF. NGF withdrawal from axons induced the “axon apoptotic signal” that was retrogradely transmitted to cell bodies to activate a key pro-apoptotic molecule, c-jun. The axon apoptotic signal, which was blocked by the kinase inhibitors rottlerin and chelerythrine, was necessary for apoptosis in response to NGF deprivation. Evidence GSK3 is involved in generation or transmission of the axon apoptotic signal was provided by experiments with GSK3 inhibitors and siRNA. The axon apoptotic signal discovery refutes the previous view that NGF acting on axon terminals supports survival exclusively by generating retrograde survival signals. The axon apoptotic signal has broad implications for understanding nervous system development and other conditions where neuronal apoptosis occurs, such as neurotrauma and neurodegenerative diseases.
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Book chapters on the topic "Apoptosis signal-regulating kinase 1"

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Zimmermann, Arthur. "Etiology and Pathogenesis of Hepatocellular Carcinoma: Transcription Factors, Signal Pathways Regulating Proliferation and Apoptosis, and Telomeres/Telomerases." In Tumors and Tumor-Like Lesions of the Hepatobiliary Tract, 1–22. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-26587-2_167-1.

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"ASK1 (apoptosis signal regulating kinase)." In Encyclopedia of Genetics, Genomics, Proteomics and Informatics, 149. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6754-9_1223.

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Katagiri, Kazumi, Atsushi Matsuzawa, and Hidenori Ichijo. "Regulation of Apoptosis Signal-Regulating Kinase 1 in Redox Signaling." In Methods in Enzymology, 277–88. Elsevier, 2010. http://dx.doi.org/10.1016/s0076-6879(10)74016-7.

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Zou, Jin, Wei Shen, Yu Zhang, and Shibo Ying. "The Role of Protein Arginine Methyltransferase 1 in Gastrointestinal Cancers." In Post-Translational Modifications in Cellular Functions and Diseases. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.96197.

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Mammals can produce nine kinds of arginine methylation enzymes that can be divided into three types (I, II, and III) according to their catalytic activity. Arginine methyltransferase 1 (PRMT1), as the first discovered arginine methyltransferase type I, has been reported to be involved in cell signal transduction, DNA damage repair, RNA transcription and other processes. Its imbalance or abnormal expression is also involved in cancer metastasis. PRMT1 is highly expressed in gastrointestinal tumors and promotes tumor biomarkers expression, chemotherapy resistance and tumorigenicity to promote cancer progression, while downregulation of PRMT1 expression can inhibit the migration and invasion of related tumor cells or promote tumor cells apoptosis and inhibit the progression of cancer. Therefore, PRMT1 may be a cancer therapeutic target. In this paper, arginine methylase 1 expression in various types of gastrointestinal tumors, the tumorigenic mechanism and the role of PRMT1 in tumorigenesis and development were reviewed.
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Evans Adunyah, Samuel, Richard Akomeah, Fareed K.N. Arthur, Roland S. Cooper, and Joshua C.M. Williams. "IL-17 Biological Effects and Signaling Mechanisms in Human Leukemia U937 Cells." In Interleukins - The Immune and Non-Immune Systems’ Related Cytokines. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.96422.

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Human Interlekin-17 is produced by memory activated CD4+ T cells and other cells. It was initially considered unique in that its specific receptor is distinct from other cytokine receptors. IL-17 receptor is ubiquitously expressed by different cells including T cells. IL-17 plays a role in regulating growth, immune response and pro-inflammatory responses. It regulates differentiation of a subset of Th0 cells into Th-17 cells, which produce IL-17-induced cytokines. The IL-17R belongs to type 1 cytokine receptors. IL-17 belongs to a superfamily of its own, which includes IL-17A, IL-17B, IL-17C, IL-17E and IL-17F. These members of IL-17 superfamily have some sequence homology but bind to different receptors. Prior to this investigation, limited information existed on the effects of IL-17A in human leukemia cell lines. Our results show that IL-17A promotes growth, anti-apoptotic effects, chemotaxis, cytokine expression and transcriptional factor activation in leukemia cells. IL-17A activates multiple signaling pathways including PI-3 K, Jak–STAT, Raf-ERK1/2 and SRC kinase pathways, which mediate different biological effects of IL-17A in leukemia cells. Our findings implicate IL-17A in leukemia cell growth and survival, supporting potential leukemia therapy via development of anti-IL-17A drugs. This chapter focuses on IL-17A, herein referred to as IL-17.
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Conference papers on the topic "Apoptosis signal-regulating kinase 1"

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Tang, Xiaofei, Jian-Fei Zhang, Wen-wen Niu, and Min Zhang. "Abstract 2280: Role of apoptosis signal-regulating kinase 1 in the cell apoptosis in oral leukoplakia." 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.am2014-2280.

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Immanuel, C. N., B. Teng, B. Dong, J. Tatum, E. Gordon, C. Luellen, A. Schwingshackl, E. A. Fitzpatrick, S. Cormier, and C. M. Waters. "Apoptosis Signal Regulating Kinase-1 (ASK1) Differentially Activates p38- and JNK-Mediated Inflammasome Pathways." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a2092.

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Makena, Patrudu S., Manik C. Ghosh, Vijay K. Gorantla, Lavanya Bezawada, Louisa Balazs, Charlean L. Luellen, Hidenori Ichijo, Christopher M. Waters, and Scott E. Sinclair. "Regulation Of ERK-1,2 By Apoptosis Signal Regulating Kinase-1 (ASK-1) Is Required For Ventilator Induced-Apoptosis And Lung Injury." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a5435.

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Okamoto, Shinichi, Shuichiro Maruoka, Kota Tsuya, Yasuhiro Gon, Kenji Mizumura, Shu Hashimoto, Kaori Soda, Isao Naguro, and Hidenori Ichijo. "Involvement of apoptosis signal-regulating kinase-1 in house dust mite-induced allergic asthma in mice." In ERS International Congress 2017 abstracts. European Respiratory Society, 2017. http://dx.doi.org/10.1183/1393003.congress-2017.pa576.

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Makena, Patrudu S., Vijay K. Gorantla, Manik C. Ghosh, Lavanya Bezawada, Louisa Balazs, Charlean L. Luellen, Hidenori Ichijo, Scott E. Sinclair, and Christopher M. Waters. "Apoptosis Signal Regulating Kinase 1 Negatively Regulates Survivin Via P38/MAPK And Egr1 In Ventilator Induced Apoptosis And Lung Injury." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a5438.

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Makena, Patrudu S., Vijay K. Gorantla, Charlean Luellen, Christopher M. Waters, and Scott E. Sinclair. "Apoptosis Signal Regulating Kinase-1 (ASK-1) Deficiency Protects From Apoptosis And Autophagy Induced By Combined High Tidal Volume Mechanical Ventilation And Hyperoxia." In 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.a1673.

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Boehm, Mario, Baktybek Kojonazarov, Hossein Ardeschir Ghofrani, Friedrich Grimminger, Norbert Weissmann, John T. Liles, Grant R. Budas, Werner Seeger, and Ralph T. Schermuly. "Effects of apoptosis signal- regulating kinase 1 (ASK1) inhibition in experimental pressure overload-induced right ventricular dysfunction." In Annual Congress 2015. European Respiratory Society, 2015. http://dx.doi.org/10.1183/13993003.congress-2015.pa4913.

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Hayakawa, Yoku, Yoshihiro Hirata, Hayato Nakagawa, Kei Sakamoto, Wachiko Nakata, Hiroto Kinoshita, Ryota Takahashi, et al. "Abstract 3133: Apoptosis signal-regulating kinase 1 and cyclin D1 compose a positive feedback loop contributing to tumor growth in gastric cancer." In 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.am2011-3133.

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Makena, Patrudu S., Manik C. Ghosh, Vijay K. Gorantla, Lavanya Bezawada, Charlean L. Luellen, Christopher M. Waters, and Scott E. Sinclair. "Apoptosis Signal-Regulating Kinase-1 (ASK-1) Knockdown Augments Antioxidant Response Element (ARE)-Mediated Gene Expression Of Phase-II Antioxidant Enzymes (AOES) During Acute Hyperoxia (HO) Exposure." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a5971.

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Wang, Xuening, Jonathan S. Harrison, and George P. Studzinski. "Abstract 315: Cell death of AML blasts induced by cytarabine and enhanced by the Vitamin D2/Carnosic acid cell differentiating combination involves apoptosis signal-regulating kinase 1 (ASK1) activation." In 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.am2018-315.

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Reports on the topic "Apoptosis signal-regulating kinase 1"

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Chamovitz, Daniel A., and Xing-Wang Deng. Developmental Regulation and Light Signal Transduction in Plants: The Fus5 Subunit of the Cop9 Signalosome. United States Department of Agriculture, September 2003. http://dx.doi.org/10.32747/2003.7586531.bard.

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Plants adjust their growth and development in a manner optimal for the prevailing light conditions. The molecular mechanisms by which light signals are transduced and integrated with other environmental and developmental signals are an area of intense research. (Batschauer, 1999; Quail, 2002) One paradigm emerging from this work is the interconnectedness of discrete physiological responses at the biochemical level, for instance, between auxin and light signaling (Colon-Carmona et al., 2000; Schwechheimer and Deng, 2001; Tian and Reed, 1999) and between light signaling and plant pathogen interactions (Azevedo et al., 2002; Liu et al., 2002). The COP9 signalosome (CSN) protein complex has a central role in the light control of plant development. Arabidopsis mutants that lack this complex develop photomorphogenically even in the absence of light signals (reviewed in (Karniol and Chamovitz, 2000; Schwechheimer and Deng, 2001). Thus the CSN was hypothesized to be a master repressor of photomorphogenesis in darkness, and light acts to bypass or eliminate this repression. However, the CSN regulates more than just photomorphogenesis as all mutants lacking this complex die near the end of seedling development. Moreover, an essentially identical complex was subsequently discovered in animals and yeast, organisms whose development is not light responsive, exemplifying how plant science can lead the way to exciting discoveries in biomedical model species (Chamovitz and Deng, 1995; Freilich et al., 1999; Maytal-Kivity et al., 2002; Mundt et al., 1999; Seeger et al., 1998; Wei et al., 1998). Our long-term objective is to determine mechanistically how the CSN controls plant development. We previously that this complex contains eight subunits (Karniol et al., 1998; Serino et al., 1999) and that the 27 ilia subunit is encoded by the FUS5/CSN7 locus (Karniol et al., 1999). The CSN7 subunit also has a role extraneous to the COP9 signalosome, and differential kinase activity has been implicated in regulating CSN7 and the COP9 signalosome (Karniol et al., 1999). In the present research, we further analyzed CSN7, both in terms of interacting proteins and in terms of kinases that act on CSN7. Furthermore we completed our analysis of the CSN in Arabidopsis by analyzing the remaining subunits. Outline of Original Objectives and Subsequent Modifications The general goal of the proposed research was to study the CSN7 (FUS5) subunit of the COP9 signalosome. To this end we specifically intended to: 1. Identify the residues of CSN7 that are phosphorylated. 2. Monitor the phosphorylation of CSN7 under different environmental conditions and under different genetic backgrounds. 3. Generate transgenic plants with altered CSN7 phosphorylation sites. 4. Purify CSN7 kinase from cauliflower. 5. Clone the Arabidopsis cDNA encoding CSN7 kinase 6. Isolate and characterize additional CSN7 interacting proteins. 7. Characterize the interaction of CSN7 and the COP9 signalosome with the HY5-COP1 transcriptional complex. Throughout the course of the research, emphasis shifted from studying CSN7 phosphorylation (Goals 1-3), to studying the CSN7 kinase (Goal 4 and 5), an in depth analysis of CSN7 interactions (Goal 6), and the study of additional CSN subunits. Goal 7 was also abandoned as no data was found to support this interaction.
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Chamovitz, Daniel, and Albrecht Von Arnim. Translational regulation and light signal transduction in plants: the link between eIF3 and the COP9 signalosome. United States Department of Agriculture, November 2006. http://dx.doi.org/10.32747/2006.7696515.bard.

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The COP9 signalosome (CSN) is an eight-subunit protein complex that is highly conserved among eukaryotes. Genetic analysis of the signalosome in the plant model species Arabidopsis thaliana has shown that the signalosome is a repressor of light dependent seedling development as mutant Arabidopsis seedlings that lack this complex develop in complete darkness as if exposed to light. These mutant plants die following the seedling stage, even when exposed to light, indicating that the COP9 signalosome also has a central role in the regulation of normal photomorphogenic development. The biochemical mode of action of the signalosome and its position in eukaryotic cell signaling pathways is a matter of controversy and ongoing investigation, and recent results place the CSN at the juncture of kinase signaling pathways and ubiquitin-mediated protein degradation. We have shown that one of the many CSN functions may relate to the regulation of translation through the interaction of the CSN with its related complex, eukaryotic initiation factor (eIF3). While we have established a physical connection between eIF3 subunits and CSN subunits, the physiological and developmental significance of this interaction is still unknown. In an effort to understand the biochemical activity of the signalosome, and its role in regulating translation, we originally proposed to dissect the contribution of "h" subunit of eIF3 (eIF3h) along the following specific aims: (i) Isolation and phenotypic characterization of an Arabidopsis loss-of-function allele for eIF3h from insertional mutagenesis libraries; (ii) Creation of designed gain and loss of function alleles for eIF3h on the basis of its nucleocytoplasmic distribution and its yeast-two-hybrid interactions with other eIF3 and signalosome partner proteins; (iii) Determining the contribution of eIF3h and its interaction with the signalosome by expressing specific mutants of eIF3h in the eIF3h- loss-of function background. During the course of the research, these goals were modified to include examining the genetic interaction between csn and eif3h mutations. More importantly, we extended our effort toward the genetic analysis of mutations in the eIF3e subunit, which also interacts with the CSN. Through the course of this research program we have made several critical scientific discoveries, all concerned with the apparent diametrically opposed roles of eIF3h and eIF3e. We showed that: 1) While eIF3e is essential for growth and development, eIF3h is not essential for growth or basal translation; 2) While eIF3e has a negative role in translational regulation, eIF3h is positively required for efficient translation of transcripts with complex 5' UTR sequences; 3) Over-accumulation of eIF3e and loss-of-function of eIF3h both lead to cop phenotypes in dark-grown seedlings. These results were published in one publication (Kim et al., Plant Cell 2004) and in a second manuscript currently in revision for Embo J. Are results have led to a paradigm shift in translation research – eIF3 is now viewed in all systems as a dynamic entity that contains regulatory subuits that affect translational efficiency. In the long-term agronomic outlook, the proposed research has implications that may be far reaching. Many important plant processes, including developmental and physiological responses to light, abiotic stress, photosynthate, and hormones operate in part by modulating protein translation [23, 24, 40, 75]. Translational regulation is slowly coming of age as a mechanism for regulating foreign gene expression in plants, beginning with translational enhancers [84, 85] and more recently, coordinating the expression of multiple transgenes using internal ribosome entry sites. Our contribution to understanding the molecular mode of action of a protein complex as fundamental as eIF3 is likely to lead to advances that will be applicable in the foreseeable future.
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Barash, Itamar, and Robert Rhoads. Translational Mechanisms Governing Milk Protein Levels and Composition. United States Department of Agriculture, 2006. http://dx.doi.org/10.32747/2006.7696526.bard.

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Original objectives: The long-term goal of the research is to achieve higher protein content in the milk of ruminants by modulating the translational apparatus of the mammary gland genetically, nutritionally, or pharmacologically. The short-term objectives are to obtain a better understanding of 1) the role of amino acids (AA) as regulators of translation in bovine and mouse mammary epithelial cells and 2) the mechanism responsible for the synergistic enhancement of milk-protein mRNA polyadenylation by insulin and prolactin. Background of the topic: In many cell types and tissues, individual AA affect a signaling pathway which parallels the insulin pathway to modulate rates and levels of protein synthesis. Diverse nutritional and hormonal conditions are funneled to mTOR, a multidomain serine/threonine kinase that regulates a number of components in the initiation and elongation stages of translation. The mechanism by which AA signal mTOR is largely unknown. During the current grant period, we have studied the effect of essential AA on mechanisms involved in protein synthesis in differentiated mammary epithelial cells cultured under lactogenic conditions. We also studied lactogenic hormone regulation of milk protein synthesis in differentiated mammary epithelial cells. In the first BARD grant (2000-03), we discovered a novel mechanism for mRNA-specific hormone-regulated translation, namely, that the combination of insulin plus prolactin causes cytoplasmic polyadenylation of milk protein mRNAs, which leads to their efficient translation. In the current BARD grant, we have pursued the signaling pathways of this novel hormone action. Major conclusions/solutions/achievements: The positive and negative signaling from AA to the mTOR pathway, combined with modulation of insulin sensitization, mediates the synthesis rates of total and specific milk proteins in mammary epithelial cells. The current in vitro study revealed cryptic negative effects of Lys, His, and Thr on cellular mechanisms regulating translation initiation and protein synthesis in mammary epithelial cells that could not be detected by conventional in vivo analyses. We also showed that a signaling pathway involving Jak2 and Stat5, previously shown to lead from the prolactin receptor to transcription of milk protein genes, is also used for cytoplasmic polyadenylation of milk protein mRNAs, thereby stabilizing these mRNAs and activating them for translation. Implications: In vivo, plasma AA levels are affected by nutritional and hormonal effects as well as by conditions of exercise and stress. The amplitude in plasma AA levels resembles that applied in the current in vitro study. Thus, by changing plasma AA levels in the epithelial cell microenvironment or by sensitizing the mTOR pathway to their presence, it should be possible to modulate the rate of milk protein synthesis. Furthermore, knowledge that phosphorylation of Stat5 is required for enhanced milk protein synthesis in response to lactogenic opens the possibility for pharmacologic approaches to increase the phosphorylation of Stat5 and, thereby, milk protein production.
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