Gotowe bibliografie tematyczne / Stress activated protein kinase

Gotowa bibliografia na temat „Stress activated protein kinase”

Autor: Grafiati

Data publikacji: 4 czerwca 2021

Data aktualizacji: 20 lutego 2023

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Artykuły w czasopismach na temat "Stress activated protein kinase"

Holtmann, Helmut, Reinhard Winzen, Pamela Holland, Solveig Eickemeier, Elke Hoffmann, David Wallach, Nikolai L. Malinin, Jonathan A. Cooper, Klaus Resch i Michael Kracht. "Induction of Interleukin-8 Synthesis Integrates Effects on Transcription and mRNA Degradation from at Least Three Different Cytokine- or Stress-Activated Signal Transduction Pathways". Molecular and Cellular Biology 19, nr 10 (1.10.1999): 6742–53. http://dx.doi.org/10.1128/mcb.19.10.6742.

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ABSTRACT A hallmark of inflammation is the burst-like formation of certain proteins, initiated by cellular stress and proinflammatory cytokines like interleukin 1 (IL-1) and tumor necrosis factor, stimuli which simultaneously activate different mitogen-activated protein (MAP) kinases and NF-κB. Cooperation of these signaling pathways to induce formation of IL-8, a prototype chemokine which causes leukocyte migration and activation, was investigated by expressing active and inactive forms of protein kinases. Constitutively active MAP kinase kinase 7 (MKK7), an activator of the stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) pathway, induced IL-8 synthesis and transcription from a minimal IL-8 promoter. Furthermore, MKK7 synergized in both effects with NF-κB-inducing kinase (NIK). Activation of the IL-8 promoter by either of the kinases required functional NF-κB and AP-1 sites. While NIK and MKK7 did not affect degradation of IL-8 mRNA, an active form of MKK6, which selectively activates p38 MAP kinase, induced marked stabilization of the transcript and further increased IL-8 protein formation induced by NIK plus MKK7. Consistently, the MAP kinase kinase kinase MEKK1, which can activate NF-κB, SAPK/JNK, and p38 MAP kinases, most potently induced IL-8 formation. These results provide evidence that maximal IL-8 gene expression requires the coordinate action of at least three different signal transduction pathways which cooperate to induce mRNA synthesis and suppress mRNA degradation.

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Frost, J. A., S. Xu, M. R. Hutchison, S. Marcus i M. H. Cobb. "Actions of Rho family small G proteins and p21-activated protein kinases on mitogen-activated protein kinase family members." Molecular and Cellular Biology 16, nr 7 (lipiec 1996): 3707–13. http://dx.doi.org/10.1128/mcb.16.7.3707.

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The mitogen-activated protein (MAP) kinases are a family of serine/threonine kinases that are regulated by distinct extracellular stimuli. The currently known members include extracellular signal-regulated protein kinase 1 (ERK1), ERK2, the c-Jun N-terminal kinase/stress-activated protein kinases (JNK/SAPKs), and p38 MAP kinases. We find that overexpression of the Ste20-related enzymes p21-activated kinase 1 (PAK1) and PAK2 in 293 cells is sufficient to activate JNK/SAPK and to a lesser extent p38 MAP kinase but not ERK2. Rat MAP/ERK kinase kinase 1 can stimulate the activity of each of these MAP kinases. Although neither activated Rac nor the PAKs stimulate ERK2 activity, overexpression of either dominant negative Rac2 or the N-terminal regulatory domain of PAK1 inhibits Ras-mediated activation of ERK2, suggesting a permissive role for Rac in the control of the ERK pathway. Furthermore, constitutively active Rac2, Cdc42hs, and RhoA synergize with an activated form of Raf to increase ERK2 activity. These findings reveal a previously unrecognized connection between Rho family small G proteins and the ERK pathway.

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Wang, Pengcheng, Chuan-Chih Hsu, Yanyan Du, Peipei Zhu, Chunzhao Zhao, Xing Fu, Chunguang Zhang i in. "Mapping proteome-wide targets of protein kinases in plant stress responses". Proceedings of the National Academy of Sciences 117, nr 6 (28.01.2020): 3270–80. http://dx.doi.org/10.1073/pnas.1919901117.

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Protein kinases are major regulatory components in almost all cellular processes in eukaryotic cells. By adding phosphate groups, protein kinases regulate the activity, localization, protein–protein interactions, and other features of their target proteins. It is known that protein kinases are central components in plant responses to environmental stresses such as drought, high salinity, cold, and pathogen attack. However, only a few targets of these protein kinases have been identified. Moreover, how these protein kinases regulate downstream biological processes and mediate stress responses is still largely unknown. In this study, we introduce a strategy based on isotope-labeled in vitro phosphorylation reactions using in vivo phosphorylated peptides as substrate pools and apply this strategy to identify putative substrates of nine protein kinases that function in plant abiotic and biotic stress responses. As a result, we identified more than 5,000 putative target sites of osmotic stress-activated SnRK2.4 and SnRK2.6, abscisic acid-activated protein kinases SnRK2.6 and casein kinase 1-like 2 (CKL2), elicitor-activated protein kinase CDPK11 and MPK6, cold-activated protein kinase MPK6, H2O2-activated protein kinase OXI1 and MPK6, and salt-induced protein kinase SOS1 and MPK6, as well as the low-potassium-activated protein kinase CIPK23. These results provide comprehensive information on the role of these protein kinases in the control of cellular activities and could be a valuable resource for further studies on the mechanisms underlying plant responses to environmental stresses.

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CHAN-HUI, Po-Ying, i Robert WEAVER. "Human mitogen-activated protein kinase kinase kinase mediates the stress-induced activation of mitogen-activated protein kinase cascades". Biochemical Journal 336, nr 3 (15.12.1998): 599–609. http://dx.doi.org/10.1042/bj3360599.

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The mitogen-activated protein kinase (MAPK) cascades represent one of the important signalling mechanisms in response to environmental stimuli. We report the identification of a human MAPK kinase kinase, MAPKKK4, via sequence similarity with other MAPKKKs. When truncated MAPKKK4 (ΔMAPKKK4) was overexpressed in HEK293 cells, it was constitutively active and induced the activation of endogenous p38α, c-Jun N-terminal kinase (JNK)1/2 and extracellular signal-regulated kinase (ERK)2 in vivo. Kinase-inactive ΔMAPKKK4 partly inhibited the activation of p38α, JNK1/2 and ERK2 induced by stress, tumour necrosis factor α or epidermal growth factor, suggesting that MAPKKK4 might be physiologically involved in all three MAPK cascades. Co-expressed MAP kinase kinase (MKK)-1, MKK-4, MKK-3 and MKK-6 were activated in vivo by ΔMAPKKK4. All of the above MKKs purified from Escherichia coli were phosphorylated and activated by ΔMAPKKK4 immunoprecipitates in vitro. When expressed by lower plasmid doses, ΔMAPKKK4 preferentially activated MKK-3 and p38α in vivo. Overexpression of ΔMAPKKK4 did not activate the NF-κB pathway. Immunoprecipitation of endogenous MAPKKK4 by specific antibodies showed that MAPKKK4 was activated after the treatment of K562 cells with various stress conditions. As a broadly distributed kinase, MAPKKK4 might serve as a stress responder. MAPKKK4 is 91% identical with the recently described murine MEKK-4β and might be its human homologue. It is also identical with the recently cloned human MAP three kinase 1 except for the lack of an internal sequence homologous to the murine MEKK-4α isoform. Differences in the reported functional activities of the three kinases are discussed.

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Ludwig, S., K. Engel, A. Hoffmeyer, G. Sithanandam, B. Neufeld, D. Palm, M. Gaestel i U. R. Rapp. "3pK, a novel mitogen-activated protein (MAP) kinase-activated protein kinase, is targeted by three MAP kinase pathways." Molecular and Cellular Biology 16, nr 12 (grudzień 1996): 6687–97. http://dx.doi.org/10.1128/mcb.16.12.6687.

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Recently we have identified a mitogen-activated protein kinase (MAPK)-activated protein kinase, named 3pK (G. Sithanandam, F. Latif, U. Smola, R. A. Bernal, F.-M. Duh, H. Li, I. Kuzmin, V. Wixler, L. Geil, S. Shresta, P. A. Lloyd, S. Bader, Y. Sekido, K. D. Tartof, V. I. Kashuba, E. R. Zabarovsky, M. Dean, G. Klein, B. Zbar, M. I. Lerman, J. D. Minna, U. R. Rapp, and A. Allikmets, Mol. Cell. Biol. 16:868-876, 1996). In vitro characterization of the kinase revealed that 3pK is activated by ERK. It was further shown that 3pK is phosphorylated in vivo after stimulation of cells with serum. However, the in vivo relevance of this observation in terms of involvement of the Raf/MEK/ERK cascade has not been established. Here we show that 3pK is activated in vivo by the growth inducers serum and tetradecanoyl phorbol acetate in promyelocytic HL60 cells and transiently transfected embryonic kidney 293 cells. Activation of 3pK was Raf dependent and was mediated by the Raf/MEK/ERK kinase cascade. 3pK was also shown to be activated after stress stimulation of cells. In vitro studies with recombinant proteins demonstrate that in addition to ERK, members of other subgroups of the MAPK family, namely, p38RK and Jun-N-terminal kinases/stress-activated protein kinases, were also able to phosphorylate and activate 3pK. Cotransfection experiments as well as the use of a specific inhibitor of p38RK showed that these in vitro upstream activators also function in vivo, identifying 3pK as the first kinase to be activated through all three MAPK cascades. Thus, 3pK is a novel convergence point of different MAPK pathways and could function as an integrative element of signaling in both mitogen and stress responses.

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CUENDA, Ana, i Donna S. DOROW. "Differential activation of stress-activated protein kinase kinases SKK4/MKK7 and SKK1/MKK4 by the mixed-lineage kinase-2 and mitogen-activated protein kinase kinase (MKK) kinase-1". Biochemical Journal 333, nr 1 (1.07.1998): 11–15. http://dx.doi.org/10.1042/bj3330011.

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Overexpression of the protein kinases mixed-lineage kinase-2 (MLK2) or mitogen-activated protein kinase (MAPK) kinase kinase-1 (MEKK1) is known to trigger the activation of stress-activated protein kinase (SAPK1)/c-Jun N-terminal kinase (JNK). Here we demonstrate that MLK2 activates SAPK kinase-1 (SKK1)/MAPK kinase 4 (MKK4) and SKK4/MKK7, the two known direct activators of SAPK1/JNK (both in transfection studies and in vitro). In contrast, MEKK1 activates SKK1/MKK4 more efficiently than MLK2, but barely activates SKK4/MKK7. Since SKK4/MKK7 (but not SKK1/MKK4) is activated by interleukin-1 and tumour necrosis factor in several cells and tissues, we suggest that MEKK1 does not mediate the activation of SKK4/MKK7 and SAPK1/JNK induced by these pro-inflammatory cytokines. MLK2 and MEKK1 also activated SKK2/MKK3 and SKK3/MKK6, the direct upstream activators of SAPK2a/p38.

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Hirsch, Dale D., i Philip J. S. Stork. "Mitogen-activated Protein Kinase Phosphatases Inactivate Stress-activated Protein Kinase Pathwaysin Vivo". Journal of Biological Chemistry 272, nr 7 (14.02.1997): 4568–75. http://dx.doi.org/10.1074/jbc.272.7.4568.

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Kracht, M., O. Truong, N. F. Totty, M. Shiroo i J. Saklatvala. "Interleukin 1 alpha activates two forms of p54 alpha mitogen-activated protein kinase in rabbit liver." Journal of Experimental Medicine 180, nr 6 (1.12.1994): 2017–25. http://dx.doi.org/10.1084/jem.180.6.2017.

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We have identified in rabbits two hepatic forms of T669 peptide kinases that are very strongly activated after systemic injection with the inflammatory cytokine interleukin 1 (IL-1). The T669 peptide contains a major phosphorylation site of the epidermal growth factor receptor, threonine 699 and is a substrate for mitogen-activated protein (MAP) kinases. The kinases were purified to homogeneity and corresponded to 50- and 55-kD proteins on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Amino acid sequencing of 12 tryptic peptides of both kinases identified them as p54 MAP kinase alpha. This kinase belongs to the novel family of stress-activated protein kinases. This is the first evidence of IL-1 activating a specific protein kinase in vivo.

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Sun, Binggang, Hui Ma i Richard A. Firtel. "DictyosteliumStress-activated Protein Kinase α, a Novel Stress-activated Mitogen-activated Protein Kinase Kinase Kinase-like Kinase, Is Important for the Proper Regulation of the Cytoskeleton". Molecular Biology of the Cell 14, nr 11 (listopad 2003): 4526–40. http://dx.doi.org/10.1091/mbc.e03-01-0039.

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Mitogen-activated protein kinase cascades regulate various cellular functions, including growth, cell differentiation, development, and stress responses. We have identified a new Dictyostelium kinase (stress-activated protein kinase [SAPK]α), which is related to members of the mixed lineage kinase class of mitogen-activated protein kinase kinases. SAPKα is activated by osmotic stress, heat shock, and detachment from the substratum and by a membrane-permeable cGMP analog, a known regulator of stress responses in Dictyostelium. SAPKα is important for cellular resistance to stresses, because SAPKα null cells exhibit reduced viability in response to osmotic stress. We found that SAPKα mutants affect cellular processes requiring proper regulation of the actin cytoskeleton, including cell motility, morphogenesis, cytokinesis, and cell adhesion. Overexpression of SAPKα results in highly elevated basal and chemoattractant-stimulated F-actin levels and strong aggregation and developmental defects, including a failure to polarize and chemotax, and abnormal morphogenesis. These phenotypes require a kinase-active SAPKα. SAPKα null cells exhibit reduced chemoattractant-stimulated F-actin levels, cytokinesis, developmental and adhesion defects, and a motility defect that is less severe than that exhibited by SAPKα-overexpressing cells. SAPKα colocalizes with F-actin in F-actin–enriched structures, including membrane ruffles and pseudopodia during chemotaxis. Although SAPKα is required for these F-actin–mediated processes, it is not detectably activated in response to chemoattractant stimulation.

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Tibbles, L. A., i J. R. Woodgett. "The stress-activated protein kinase pathways". Cellular and Molecular Life Sciences (CMLS) 55, nr 10 (1.08.1999): 1230–54. http://dx.doi.org/10.1007/s000180050369.

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Rozprawy doktorskie na temat "Stress activated protein kinase"

Adams, Deanna Grace. "Characterization of the stress-activated protein kinase, MEKK3". Diss., The University of Arizona, 2002. http://hdl.handle.net/10150/279970.

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The cAMP-dependent protein kinase, PKA, mediates diverse cellular processes including proliferation and differentiation, as well as the phosphorylation of proteins involved in cell death and survival such as BAD and GSK-3beta. In this work, I demonstrate that PKA phosphorylates the stress-activated protein kinase, MEKK3 in vivo and in vitro. When (His)6FLAG·MEKK3 was expressed in Sf9 insect cells and purified with Ni-Sepharose, we identified 14-3-3 protein by liquid chromatography and electrospray tandem mass spectrometry (LC-MS) as co-purifying with recombinant MEKK3. The yeast two hybrid system was also utilized to identify 14-3-3 as interacting proteins with MEKK3 as well as Bcl-xL. The interaction between MEKK3 and Bcl-xL was specific for the caspase-cleaved Bcl-x L which suggests a role for MEKK3 in apoptotic signaling pathways. However, the physiological significance of this interaction is unclear since caspase-cleaved Bcl-xL did not act as a MEKK3 substrate or alter MEKK3 kinase activity. Since 14-3-3 proteins have been reported to interact with proteins through phosphoserine, we sequenced (His)6FLAG·MEKK3 by LC-MS to identify phosphorylated amino acids. Of the tryptic peptides sequenced, two consisted of amino acids 164--174 and 335--349 and serines 166 and 337 were phosphorylated within the respective peptides. Phosphorylation of both serines was localized within two consensus PKA phosphorylation sites, RXX(S/T). PKA activators such as serum and forskolin increased phosphorylation of endogenous MEKK3 at Ser166 as well as the preferential recruitment of phospho-MEKK3 with 14-3-3. These results connect the stress-activated pathways regulated by MEKK3 with pathways regulated by PKA.

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Brancho, Deborah Marie. "Regulation and Function of Stress-Activated Protein Kinase Signal Transduction Pathways: A Dissertation". eScholarship@UMMS, 2005. https://escholarship.umassmed.edu/gsbs_diss/101.

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The c-Jun NH2-terminal kinase (JNK) group and the p38 group of mitogen-activated protein kinases (MAPK) are stress-activated protein kinases that regulate cell proliferation, differentiation, development, and apoptosis. These protein kinases are involved in a signal transduction cascade that includes a MAP kinase (MAPK), a MAP kinase kinase (MAP2K), and a MAP kinase kinase kinase (MAP3K). MAPK are phosphorylated and activated by the MAP2K, which are phosphorylated and activated by various MAP3K. The work presented in this dissertation focuses on understanding the regulation and function of the JNK and p38 MAPK pathways. Two different strategies were utilized. First, I used molecular and biochemical techniques to examine how MAP2K and MAP3K mediate signaling specificity and to define their role in the MAPK pathway. Second, I used gene targeted disruption studies to determine the in vivo role ofMAP2K and MAP3K in MAPK activation. I specifically used these approaches to examine: (1) docking interactions between p38 MAPK and MAP2K [MKK3 and MKK6 (Chapter II)]; (2) the differential activation of p38 MAPK by MAP2K [MKK3, MKK4, and MKK6 (Chapter III)]; and (3) the selective involvement of the mixed lineage kinase (MLK) group of MAP3K in JNK and p38 MAPK activation (Chapter IV and Appendix). In addition, I analyzed the role of the MKK3 and MKK6 MAP2K in cell proliferation and the role of the MLK MAP3K in adipocyte differentiation (Chapter III and Chapter IV). Together, these data provide insight into the regulation and function of the stress-activated MAPK signal transduction pathways.

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Ferreiro, Neira Isabel. "Transcriptional regulation by the mammalian stress-activated protein kinase p38". Doctoral thesis, Universitat Pompeu Fabra, 2011. http://hdl.handle.net/10803/80661.

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Regulation of transcription by Stress Activated Protein Kinases (SAPKs) is an essential aspect for adaptation to extracellular stimuli. In mammals, the activation of the p38 SAPK results in the regulation of gene expression through the direct phosphorylation of several transcription factors. However, how p38 SAPK regulates the proper gene expression program of adaptation to stress as well as the basic mechanisms used by the SAPK remains uncharacterized. The results displayed in this manuscript show that the p38 SAPK plays a central role in the regulation of gene expression upon stress, as up to 80% of the upregulated genes are p38 SAPK dependent. Moreover, we also observed that a specific set of genes were upregulated in response to each specific stimuli, and just a small set of genes were commonly up-regulated by several stresses, which involves mainly transcription factors. In addition, we observed that, to proper regulate gene transcription, the p38 SAPK is recruited to stress-induced promoters via its interaction with transcription factors. Additionally, p38 activity allows the recruitment of RNA polymerase II and the MAPKK MKK6 to stress-responsive promoters. The presence of active p38 SAPK at open reading frames also suggests the involvement of the SAPK in elongation. Altogether, the results showed in this manuscript establish the p38 SAPK as an essential regulator in the transcriptional response to stress, as well as define new roles for p38 in the regulation of transcription in response to stress.
La regulación de la transcripción por las Proteínas Quinasas activadas por Estrés (SAPKs) es un aspecto esencial para la adaptación a los estímulos extracelulares. En mamíferos, la activación de la SAPK p38 da lugar a la regulación de la expresión génica a través de la fosforilación de varios factores de transcripción. Sin embargo, cómo p38 SAPK regula el programa de expresión génica de adaptación al estrés así como los mecanismos utilizados por la SAPK permanece sin caracterizar. Los resultados presentados en este manuscrito muestran que p38 SAPK juega un rol central en la regulación de la expresión génica en respuesta a estrés, ya que hasta el 80% de los genes inducidos son dependientes de p38 SAPK. También observamos que en respuesta a cada tipo de estrés se induce un grupo de genes específicos, y sólo hay una pequeña respuesta de genes comunes a los diferentes tipos de estrés la cual engloba principalmente factores de transcripción. Además, hemos observado que para regular la transcripción, p38 se recluta a los promotores de respuesta a estrés a través de su interacción con factores de transcripción. Asimismo, la actividad de p38 permite el reclutamiento de la RNA Polimerasa II y de la MAPKK MKK6 a los promotores inducidos por estrés. La presencia de p38 activa en las regiones codificantes sugiere su participación durante la elongación. En conjunto, los resultados mostrados en este manuscrito establecen a p38 como un regulador esencial de la transcripción en respuesta a estrés, así como definen nuevas funciones de p38 en la regulación de la transcripción en respuesta a estrés.

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Auciello, Francesca Romana. "Canonical and non-canonical regulation of AMP-activated protein kinase". Thesis, University of Dundee, 2015. https://discovery.dundee.ac.uk/en/studentTheses/2720a2b7-3f1e-445c-b008-c5c235f35395.

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The AMP-activated protein kinase (AMPK) is a sensor of cellular energy stress that, once activated, promotes ATP-producing process while it switches off ATP-consuming pathways, in order to restore the cellular energetic balance under conditions of stress. Activation of AMPK is dependent on the phosphorylation of the residue Thr172 in its α subunit. This phosphorylation is generally mediated by the known tumour suppressor LKB1, but also CaMKKβ has been shown to phosphorylate AMPK. As its name suggests, AMPK is also activated by the binding of AMP to its γ subunit. This binding causes a >10 fold allosteric stimulation, promotes phosphorylation of Thr172 by upstream kinases and protects AMPK from dephosphorylation of Thr172 by protein phosphatase(s). In 2010 it was reported that oxidative stress mediated by H₂O₂ activated AMPK by increasing the cellular AMP:ATP and ADP:ATP ratios (Hawley et al, 2010). However, the same year another work suggested that the mechanism of activation of AMPK by H₂O₂was direct, independent of AMP and involved the oxidation of two cysteine residues in the α subunit of AMPK (Zmijewski et al, 2010). Given this discrepancy, here we provided evidence that H₂O₂, generated by addition of glucose oxidase in the cell medium, activates AMPK mostly through an increase of AMP:ATP and ADP:ATP ratios, as previously suggested in our laboratory. However, it seems that there might be a second, minor mechanism of activation that is independent of the changes in cellular nucleotides. This second mechanism was not identified in our previous work because we were not aware of how rapidly a single bolus of H₂O₂ can be metabolized by the antioxidant defences of the cell. We could not identify the alternative mechanism of activation by H₂O₂but showed that H₂O₂ could protect Thr172 from dephosphorylation, which might suggest a direct effect of H₂O₂ on the phosphatase(s) dephosphorylating AMPK. However, since the identity of this phosphatase(s) remains unclear, we could not rule out the possibility that the protection from dephosphorylation that we observed could still be mediated by the increase in AMP:ATP and ADP:ATP ratios. Moreover, it remains still possible that a direct effect of H₂O₂ on AMPK might be responsible for the small but significant activation we detected in cell expressing a nucleotides-insensitive mutant of AMPK. Recently, a new crystal structure of AMPK obtained by Xiao et al (2013) provided new insights about AMPK structure and regulation. In particular, the authors identified a new binding pocket located at the interface between the N-lobe of the α-kinase domain and the β-CBM of AMPK, which appeared to be the binding site for two direct activators of AMPK: A769662 and 991. Here we confirm that this novel binding pocket is indeed the binding site for both A769662 and 991, and provide evidence that another direct activator of AMPK, MT63-78, also binds at the same site. Mutation of two important residues in this pocket (Lys29 and Lys31 of the α2 subunit) abolished the allosteric stimulation of AMPK by A769662, 991 and MT63-78 while it had no effect on allosteric stimulation by AMP. However, we also showed that the same mutation abolished protection against Thr172 dephosphorylation not only by A769662, 991 and MT63-78, but also by phenformin and H2O2, which are known to activate AMPK by increasing the AMP:ATP and ADP:ATP ratios. These data show that the integrity of this pocket is important for the effect of AMP to protect against Thr172 dephosphorylation, but not for its ability to cause allosteric stimulation. Moreover, in HEK-293 cell stably expressing an α2 subunit carrying the mutation of both Lys29 and Lys31, the basal activity of AMPK due to Thr172 phosphorylation was almost 6-fold less than in cells expressing wild-type α2. This result pointed out for the first time that there might be a natural ligand binding in the newly discovered binding pocket that is not able to bind to the double mutant, explaining the difference in activity observed. However the identity of this possible natural ligand remains unclear and more studies will be necessary to uncover it.

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Foltz, Ian Nevin. "Regulation of the stress-activated protein kinase pathways in hematopoietic cells". Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp02/NQ38887.pdf.

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O'Ferrall, Erin K. "Phosphorylation of the neurofilament heavy subunit by stress-activated protein kinase". Thesis, McGill University, 2000. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=33433.

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Stress-activated protein kinases (SAPKs) were previously implicated in the phosphorylation of the neurofilament heavy subunit (NFH). This study presents direct evidence that stress-induced phosphorylation of NFH in both differentiated PC12 cells and cultured sensory neurons is inhibited by CEP-1347 (KT7515), a specific inhibitor of SAPK activation. In addition, long-term treatment of unstressed sensory neurons with CEP-1347 decreased the phosphorylation state of NFH in neurites. CEP-1347 differentially inhibited the activation of various SAPK isoforms in neuronal cell body and neurite fractions. Specifically, activation of a 55 kDa SAPK isoform in the neurite fraction was highly sensitive to CEP-1347 inhibition, with an IC50 of about 0.02 muM, while IC50 values for other SAPK species were at least 10-fold higher. The data indicate that SAPKs are involved in both constitutive phosphorylation of axonal NFH and stress-induced phosphorylation of perikaryal NFH in cultured sensory neurons and that SAPKs in the two neuronal compartments are activated by different signaling pathways.

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De, Zutter Gerard S. "Stress Activated Protein Kinase Regulation of Gene Expression in Apoptotic Neurons: A Dissertation". eScholarship@UMMS, 2001. https://escholarship.umassmed.edu/gsbs_diss/168.

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Summary Basic biological processes require gene expression. Tightly regulated molecules known as transcription factors mediate the expression of genes in development and disease. Signal transduction pathways, which respond to environmental cues or stressors are major regulators of the transcription factors. Use of macromolecular synthesis inhibitors in models of normal neurodevelopment and neurodegenerative cell death has led to the discovery that gene expression is required for these processes to occur (Martin et. al.,(1988), J Cell Biol 106p829). To date, however, the identities of very few of the genes required in these events have been revealed. Hence, the activation or requirement of specific signaling pathways leading to the expression of known apoptotic genes is not well established. Utilizing the neurothrophic factor deprivation and neurotoxin models of programmed cell death we address these gaps in our understanding of the molecular mechanism of apoptosis as it occurs in neuronal cell death. Nerve growth factor (NGF) withdrawal from PC12 cells leads to the activation of p38 and apoptosis. The functional significance of 38 activation in this paradigm of cell death is not known. To increase our understanding of apoptosis I examined the requirement for p38 activity in pro-apoptotic gene expression in PC12 cells. I performed a subtractive hybridization that led to the identification of the monoamine oxidase (MAG) gene as induced in response to NGF withdrawal. Using the p38 inhibitor PD169316 I showed that the NGF withdrawal stimulated induction of the MAG gene and apoptosis is blocked by inhibition of the p38 MAP kinase pathway. I also determined that the MAG inhibitor clorgyline blocked cell death indicating that MAG activity contributes to the cell death caused by NGF withdrawal. Together, these data indicate that the p38 MAP kinase pathway targets the MAG gene in response to apoptotic stimuli. To study the requirement for the JNK signaling pathway in neurodegeneration I stimulated primary cortical neurons with the neurotoxin arsenite. Arsenite treatment of primary neurons leads to both JNK and p38 activation and subsequently apoptosis. Utilizing transgenic mice lacking the JNK3 gene I demonstrated that JNK3 specifically contributes to the effects of arsenite in these cells. Ribonuclease protection assays were used to identify Fas ligand as a molecule whose arsenite-induced expression is dependent on the JNK3 signal transduction pathway. Furthermore, I have shown that neurons deficient in signaling mediated by the receptor for Fas ligand are resistant to cell death due to arsenite treatment. These results in total have established that the JNK3 mediated expression of Fas ligand contributes to the arsenite induced death of cortical neurons. In summary, the work presented in these studies identifies the JNK and p38 MAP kinase signal transduction pathways as mediators of apoptosis in neuronal cells. Importantly, I have provided evidence that these stress activated pathways are responsible for the expression of specific genes in apoptotic neuronal cells.

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Cheetham, Jill. "The Regulation of the Hog1 Stress Activated Protein Kinase in Candida albicans". Thesis, University of Newcastle Upon Tyne, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.489302.

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Yates, Alexandra Caroline. "Stress-activated protein kinases and neurodegenerative disease". Thesis, King's College London (University of London), 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.287325.

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Schroder, Wayne Ashley. "Cloning and Characterisation of the Human SinRIP Proteins". Thesis, Griffith University, 2003. http://hdl.handle.net/10072/366190.

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This thesis describes the cloning and characterisation of a novel human gene and its protein products, which have been designated SAPK- and Ras-interacting protein (SinRIP). SinRIP shares identity with JC310, a partial human cDNA that was previously identified a candidate Ras-inhibitor (Colicelli et al., 1991, Proc Natl Acad Sci USA 88, p. 2913). In this study, it was shown that SinRIP is a member of an orthologous family of proteins that is conserved from yeast to mammals and contains proteins involved in Ras- and SAPK-mediated signalling pathways. Comparison of this family of proteins showed that human SinRIP contains a potential Ras-binding domain (RBD; residues 279-354), a PH-like domain (PHL; 376-487), and a highly conserved novel region designated the CRIM (134-265). Several other potential targeting sites, such as nuclear localisation signals and target sites for kinases, were identified within the SinRIP sequence. The human SinRIP gene is unusually large (>280 kbp) and is located on chromosome 9 at 9q34. SinRIP mRNA was detected in a wide variety of tissue-types and cell lines by RT-PCR, and the SinRIP sequences in the EST database were derived from an diverse array of tissues, suggesting a widespread or ubiquitous expression. Northern blot analysis revealed the highest levels in skeletal muscle and heart tissue. However, the steady-state levels of SinRIP mRNA vary greatly from cell to cell, and SinRIP expression is likely to be regulated at multiple post-transcriptional levels. It was shown that SinRIP mRNA is likely to be translated inefficiently by the normal cap-scanning mechanism, due to the presence of a GC-rich and structured 5’-UTR, which also contains upstream ORFs. Alternative polyadenylation signals in the SinRIP 3’-UTR can be used, resulting in the expression of short and long SinRIP mRNA isoforms. Several potential A/T-rich regulatory elements were also identified in SinRIP mRNA, which may target specific SinRIP mRNA isoforms for rapid degradation. Importantly, it was shown that SinRIP mRNA is alternatively spliced, resulting in the production of distinct SinRIP protein isoforms. Three isoforms, SinRIP2-4, were definitively identified by RT-PCR and full-length cloning. The SinRIP isoforms contain deletions in conserved regions, and are likely to have biochemical characteristics that are different to full-length SinRIP1. SinRIP2 is C-terminally truncated and lacks the PHL domain and part of the RBD, and relatively high levels of SinRIP2 expression arelikely to occur in kidneys. The RBD is disrupted in SinRIP3, but all other domains are intact, and RT-PCR analyses suggest that SinRIP3 is present in some cells at levels comparable to SinRIP1. A rabbit polyclonal antiserum against SinRIP was generated and detected endogenous SinRIP proteins. Using the anti-SinRIP antibody in immunoblots, multiple SinRIP isoforms were observed in most cell types. SinRIP1 and another endogenous SinRIP protein, likely to be SinRIP3, were detected in most cell lines, and appear to be are the major SinRIP proteins expressed in most cells. The subcellular localisation of both recombinant and endogenous SinRIP proteins was investigated by immunofluorescence assays and biochemical fractionation. Recombinant SinRIP1 protein was found in the cytoplasm and associated with the plasma membrane. In contrast, the SinRIP2 protein was predominantly nuclear, with only low-level cytoplasmic staining observed. The endogenous SinRIP proteins, likely to comprise these and other SinRIP isoforms, were found in both the nucleus and cytoplasm. SinRIP1 interacted with GTP-bound (active) Ras, but not GDP-bound (inactive) Ras, in an in vitro assay, and also co-localised with activated H- and K-Ras in cells. The binding profile observed is typical of Ras-effectors, and SinRIP did not inhibit signalling by the Ras proteins, suggesting that it is not likely to be a Ras-inhibitor. It was also shown that SinRIP1 and SinRIP2 both interact and colocalise with c-Jun NH2- terminal kinase (JNK). Both SinRIP proteins were able to recruit JNK to their respective sub-cellular compartments. These interactions suggest an adaptor role for SinRIP in the Ras and/or JNK pathways. In addition, Sam68 was isolated as a SinRIP-binding protein in a yeast two-hybrid screen. Sam68 was shown to colocalise with SinRIP2 and endogenous SinRIP proteins, but not SinRIP1. Further colocalisation studies showed that endogenous SinRIP proteins localise in nuclear structures that may be associated with pre-mRNA splicing. Likely functions for SinRIP, as indicated by experimental results and studies of the orthologues of SinRIP in other species, are discussed.
Thesis (PhD Doctorate)
Doctor of Philosophy (PhD)
School of Biomolecular and Biomedical Sciences
Faculty of Science
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Książki na temat "Stress activated protein kinase"

Posas, Francesc, i Angel R. Nebreda, red. Stress-Activated Protein Kinases. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/978-3-540-75569-2.

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Francesc, Posas, i Nebreda Angel R, red. Stress-activated protein kinases. New York: Springer, 2008.

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Dai, Tianang. Characterization of a novel stress-activated protein kinase pathway. Ottawa: National Library of Canada, 1996.

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Chang, Malcolm Elliott. Role of the stress activated protein kinases (sapk's) in mediating resistance to the antineoplastic agent adriamycin (ADR). Ottawa: National Library of Canada, 1998.

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Cordero, Mario D., i Benoit Viollet, red. AMP-activated Protein Kinase. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-43589-3.

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Randall, Susan. Interactions among the mitogen-activated protein kinase cascades and the identification of a novel cdc2-related protein kinase. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1999.

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Ho, Jenny Mei-Yen. The activation of mitogen-activated protein kinase pathways by the TEL-JAK2 oncoprotein. Ottawa: National Library of Canada, 2000.

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Glogowski, Emily Anne Cherry. Effect of high glucose on endothelin-1 and platelet-derived growth factor stimulation of mesangial cell protein kinase C and mitogen-activated protein kinase. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1999.

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MAP kinase signaling protocols. Wyd. 2. New York, N.Y: Humana Press, 2010.

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Asefaw, Senai. Stimulation of myocardial AMP-activated protein kinase by AICAR increases cardiac glucose uptake and causes GLUT4 and GLUT1 translocation in vivo. [New Haven, Conn: s.n.], 1999.

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Części książek na temat "Stress activated protein kinase"

Gewies, Andreas, Jürgen Ruland, Alexey Kotlyarov, Matthias Gaestel, Shiri Procaccia, Rony Seger, Shin Yasuda i in. "Mitogen- and Stress-Activated Protein Kinase 1". W Encyclopedia of Signaling Molecules, 1081. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100809.

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Horstkorte, Rüdiger, Bettina Büttner, Kaya Bork, Navdeep Sahota, Sarah Sabir, Laura O’Regan, Joelle Blot i in. "Nuclear Mitogen- and Stress-Activated Protein Kinase-1". W Encyclopedia of Signaling Molecules, 1275. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100951.

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Bharti, Jyotsna, Sahil, Sahil Mehta, Shaban Ahmad, Baljinder Singh, Asish K. Padhy, Neha Srivastava i Vimal Pandey. "Mitogen-Activated Protein Kinase, Plants, and Heat Stress". W Harsh Environment and Plant Resilience, 323–54. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-65912-7_13.

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Seo, Shigemi, i Yuko Ohashi. "Mitogen-Activated Protein Kinases and Wound Stress". W Results and Problems in Cell Differentiation, 53–63. Berlin, Heidelberg: Springer Berlin Heidelberg, 2000. http://dx.doi.org/10.1007/978-3-540-49166-8_5.

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Naor, Zvi, i Jacob Hermon. "Calcium-Activated Phospholipid-Dependent Protein Kinase: A Novel Signal Transduction Mechanism in the Pituitary". W Neuroendocrine Correlates of Stress, 325–36. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-8553-0_18.

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Pelosse, Martin, Malgorzata Tokarska-Schlattner i Uwe Schlattner. "AMP-Activated Protein Kinase: A Metabolic Stress Sensor in the Heart". W Cardiac Cytoarchitecture, 187–225. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-15263-9_10.

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Ara, Hussain, i Alok Krishna Sinha. "Role of Mitogen-Activated Protein Kinase Cascade in Combating Abiotic Stress in Plants". W Elucidation of Abiotic Stress Signaling in Plants, 207–29. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4939-2211-6_8.

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Toska, K., R. Kleppe i J. Haavik. "Mechanisms of Tyrosine Hydroxylase Activation by Stress Activated Protein Kinases". W Chemistry and Biology of Pteridines and Folates, 121–26. Boston, MA: Springer US, 2002. http://dx.doi.org/10.1007/978-1-4615-0945-5_20.

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Conrad, P. William, David E. Millhorn i Dana Beitner-Johnson. "Hypoxia Differentially Regulates the Mitogen- and Stress-Activated Protein Kinases". W Oxygen Sensing, 293–302. Boston, MA: Springer US, 2002. http://dx.doi.org/10.1007/0-306-46825-5_28.

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Roychoudhury, Aryadeep, i Aditya Banerjee. "Abscisic Acid Signaling and Involvement of Mitogen Activated Protein Kinases and Calcium-Dependent Protein Kinases During Plant Abiotic Stress". W Mechanism of Plant Hormone Signaling under Stress, 197–241. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2017. http://dx.doi.org/10.1002/9781118889022.ch9.

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Streszczenia konferencji na temat "Stress activated protein kinase"

Torres Acosta, M. A., S. Weinberg, K. Helmin, L. Morales-Nebreda, C. P. Reyes Flores, A. M. Joudi i B. D. Singer. "AMP-Activated Protein Kinase Is Required for Treg Cell Function During Microenvironmental Stress". W American Thoracic Society 2022 International Conference, May 13-18, 2022 - San Francisco, CA. American Thoracic Society, 2022. http://dx.doi.org/10.1164/ajrccm-conference.2022.205.1_meetingabstracts.a1215.

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Kim, Hong-Gyum, Margarita Malakhova, Igor D'Angelo, Ann Bode i Zigang Dong. "Abstract 2680: Nonautoinhibitory properties of the C-terminal helix of the mitogen- and stress-activated protein kinase 1". W Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-2680.

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Lopes, Ana P., Joel van Roon, Sofie Blokland, Maojie Wang, Eleni Chouri, Aike A. Kruize, Boudewijn Burgering, Marzia Rossato, Timothy R. Radstake i Maarten Hillen. "AB0176 MITOGEN- AND STRESS-ACTIVATED PROTEIN KINASE-1 (MSK1) AS THE LINK BETWEEN MIR-130A-DYSREGULATION AND CDC2-ACTIVATION IN SJöGREN’S SYNDROME". W Annual European Congress of Rheumatology, EULAR 2019, Madrid, 12–15 June 2019. BMJ Publishing Group Ltd and European League Against Rheumatism, 2019. http://dx.doi.org/10.1136/annrheumdis-2019-eular.6806.

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Sundar, I., S. Rajendrasozhan, H. Yao, S. Chung i I. Rahman. "Mitogen- and Stress-Activated Protein Kinase-1 (MSK1) Is Involved in Cigarette Smoke-Induced Chromatin Remodeling in Human Lung Epithelial Cells and Mouse Lung." W 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.a4170.

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Ye, Jianfeng, Baoguo Chen i Lisa X. Xu. "Shear Stress Effect on the Production of Nitric Oxide in Cultured Rat Aorta Endothelial Cells". W ASME 2002 International Mechanical Engineering Congress and Exposition. ASMEDC, 2002. http://dx.doi.org/10.1115/imece2002-33074.

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Atherosclerotic lesions tend to develop in regions where there are separations from unidirectional laminar blood flow, typically near branches, bifurcations, regions of arterial narrowing, and curvatures in the arteries (1, 2). Obviously, homodynamic forces play a key role in atherosclerosis. Studies also indicate that vascular endothelium function disturbance, especially impairment of endothelium dependent vasodilation, is involved (3). Shear stress affects endothelial cells in many ways, such as cytoskeletal rearrangement, decrease of intracellular pH, release of PGI2 and some growth factors (PDGF, FGF, ECGF, TGF-b, etc), activation of IP3 and mitogen-activated protein kinases, and the significant increase in the production of nitric oxide (1,2,4,5). As an important function factor of vascular endothelial cells, nitric oxide (NO) is closely related to the endothelial dysfunction and atherosclerosis (6). Endothelial derived nitric oxide involves in many events in the vasculature, including vasodilation, inhibition of platelet aggregation, adhesion molecule expression, and vascular smooth muscle proliferation, which are directly or indirectly related to atherosclerosis. Endothelial cells release NO more potently in response to increased shear stress than to agonists that raise intracellular free calcium concentration [Ca2+]i. Studies have indicated that NO production increases with a calcium/CaM dependent manner in the first few minutes after exposed to shear stress, followed by a sustained NO production that occurs more than 30min which is Ca2+ independent (7). The activation of eNOS by shear stress, which modulated by Ca/CaM, G protein, tyrosine kinase phosphorylation and eNOS gene expression, is responsible for the increase of NO production (8). However, the contribution of extracellular calcium to the production of NO is somewhat contradictory.

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Guo, X. Edward, Erica Takai, Kai Liu i Xiaodong Wang. "An Exploration of Cell Stress and Deformation Under Shear Flow". W ASME 2001 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2001. http://dx.doi.org/10.1115/imece2001/bed-23160.

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Abstract The biological response of bone cells (osteoblasts and/or osteocytes) to mechanical loading is an important basic science topic in the mechanism of mechano-signal transduction in bone adaptation to mechanical loading. The characterization of this mechanism of signal transduction is crucial in the understanding of the etiology of age-related bone loss, bone loss during space flight and the optimal design of implants for total joint replacements. It has been hypothesized that deformation-generated fluid shear stress is one of the major mechanical stimuli that bone cells respond to. Many in vitro experiments utilize a parallel-plate flow chamber by imposing fluid shear stress on cultured osteoblasts. For example, changes in intracellular Ca++ levels and mitogen-activated protein kinase (MAPK) phosphorylation has been quantified in response to applied shear flow [1,2]. In these studies, the flow shear stress at the wall of the flow chamber τ wall = 6 μ Q w h 2 , where Q is the volumetric flow rate, w and h are the width and height of the flow chamber, respectively, and μ is the media viscosity. However, this wall shear stress may not indicate the actual stress state which bone cells experience, which depends on the details of the flow-cell interaction, including the mechanical properties of the cell, the attachment condition of the cell to the wall as well as the cell density. In order to obtain a quantitative relationship between the biological response of bone cells to applied shear flow, it is necessary to quantify in detail the flow-cell interaction in a typical shear flow experiment. The objective of this study was to quantify the shear stress within the cell under applied shear flow, incorporating fully coupled flow and solid deformation analyses using the finite element technique. Specifically, we examined the influence of the elastic modulus of the cell and the spacing distance between cells on the shear stress within the cell.

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Paniagua-Morales, Oscar, Laura Johnston, Leonid Serebreni, Gigi Liu, Paul Hassoun i Mahendra Damarla. "Abstract 1350: Mitogen activated protein kinase activated protein kinase 2 (MK2) signaling in non-small cell lung carcinoma". W 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.am2014-1350.

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Parniani, Ahmad, Hasina Maredia, Rachel L. Damico, Bo S. Kim, Todd M. Kolb, Allen Myers, Paul M. Hassoun i Mahendra Damarla. "Mitogen Activated Protein Kinase-Activated Protein Kinase 2 Deficiency Is Protective Against LPS-Mediated Apoptosis Induced Acute Lung Injury". W 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.a3668.

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Chen, Chien-Yu, Da-Tian Bau, Ming-Hsui Tsai, Yuan-Man Hsu, Tin-Yun Ho, Hung-Jin Huang, Yea-Huey Chang, Fuu-Jen Tsai, Chang-Hai Tsai i Calvin Yu-Chian Chen. "Drug Design for AMP-Activated Protein Kinase Agonists in Silico". W 2009 2nd International Conference on Biomedical Engineering and Informatics. IEEE, 2009. http://dx.doi.org/10.1109/bmei.2009.5304901.

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Krishna, Sankar Narayan, Chi-Hao Luan, George Minasov, Ludmilla Shuvalova, Rebecca L. Farmer, Antoinette Nibbs, Karl A. Scheidt, Wayne F. Anderson i Raymond C. Bergan. "Abstract 4751: Structure and inhibition of mitogen-activated protein kinase kinase 4 (MEK4): A prostate cancer pro-invasion protein". W Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-4751.

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Raporty organizacyjne na temat "Stress activated protein kinase"

Liu, Wei, i Javdutt Vadgama. Characterization of the Mechanisms of IGF-I-Mediated Stress-Activated Protein Kinase Activation in Human Breast Cancer Cell MCF-7. Fort Belvoir, VA: Defense Technical Information Center, lipiec 2000. http://dx.doi.org/10.21236/ada392429.

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Droby, Samir, Michael Wisniewski, Ron Porat i Dumitru Macarisin. Role of Reactive Oxygen Species (ROS) in Tritrophic Interactions in Postharvest Biocontrol Systems. United States Department of Agriculture, grudzień 2012. http://dx.doi.org/10.32747/2012.7594390.bard.

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To elucidate the role of ROS in the tri-trophic interactions in postharvest biocontrol systems a detailed molecular and biochemical investigation was undertaken. The application of the yeast biocontrol agent Metschnikowia fructicola, microarray analysis was performed on grapefruit surface wounds using an Affymetrix Citrus GeneChip. the data indicated that 1007 putative unigenes showed significant expression changes following wounding and yeast application relative to wounded controls. The expression of the genes encoding Respiratory burst oxidase (Rbo), mitogen-activated protein kinase (MAPK) and mitogen-activated protein kinase kinase (MAPKK), G-proteins, chitinase (CHI), phenylalanine ammonia-lyase (PAL), chalcone synthase (CHS) and 4-coumarate-CoA ligase (4CL). In contrast, three genes, peroxidase (POD), superoxide dismutase (SOD) and catalase (CAT), were down-regulated in grapefruit peel tissue treated with yeast cells. The yeast antagonists, Metschnikowia fructicola (strain 277) and Candida oleophila (strain 182) generate relatively high levels of super oxide anion (O2−) following its interaction with wounded fruit surface. Using laser scanning confocal microscopy we observed that the application of M. fructicola and C. oleophila into citrus and apple fruit wounds correlated with an increase in H2O2 accumulation in host tissue. The present data, together with our earlier discovery of the importance of H₂O₂ production in the defense response of citrus flavedo to postharvest pathogens, indicate that the yeast-induced oxidative response in fruit exocarp may be associated with the ability of specific yeast species to serve as biocontrol agents for the management of postharvest diseases. Effect of ROS on yeast cells was also studied. Pretreatment of the yeast, Candida oleophila, with 5 mM H₂O₂ for 30 min (sublethal) increased yeast tolerance to subsequent lethal levels of oxidative stress (50 mM H₂O₂), high temperature (40 °C), and low pH (pH 4). Suppression subtractive hybridization analysis was used to identify genes expressed in yeast in response to sublethal oxidative stress. Transcript levels were confirmed using semi quantitative reverse transcription-PCR. Seven antioxidant genes were up regulated. Pretreatment of the yeast antagonist Candida oleophila with glycine betaine (GB) increases oxidative stress tolerance in the microenvironment of apple wounds. ROS production is greater when yeast antagonists used as biocontrol agents are applied in the wounds. Compared to untreated control yeast cells, GB-treated cells recovered from the oxidative stress environment of apple wounds exhibited less accumulation of ROS and lower levels of oxidative damage to cellular proteins and lipids. Additionally, GB-treated yeast exhibited greater biocontrol activity against Penicillium expansum and Botrytis cinerea, and faster growth in wounds of apple fruits compared to untreated yeast. The expression of major antioxidant genes, including peroxisomal catalase, peroxiredoxin TSA1, and glutathione peroxidase was elevated in the yeast by GB treatment. A mild heat shock (HS) pretreatment (30 min at 40 1C) improved the tolerance of M. fructicola to subsequent high temperature (45 1C, 20–30 min) and oxidative stress (0.4 mol-¹) hydrogen peroxide, 20–60 min). HS-treated yeast cells showed less accumulation of reactive oxygen species (ROS) than non-treated cells in response to both stresses. Additionally, HS-treated yeast exhibited significantly greater (P≥0.0001) biocontrol activity against Penicillium expansum and a significantly faster (Po0.0001) growth rate in wounds of apple fruits stored at 25 1C compared with the performance of untreated yeast cells. Transcription of a trehalose-6-phosphate synthase gene (TPS1) was up regulated in response to HS and trehalose content also increased.

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Anderson, C. W., M. A. Connelly, H. Zhang, J. A. Sipley, S. P. Lees-Miller, L. G. Lintott, Kazuyasu Sakaguchi i E. Appella. The human DNA-activated protein kinase, DNA-PK: Substrate specificity. Office of Scientific and Technical Information (OSTI), listopad 1994. http://dx.doi.org/10.2172/113929.

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Bakin, Andrei V. P38 Mitogen-Activated Protein Kinase in Metastasis Associated With Transforming Growth Factor Beta. Fort Belvoir, VA: Defense Technical Information Center, czerwiec 2005. http://dx.doi.org/10.21236/ada443019.

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Bakin, Andrei. p38 Mitogen-Activated Protein Kinase in Metastasis Associated with Transforming Growth Factor Beta. Fort Belvoir, VA: Defense Technical Information Center, czerwiec 2006. http://dx.doi.org/10.21236/ada456265.

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Bakin, Andrei V. P38 Mitogen-Activated Protein Kinase in Metastasis Associated with Transforming Growth Factor Beta. Fort Belvoir, VA: Defense Technical Information Center, czerwiec 2004. http://dx.doi.org/10.21236/ada427109.

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Coyner, Jennifer L. Differential Expression of Phosphorylated Mitogen-Activated Protein Kinase (pMAPK) in the Lateral Amygdala of Mice Selectively Bred for High and Low Fear. Fort Belvoir, VA: Defense Technical Information Center, czerwiec 2013. http://dx.doi.org/10.21236/ad1012913.

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Sessa, Guido, i Gregory Martin. MAP kinase cascades activated by SlMAPKKKε and their involvement in tomato resistance to bacterial pathogens. United States Department of Agriculture, styczeń 2012. http://dx.doi.org/10.32747/2012.7699834.bard.

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The research problem: Pseudomonas syringae pv. tomato (Pst) and Xanthomonas campestrispv. vesicatoria (Xcv) are the causal agents of tomato bacterial speck and spot diseases, respectively. These pathogens colonize the aerial parts of the plant and cause economically important losses to tomato yield worldwide. Control of speck and spot diseases by cultural practices or chemicals is not effective and genetic sources of resistance are very limited. In previous research supported by BARD, by gene expression profiling we identified signaling components involved in resistance to Xcvstrains. Follow up experiments revealed that a tomato gene encoding a MAP kinase kinase kinase (MAPKKKe) is required for resistance to Xcvand Pststrains. Goals: Central goal of this research was to investigate the molecular mechanisms by which MAPKKKεand associated MAP kinase cascades regulate host resistance. Specific objectives were to: 1. Determine whether MAPKKKεplays a broad role in defense signaling in plants; 2. Identify components of MAP kinase cascades acting downstream of MAPKKKε; 3. Determine the role of phosphorylation-related events in the function of MAPKKKε; 4. Isolate proteins directly activated by MAPKKKε-associatedMAPK modules. Our main achievements during this research program are in the following major areas: 1. Characterization of MAPKKKεas a positive regulator of cell death and dissection of downstream MAP kinase cascades (Melech-Bonfil et al., 2010; Melech-Bonfil and Sessa, 2011). The MAPKKKεgene was found to be required for tomato resistance to Xcvand Pstbacterial strains and for hypersensitive response cell death triggered by different R gene/effector gene pairs. In addition, overexpression analysis demonstrated that MAPKKKεis a positive regulator of cell death, whose activity depends on an intact kinase catalytic domain. Epistatic experiments delineated a signaling cascade downstream of MAPKKKεand identified SIPKK as a negative regulator of MAPKKKε-mediated cell death. Finally, genes encoding MAP kinase components downstream of MAPKKKεwere shown to contribute to tomato resistance to Xcv. 2. Identification of tomato proteins that interact with MAPKKKεand play a role in plant immunity (Oh et al., 2011). We identified proteins that interact with MAPKKKε. Among them, the 14-3-3 protein TFT7 was required for cell death mediated by several R proteins. In addition, TFT7 interacted with the MAPKK SlMKK2 and formed homodimersin vivo. Thus, TFT7 is proposed to recruit SlMKK2 and MAPKKK client proteins for efficient signal transfer. 3. Development of a chemical genetic approach to identify substrates of MAPKKKε-activated MAP kinase cascades (Salomon et al., 2009, 2011). This approach is based on engineering the kinase of interest to accept unnatural ATP analogs. For its implementation to identify substrates of MAPKKKε-activated MAP kinase modules, we sensitized the tomato MAP kinase SlMPK3 to ATP analogs and verified its ability to use them as phosphodonors. By using the sensitized SlMPK3 and radiolabeled N6(benzyl)ATP it should be possible to tag direct substrates of this kinase. 4. Development of methods to study immunity triggered by pathogen-associated molecular patterns (PAMPs) in tomato and N. benthamiana plants (Kim et al., 2009; Nguyen et al. 2010). We developed protocols for measuring various PTI-associatedphenotypes, including bacterial populations after pretreatment of leaves with PAMPs, induction of reporter genes, callose deposition at the cell wall, activation of MAP kinases, and a luciferase-based reporter system for use in protoplasts. Scientific and agricultural significance: Our research activities discovered and characterized a signal transduction pathway mediating plant immunity to bacterial pathogens. Increased understanding of molecular mechanisms of immunity will allow them to be manipulated by both molecular breeding and genetic engineering to produce plants with enhanced natural defense against disease. In addition, we successfully developed new biochemical and molecular methods that can be implemented in the study of plant immunity and other aspects of plant biology.

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Avni, Adi, i Gitta L. Coaker. Proteomic investigation of a tomato receptor like protein recognizing fungal pathogens. United States Department of Agriculture, styczeń 2015. http://dx.doi.org/10.32747/2015.7600030.bard.

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Maximizing food production with minimal negative effects on the environment remains a long-term challenge for sustainable food production. Microbial pathogens cause devastating diseases, minimizing crop losses by controlling plant diseases can contribute significantly to this goal. All plants possess an innate immune system that is activated after recognition of microbial-derived molecules. The fungal protein Eix induces defense responses in tomato and tobacco. Plants recognize Eix through a leucine-rich-repeat receptor- like-protein (LRR-RLP) termed LeEix. Despite the knowledge obtained from studies on tomato, relatively little is known about signaling initiated by RLP-type immune receptors. The focus of this grant proposal is to generate a foundational understanding of how the tomato xylanase receptor LeEix2 signals to confer defense responses. LeEix2 recognition results in pattern triggered immunity (PTI). The grant has two main aims: (1) Isolate the LeEix2 protein complex in an active and resting state; (2) Examine the biological function of the identified proteins in relation to LeEix2 signaling upon perception of the xylanase elicitor Eix. We used two separate approaches to isolate receptor interacting proteins. Transgenic tomato plants expressing LeEix2 fused to the GFP tag were used to identify complex components at a resting and activated state. LeEix2 complexes were purified by mass spectrometry and associated proteins identified by mass spectrometry. We identified novel proteins that interact with LeEix receptor by proteomics analysis. We identified two dynamin related proteins (DRPs), a coiled coil – nucleotide binding site leucine rich repeat (SlNRC4a) protein. In the second approach we used the split ubiquitin yeast two hybrid (Y2H) screen system to identified receptor-like protein kinase At5g24010-like (SlRLK-like) (Solyc01g094920.2.1) as an interactor of LeEIX2. We examined the role of SlNRC4a in plant immunity. Co-immunoprecipitation demonstrates that SlNRC4a is able to associate with different PRRs. Physiological assays with specific elicitors revealed that SlNRC4a generally alters PRR-mediated responses. SlNRC4a overexpression enhances defense responses while silencing SlNRC4 reduces plant immunity. We propose that SlNRC4a acts as a non-canonical positive regulator of immunity mediated by diverse PRRs. Thus, SlNRC4a could link both intracellular and extracellular immune perception. SlDRP2A localizes at the plasma membrane. Overexpression of SlDRP2A increases the sub-population of LeEIX2 inVHAa1 endosomes, and enhances LeEIX2- and FLS2-mediated defense. The effect of SlDRP2A on induction of plant immunity highlights the importance of endomembrane components and endocytosis in signal propagation during plant immune . The interaction of LeEIX2 with SlRLK-like was verified using co- immunoprecipitation and a bimolecular fluorescence complementation assay. The defence responses induced by EIX were markedly reduced when SlRLK-like was over-expressed, and mutation of slrlk-likeusing CRISPR/Cas9 increased EIX- induced ethylene production and SlACSgene expression in tomato. Co-expression of SlRLK-like with different RLPs and RLKs led to their degradation, apparently through an endoplasmic reticulum-associated degradation process. We provided new knowledge and expertise relevant to expression of specific be exploited to enhance immunity in crops enabling the development of novel environmentally friendly disease control strategies.

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