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Journal articles on the topic 'JNK'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

Zhao, Yi, Giada Spigolon, Christophe Bonny, Juraj Culman, Alessandro Vercelli, and Thomas Herdegen. "The JNK inhibitor D-JNKI-1 blocks apoptotic JNK signaling in brain mitochondria." Molecular and Cellular Neuroscience 49, no. 3 (2012): 300–310. http://dx.doi.org/10.1016/j.mcn.2011.12.005.

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2

Weitzman, Jonathan B. "JNK." Current Biology 10, no. 8 (2000): R290. http://dx.doi.org/10.1016/s0960-9822(00)00429-2.

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3

Chen, Wei-Kai, Yvonne Y. C. Yeap, and Marie A. Bogoyevitch. "The JNK1/JNK3 interactome – Contributions by the JNK3 unique N-terminus and JNK common docking site residues." Biochemical and Biophysical Research Communications 453, no. 3 (2014): 576–81. http://dx.doi.org/10.1016/j.bbrc.2014.09.122.

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4

Wong, W. "JNK Slowdown." Science Signaling 2, no. 78 (2009): ec230-ec230. http://dx.doi.org/10.1126/scisignal.278ec230.

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5

Dempsey, Laurie A. "Macrophage Jnk." Nature Immunology 14, no. 2 (2013): 118. http://dx.doi.org/10.1038/ni.2532.

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6

Okugawa, Shu, Yasuo Ota, Takatoshi Kitazawa, et al. "Janus kinase 2 is involved in lipopolysaccharide-induced activation of macrophages." American Journal of Physiology-Cell Physiology 285, no. 2 (2003): C399—C408. http://dx.doi.org/10.1152/ajpcell.00026.2003.

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The mechanisms by which lipopolysaccharide (LPS) is recognized, and how such recognition leads to innate immune responses, are poorly understood. Stimulation with LPS induces the activation of a variety of proteins, including mitogen-activated protein kinases (MAPKs) and NF-κB. Activation of protein tyrosine kinases (PTKs) is also necessary for a number of biological responses to LPS. We used a murine macrophage-like cell line, RAW264.7, to demonstrate that Janus kinase (JAK)2 is tyrosine phosphorylated immediately after LPS stimulation. Anti-Toll-like receptor (TLR)4 neutralization antibody i

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7

Lan, K. P., C. J. Wang, J. D. Hsu, K. M. Chen, S. C. Lai та H. H. Lee. "Induced eosinophilia and proliferation inAngiostrongylus cantonensis-infected mouse brain are associated with the induction of JAK/STAT1, IAP/NF-κB and MEKK1/JNK signals". Journal of Helminthology 78, № 4 (2004): 311–17. http://dx.doi.org/10.1079/joh2004256.

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AbstractEosinophilic meningitis or meningoencephalitis caused byAngiostrongylus cantonensisis endemic to the Pacific area of Asia, especially Taiwan, Thailand, and Japan. Although eosinophilia is an important clinical manifestation ofA. cantonensisinfection, the role of eosinophils in the progress of the infection remains to be elucidated. In this experiment, we show thatA. cantonensis-induced eosinophilia and inflammation might lead to the induction of IAP/NF-κB, JAK/STAT1 and MEKK1/JNK signals. The phosphorylation levels of JAK and JNK, STAT1, IAP, NF-κB and MEKK1 protein products were signi

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8

Nihalani, Deepak, Hetty N. Wong, and Lawrence B. Holzman. "Recruitment of JNK to JIP1 and JNK-dependent JIP1 Phosphorylation Regulates JNK Module Dynamics and Activation." Journal of Biological Chemistry 278, no. 31 (2003): 28694–702. http://dx.doi.org/10.1074/jbc.m304212200.

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9

Sabapathy, Kanaga, Konrad Hochedlinger, Shin Yuen Nam, Anton Bauer, Michael Karin, and Erwin F. Wagner. "Distinct Roles for JNK1 and JNK2 in Regulating JNK Activity and c-Jun-Dependent Cell Proliferation." Molecular Cell 15, no. 5 (2004): 713–25. http://dx.doi.org/10.1016/j.molcel.2004.08.028.

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10

Kinoshita, Juri, Yuriko Kinoshita, Tadashi Nomura, and Yoshihiro H. Inoue. "Macrophage-like Blood Cells Are Involved in Inter-Tissue Communication to Activate JAK/STAT Signaling, Inducing Antitumor Turandot Proteins in Drosophila Fat Body via the TNF-JNK Pathway." International Journal of Molecular Sciences 25, no. 23 (2024): 13110. https://doi.org/10.3390/ijms252313110.

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Abstract: Turandot (Tot) family proteins, which are induced via the JAK/STAT pathway after infection, also suppress lymph gland tumors in Drosophila mxcmbn1 mutant larvae. We investigated the potential role of hemocytes in Tot induction in tumor-bearing mutants via immunostaining and RNAi experiments. Normal hemocytes transplanted into mutant larvae were recruited to the tumor and fat body (FB), suggesting that these cells transmit tumor-related information. The transplanted hemocytes ectopically expressed Unpaired3 (Upd3), which is necessary for the activation of JAK/STAT. Eiger, a Drosophila

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11

Borhani, David W. "Covalent JNK inhibitors?" Proceedings of the National Academy of Sciences 106, no. 8 (2009): E18. http://dx.doi.org/10.1073/pnas.0812246106.

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12

Weitzman, Jonathan B. "JNK and obesity." Genome Biology 3 (2002): spotlight—20021121–01. http://dx.doi.org/10.1186/gb-spotlight-20021121-01.

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13

Barker, Ralph J., and Robert G. Gourdie. "JNK Bond Regulation." Circulation Research 91, no. 7 (2002): 556–58. http://dx.doi.org/10.1161/01.res.0000036861.37203.2f.

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14

Leavy, Olive. "The JNK diet." Nature Reviews Immunology 7, no. 12 (2007): 918–19. http://dx.doi.org/10.1038/nri2226.

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15

Pinal, Noelia, and Ginés Morata. "Short-term activation of the Jun N-terminal Kinase pathway in apoptosis-deficient cells of Drosophila induces tumorigenesis." Nat Comm 9, no. (1) (2018): 1541. https://doi.org/10.1038/s41467-018-04000-6.

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In Drosophila, the JNK pathway eliminates by apoptosis aberrant cells that appear in development. It also performs other functions associated with cell proliferation, but analysis of the latter is hindered by the pro-apoptotic activity. We report the response of apoptosis-deficient cells to transient activation of JNK and show that it causes persistent JNK function during the rest of the development. As a consequence, there is continuous activity of the downstream pathways JAK/STAT, Wg and Dpp, which results in tumour overgrowths. We also show that the oncogenic potential of the Ras-MAPK pathw

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Bae, Yoe-Sik, Ha Young Lee, Sun Young Lee, et al. "Sphingosylphosphorylcholine stimulates CCL2 production and ICAM expression from human umbilical vein endothelial cells (60.2)." Journal of Immunology 186, no. 1_Supplement (2011): 60.2. http://dx.doi.org/10.4049/jimmunol.186.supp.60.2.

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Abstract We investigated the functional role of sphingosylphosphorylcholine (SPC), a component of high density lipoprotein (HDL) particles, in human umbilical vein endothelial cells (HUVECs). SPC stimulation induced production of the CCL2 chemokine in a PTX-sensitive G-protein-dependent manner. SPC treatment caused the activation of NF-κB and AP-1, which are essential for SPC-induced CCL2 production, and also induced the activation of three MAPKs, ERK, p38 MAPK, and JNK. p38 MAPK or JNK by specific inhibitors caused a dramatic decrease in SPC-induced CCL2 production. The Jak/STAT3 pathway was

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17

Wang, Ziqian, Chenyue Zhan, Fang Zeng, and Shuizhu Wu. "A biopolymer-based and inflammation-responsive nanodrug for rheumatoid arthritis treatment via inhibiting JAK-STAT and JNK signalling pathways." Nanoscale 12, no. 45 (2020): 23013–27. http://dx.doi.org/10.1039/d0nr05551d.

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18

Chambers, Jeremy W., and Philip V. LoGrasso. "Mitochondrial c-Jun N-terminal Kinase (JNK) Signaling Initiates Physiological Changes Resulting in Amplification of Reactive Oxygen Species Generation." Journal of Biological Chemistry 286, no. 18 (2011): 16052–62. http://dx.doi.org/10.1074/jbc.m111.223602.

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The JNK signaling cascade is critical for cellular responses to a variety of environmental and cellular stimuli. Although gene expression aspects of JNK signal transduction are well studied, there are minimal data on the physiological impact of JNK signaling. To bridge this gap, we investigated how JNK impacted physiology in HeLa cells. We observed that inhibition of JNK activity and JNK silencing with siRNA reduced the level of reactive oxygen species (ROS) generated during anisomycin-induced stress in HeLa cells. Silencing p38 had no significant impact on ROS generation under anisomycin stre

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19

Eliopoulos, Aristides G., Elyse R. Waites, Sarah M. S. Blake, Clare Davies, Paul Murray, and Lawrence S. Young. "TRAF1 Is a Critical Regulator of JNK Signaling by the TRAF-Binding Domain of the Epstein-Barr Virus-Encoded Latent Infection Membrane Protein 1 but Not CD40." Journal of Virology 77, no. 2 (2003): 1316–28. http://dx.doi.org/10.1128/jvi.77.2.1316-1328.2003.

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ABSTRACT The oncogenic Epstein-Barr virus (EBV)-encoded latent infection membrane protein 1 (LMP1) mimics a constitutive active tumor necrosis factor (TNF) family receptor in its ability to recruit TNF receptor-associated factors (TRAFs) and TNF receptor-associated death domain protein (TRADD) in a ligand-independent manner. As a result, LMP1 constitutively engages signaling pathways, such as the JNK and p38 mitogen-activated protein kinases (MAPK), the transcription factor NF-κB, and the JAK/STAT cascade, and these activities may explain many of its pleiotropic effects on cell phenotype, grow

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20

Tan, X., Y. A. Alrashdan, H. Alkhouri, B. G. G. Oliver, C. L. Armour, and J. M. Hughes. "Airway smooth muscle CXCR3 ligand production: regulation by JAK-STAT1 and intracellular Ca2+." American Journal of Physiology-Lung Cellular and Molecular Physiology 304, no. 11 (2013): L790—L802. http://dx.doi.org/10.1152/ajplung.00356.2012.

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In asthma, airway smooth muscle (ASM) chemokine (C-X-C motif) receptor 3 (CXCR3) ligand production may attract mast cells or T lymphocytes to the ASM, where they can modulate ASM functions. In ASM cells (ASMCs) from people with or without asthma, we aimed to investigate JAK-STAT1, JNK, and Ca2+ involvement in chemokine (C-X-C motif) ligand (CXCL)10 and CXCL11 production stimulated by interferon-γ, IL-1β, and TNF-α combined (cytomix). Confluent, growth-arrested ASMC were treated with inhibitors for pan-JAK (pyridone-6), JAK2 (AG-490), JNK (SP-600125), or the sarco(endo)plasmic reticulum Ca2+ATP

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21

Biggi, Silvia, Lucia Buccarello, Alessandra Sclip, et al. "Evidence of Presynaptic Localization and Function of the c-Jun N-Terminal Kinase." Neural Plasticity 2017 (2017): 1–14. http://dx.doi.org/10.1155/2017/6468356.

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The c-Jun N-terminal kinase (JNK) is part of a stress signalling pathway strongly activated by NMDA-stimulation and involved in synaptic plasticity. Many studies have been focused on the post-synaptic mechanism of JNK action, and less is known about JNK presynaptic localization and its physiological role at this site. Here we examined whether JNK is present at the presynaptic site and its activity after presynaptic NMDA receptors stimulation. By using N-SIM Structured Super Resolution Microscopy as well as biochemical approaches, we demonstrated that presynaptic fractions contained significant

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22

UDOMSINPRASERT, Rungrutai, Marie A. BOGOYEVITCH, and Albert J. KETTERMAN. "Reciprocal regulation of glutathione S-transferase spliceforms and the Drosophila c-Jun N-terminal kinase pathway components." Biochemical Journal 383, no. 3 (2004): 483–90. http://dx.doi.org/10.1042/bj20040519.

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In mammalian systems, detoxification enzymes of the GST (glutathione S-transferase) family regulate JNK (c-Jun N-terminal kinase) signal transduction by interaction with JNK itself or other proteins upstream in the JNK pathway. In the present study, we have studied GSTs and their interaction with components of the JNK pathway from Diptera. We have evaluated the effects of four Delta class Anopheles dirus GSTs, GSTD1-1, GSTD2-2, GSTD3-3 and GSTD4-4, on the activity of full-length recombinant Drosophila HEP (mitogen-activated protein kinase kinase 7; where HEP stands for hemipterous) and the Dro

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23

Clarke, Penny, Suzanne M. Meintzer, Christian Widmann, Gary L. Johnson, and Kenneth L. Tyler. "Reovirus Infection Activates JNK and the JNK-Dependent Transcription Factor c-Jun." Journal of Virology 75, no. 23 (2001): 11275–83. http://dx.doi.org/10.1128/jvi.75.23.11275-11283.2001.

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ABSTRACT Viral infection often perturbs host cell signaling pathways including those involving mitogen-activated protein kinases (MAPKs). We now show that reovirus infection results in the selective activation of c-Jun N-terminal kinase (JNK). Reovirus-induced JNK activation is associated with an increase in the phosphorylation of the JNK-dependent transcription factor c-Jun. Reovirus serotype 3 prototype strains Abney (T3A) and Dearing (T3D) induce significantly more JNK activation and c-Jun phosphorylation than does the serotype 1 prototypic strain Lang (T1L). T3D and T3A also induce more ap

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24

Dhanasekaran, D. N., and E. P. Reddy. "JNK signaling in apoptosis." Oncogene 27, no. 48 (2008): 6245–51. http://dx.doi.org/10.1038/onc.2008.301.

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25

Leslie, M. "JNK-ing Cellular Poisons." Science of Aging Knowledge Environment 2003, no. 44 (2003): 149nw—149. http://dx.doi.org/10.1126/sageke.2003.44.nw149.

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26

Davenport, R. J. "Feeling Spunky With JNK." Science of Aging Knowledge Environment 2005, no. 13 (2005): nf24. http://dx.doi.org/10.1126/sageke.2005.13.nf24.

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27

Flight, Monica Hoyos. "Getting rid of JNK." Nature Reviews Drug Discovery 7, no. 12 (2008): 975. http://dx.doi.org/10.1038/nrd2771.

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28

Heasley, Lynn E., and Sun-Young Han. "JNK Regulation of Oncogenesis." Molecules and Cells 21, no. 2 (2006): 167–73. http://dx.doi.org/10.1016/s1016-8478(23)12876-7.

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29

Bruna, A. "Glucocorticoid receptor-JNK interaction mediates inhibition of the JNK pathway by glucocorticoids." EMBO Journal 22, no. 22 (2003): 6035–44. http://dx.doi.org/10.1093/emboj/cdg590.

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30

Stebbins, J. L., S. K. De, T. Machleidt, et al. "Identification of a new JNK inhibitor targeting the JNK-JIP interaction site." Proceedings of the National Academy of Sciences 105, no. 43 (2008): 16809–13. http://dx.doi.org/10.1073/pnas.0805677105.

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31

Thévenin, Anastasia F., Chati L. Zony, Brian J. Bahnson, and Roberta F. Colman. "GSTpi modulates JNK activity through a direct interaction with JNK substrate, ATF2." Protein Science 20, no. 5 (2011): 834–48. http://dx.doi.org/10.1002/pro.609.

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32

de los Reyes Corrales, Teresa, María Losada-Pérez, and Sergio Casas-Tintó. "JNK Pathway in CNS Pathologies." International Journal of Molecular Sciences 22, no. 8 (2021): 3883. http://dx.doi.org/10.3390/ijms22083883.

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The c-Jun N-terminal kinase (JNK) signalling pathway is a conserved response to a wide range of internal and external cellular stress signals. Beside the stress response, the JNK pathway is involved in a series of vital regulatory mechanisms during development and adulthood that are critical to maintain tissue homeostasis. These mechanisms include the regulation of apoptosis, growth, proliferation, differentiation, migration and invasion. The JNK pathway has a diverse functionality and cell-tissue specificity, and has emerged as a key player in regeneration, tumorigenesis and other pathologies

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Meeker, Rick, and Alda Fernandes. "Osmotic and glutamate receptor regulation of c-Jun NH2-terminal protein kinase in neuroendocrine cells." American Journal of Physiology-Endocrinology and Metabolism 279, no. 3 (2000): E475—E486. http://dx.doi.org/10.1152/ajpendo.2000.279.3.e475.

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Expression of a c-Jun NH2-terminal protein kinase (JNK), also known as stress-activated protein kinase (SAPK) in rodents, has been implicated in the ability of cells to respond to a variety of stressors. In nonmammalian cells, JNK participates in the regulation of cell volume in response to hyperosmotic stress. To explore the possibility that JNK may participate in the transduction of osmotic information in mammals, we evaluated the expression of JNK immunoreactivity in neuroendocrine cells of the supraoptic nucleus. Low basal expression of JNK-2 (SAPK-α) and JNK-3 (SAPK-β) was seen in vivo an

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Kadoya, Takayuki, Ashwani Khurana, Marianna Tcherpakov, et al. "JAMP, a Jun N-Terminal Kinase 1 (JNK1)-Associated Membrane Protein, Regulates Duration of JNK Activity." Molecular and Cellular Biology 25, no. 19 (2005): 8619–30. http://dx.doi.org/10.1128/mcb.25.19.8619-8630.2005.

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ABSTRACT We report the identification and characterization of JAMP (JNK1 [Jun N-terminal kinase 1]-associated membrane protein), a predicted seven-transmembrane protein that is localized primarily within the plasma membrane and associates with JNK1 through its C-terminal domain. JAMP association with JNK1 outcompetes JNK1 association with mitogen-activated protein kinase phosphatase 5, resulting in increased and prolonged JNK1 activity following stress. Elevated expression of JAMP following UV or tunicamycin treatment results in sustained JNK activity and a higher level of JNK-dependent apopto

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Meriin, Anatoli B., Julia A. Yaglom, Vladimir L. Gabai, Dick D. Mosser, Leonard Zon, and Michael Y. Sherman. "Protein-Damaging Stresses Activate c-Jun N-Terminal Kinase via Inhibition of Its Dephosphorylation: a Novel Pathway Controlled by HSP72." Molecular and Cellular Biology 19, no. 4 (1999): 2547–55. http://dx.doi.org/10.1128/mcb.19.4.2547.

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ABSTRACT Various stresses activate the c-Jun N-terminal kinase (JNK), which is involved in the regulation of many aspects of cellular physiology, including apoptosis. Here we demonstrate that in contrast to UV irradiation, heat shock causes little or no stimulation of the JNK-activating kinase SEK1, while knocking out the SEK1gene completely blocks heat-induced JNK activation. Therefore, we tested whether heat shock activates JNK via inhibition of JNK dephosphorylation. The rate of JNK dephosphorylation in unstimulated cells was high, and exposure to UV irradiation, osmotic shock, interleukin-

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Morel, Caroline, Claire L. Standen, Dae Young Jung, et al. "Requirement of JIP1-Mediated c-Jun N-Terminal Kinase Activation for Obesity-Induced Insulin Resistance." Molecular and Cellular Biology 30, no. 19 (2010): 4616–25. http://dx.doi.org/10.1128/mcb.00585-10.

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ABSTRACT The c-Jun NH2-terminal kinase (JNK) interacting protein 1 (JIP1) has been proposed to act as a scaffold protein that mediates JNK activation. However, recent studies have implicated JIP1 in multiple biochemical processes. Physiological roles of JIP1 that are related to the JNK scaffold function of JIP1 are therefore unclear. To test the role of JIP1 in JNK activation, we created mice with a germ line point mutation in the Jip1 gene (Thr103 replaced with Ala) that selectively blocks JIP1-mediated JNK activation. These mutant mice exhibit a severe defect in JNK activation caused by feed

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Stricker, Stephen A., and Niharika Ravichandran. "The potential roles of c-Jun N-terminal kinase (JNK) during the maturation and aging of oocytes produced by a marine protostome worm." Zygote 25, no. 6 (2017): 686–96. http://dx.doi.org/10.1017/s0967199417000533.

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SummaryPrevious investigations have indicated that c-Jun N-terminal kinase (JNK) regulates the maturation and aging of oocytes produced by deuterostome animals. In order to assess the roles of this kinase in a protostome, oocytes of the marine nemertean worm Cerebratulus were stimulated to mature and subsequently aged before being probed with phospho-specific antibodies against active forms of JNK and maturation-promoting factor (MPF). Based on blots of maturing oocytes, a 40-kD putative JNK is normally activated during germinal vesicle breakdown (GVBD), which begins at 30 min post-stimulation

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Lagadinou, Eleni D., Panos Ziros, Olga Tsopra, et al. "C-JUN-NH2-Terminal Kinase Promotes Apoptosis, Suppresses P-Glycoprotein Mediated Multidrug Resistance but Enhances MRP Mediated Efflux in AML Cells." Blood 108, no. 11 (2006): 4379. http://dx.doi.org/10.1182/blood.v108.11.4379.4379.

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Abstract JNK has been implicated in distinct cellular events, as proliferation, cellular transformation and apoptosis. JNK has also been recently reported to reverse MDR1 mediated drug resistance and increase sensitivity to chemotherapeutic agents in non-hematopoietic cancer cells. As acquired drug resistance represents a major obstacle in successful therapy of Acute Myeloid Leukemia (AML), the significance of JNK activation in relation to apoptosis induction and drug resistance in AML was sought. JNK is active in U937 leukemia cells and undergoes further activation upon treatment with therape

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Wei, Lin, Yinglin Liu, Hideaki Kaneto, and Barry L. Fanburg. "JNK regulates serotonin-mediated proliferation and migration of pulmonary artery smooth muscle cells." American Journal of Physiology-Lung Cellular and Molecular Physiology 298, no. 6 (2010): L863—L869. http://dx.doi.org/10.1152/ajplung.00281.2009.

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JNK is a member of the MAPK family and has essential roles in inflammation and cell differentiation and apoptosis. In recent years, there have been accumulating data indicating a novel role for JNK in cell growth and migration. In this report, we demonstrate that JNK activity is necessary for serotonin (5-HT)-induced proliferation and migration of bovine pulmonary artery smooth muscle cells (PASMCs). Stimulation with 5-HT was found to lead to activation of JNK with a maximal activation at 10 min. Inhibition of JNK with its specific inhibitor, SP-600125, or its dominant-negative form, DN-JNK, s

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Xu, Bing, Yaling Zhou, Karmin O, Patrick C. Choy, Grant N. Pierce, and Yaw L. Siow. "Regulation of stress-associated scaffold proteins JIP1 and JIP3 on the c-Jun NH2-terminal kinase in ischemia–reperfusion." Canadian Journal of Physiology and Pharmacology 88, no. 11 (2010): 1084–92. http://dx.doi.org/10.1139/y10-088.

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Ischemia–reperfusion (IR)-induced cell apoptosis involves the activation of c-Jun NH2-terminal kinase (JNK). The activation of JNK requires the presence of scaffold proteins called JNK-interacting proteins (JIP), which bind several members of a signaling cascade for proper signaling specificity. In this study, the expression of scaffold proteins JIP1 and JIP3 and their roles in the regulation of JNK activity were investigated in simulated IR in a cell model (H9c2). JIP1 protein expression was significantly decreased, whereas JIP3 protein expression was increased in IR H9c2 cells. Adenovirus-in

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Chu, Shijian, and Thomas J. Ferro. "Identification of a hydrogen peroxide-induced PP1-JNK1-Sp1 signaling pathway for gene regulation." American Journal of Physiology-Lung Cellular and Molecular Physiology 291, no. 5 (2006): L983—L992. http://dx.doi.org/10.1152/ajplung.00454.2005.

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Oxidative stress often results in changes in gene expression through the regulation of transcription factors. In this study, we examine how Sp1 phosphorylation is regulated by H2O2 in a human alveolar epithelial cell line (HAE). Treatment of HAE cells with H2O2 increases phosphorylation of Sp1 and activates JNK. To establish a relationship between JNK and Sp1, we show that JNK activator anisomycin increases Sp1 phosphorylation, and JNK inhibitors as well as dominant-negative JNK1 attenuate H2O2-induced Sp1 phosphorylation. Additionally, JNK1 directly phosphorylates Sp1 in vitro, reducing Sp1 b

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Zapata, Heidi J., Masako Nakatsugawa, and Jennifer F. Moffat. "Varicella-Zoster Virus Infection of Human Fibroblast Cells Activates the c-Jun N-Terminal Kinase Pathway." Journal of Virology 81, no. 2 (2006): 977–90. http://dx.doi.org/10.1128/jvi.01470-06.

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ABSTRACT The transcription factors ATF-2 and c-Jun are important for transactivation of varicella-zoster virus (VZV) genes. c-Jun is activated by the c-Jun N-terminal kinase (JNK), a member of the mitogen-activated protein kinase pathway that responds to stress and cytokines. To study the effects of VZV on this pathway, confluent human foreskin fibroblasts were infected with cell-associated VZV for 1 to 4 days. Immunoblots showed that phosphorylated JNK and c-Jun levels increased in VZV-infected cells, and kinase assays determined that phospho-JNK was active. Phospho-JNK was detected after 24

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Fujii, Nobuharu, Marni D. Boppart, Scott D. Dufresne, et al. "Overexpression or ablation of JNK in skeletal muscle has no effect on glycogen synthase activity." American Journal of Physiology-Cell Physiology 287, no. 1 (2004): C200—C208. http://dx.doi.org/10.1152/ajpcell.00415.2003.

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c-Jun NH2-terminal kinase (JNK) is highly expressed in skeletal muscle and is robustly activated in response to muscle contraction. Little is known about the biological functions of JNK signaling in terminally differentiated muscle cells, although this protein has been proposed to regulate insulin-stimulated glycogen synthase activity in mouse skeletal muscle. To determine whether JNK signaling regulates contraction-stimulated glycogen synthase activation, we applied an electroporation technique to induce JNK overexpression (O/E) in mouse skeletal muscle. Ten days after electroporation, in sit

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Wagner, Andreas C. C., Luca Mazzucchelli, Matthew Miller, Anna Marie Camoratto, and Burkhard Göke. "CEP-1347 inhibits caerulein-induced rat pancreatic JNK activation and ameliorates caerulein pancreatitis." American Journal of Physiology-Gastrointestinal and Liver Physiology 278, no. 1 (2000): G165—G172. http://dx.doi.org/10.1152/ajpgi.2000.278.1.g165.

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Pancreatic caerulein-induced activation of c-Jun NH2-terminal kinase (JNK) has been reported, and JNK has been proposed as a mediator during induction of hyperstimulated pancreatitis. CEP-1347 has recently been described as a specific JNK inhibitor. We tested whether CEP-1347 inhibits caerulein-induced pancreatic JNK activation in isolated acini and in vivo. CEP-1347 dose dependently inhibited acinar caerulein-induced JNK activation with nearly complete inhibition at 2 μM but had no effect on digestive enzyme release. For in vivo studies, rats were pretreated with CEP-1347 before caerulein hyp

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Sun, Kai-Hui, Hyoung-gon Lee, Mark A. Smith, and Kavita Shah. "Direct and Indirect Roles of Cyclin-dependent Kinase 5 as an Upstream Regulator in the c-Jun NH2-Terminal Kinase Cascade: Relevance to Neurotoxic Insults in Alzheimer's Disease." Molecular Biology of the Cell 20, no. 21 (2009): 4611–19. http://dx.doi.org/10.1091/mbc.e09-05-0433.

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Significant increase in JNK, c-Jun, and Cdk5 activities are reported in Alzheimer's disease (AD). Inhibition of c-Jun prevents neuronal cell death in in vivo AD models, highlighting it as a major JNK effector. Both JNK and Cdk5 promote neurodegeneration upon deregulation; however, Cdk5 has not been mechanistically linked to JNK or c-Jun. This study presents the first mechanism showing Cdk5 as a major regulator of the JNK cascade. Deregulated Cdk5 induces biphasic activation of JNK pathway. The first phase revealed c-Jun as a direct substrate of Cdk5, whose activation is independent of reactive

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Manieri, Elisa, Cintia Folgueira, María Elena Rodríguez, et al. "JNK-mediated disruption of bile acid homeostasis promotes intrahepatic cholangiocarcinoma." Proceedings of the National Academy of Sciences 117, no. 28 (2020): 16492–99. http://dx.doi.org/10.1073/pnas.2002672117.

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Metabolic stress causes activation of the cJun NH2-terminal kinase (JNK) signal transduction pathway. It is established that one consequence of JNK activation is the development of insulin resistance and hepatic steatosis through inhibition of the transcription factor PPARα. Indeed, JNK1/2 deficiency in hepatocytes protects against the development of steatosis, suggesting that JNK inhibition represents a possible treatment for this disease. However, the long-term consequences of JNK inhibition have not been evaluated. Here we demonstrate that hepatic JNK controls bile acid production. We found

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Gao, Yanqin, Armando P. Signore, Wei Yin, et al. "Neuroprotection against Focal Ischemic Brain Injury by Inhibition of c-Jun N-Terminal Kinase and Attenuation of the Mitochondrial Apoptosis-Signaling Pathway." Journal of Cerebral Blood Flow & Metabolism 25, no. 6 (2005): 694–712. http://dx.doi.org/10.1038/sj.jcbfm.9600062.

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c-Jun N-terminal kinase (JNK) is an important stress-responsive kinase that is activated by various forms of brain insults. In this study, we have examined the role of JNK activation in neuronal cell death in a murine model of focal ischemia and reperfusion; furthermore, we investigated the mechanism of JNK in apoptosis signaling, focusing on the mitochondrial-signaling pathway. We show here that JNK activity was induced in the brain 0.5 to 24 h after ischemia. Systemic administration of SP600125, a small molecule JNK-specific inhibitor, diminished JNK activity after ischemia and dose-dependen

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Saunders, Philip O., Kenneth F. Bradstock, and Linda J. Bendall. "The JNK Pathway Is a Significant Determinant of Sensitivity to DNA Damaging Agents in Pre-B ALL." Blood 114, no. 22 (2009): 3786. http://dx.doi.org/10.1182/blood.v114.22.3786.3786.

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Abstract Abstract 3786 Poster Board III-722 The JNK pathway is reported to facilitate AP1 binding and promote apoptosis depending on cell type and environmental conditions. We have previously reported RAD001 (16μM) induces JNK pathway activation in pre-B ALL cells. We sought to evaluate the impact of changes in JNK pathway activation on pre-B ALL viability in vitro. Using JNK inhibitor SP600125 titrated to inhibit c-Jun activation, we determined that cell death in pre-B ALL cells treated with RAD001 (16μM) alone was not JNK dependent. In contrast, combining RAD001 (16μM) with DNA damaging agen

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Sengupta Ghosh, Arundhati, Bei Wang, Christine D. Pozniak, Mark Chen, Ryan J. Watts, and Joseph W. Lewcock. "DLK induces developmental neuronal degeneration via selective regulation of proapoptotic JNK activity." Journal of Cell Biology 194, no. 5 (2011): 751–64. http://dx.doi.org/10.1083/jcb.201103153.

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The c-Jun N-terminal kinase (JNK) signaling pathway is essential for neuronal degeneration in multiple contexts but also regulates neuronal homeostasis. It remains unclear how neurons are able to dissociate proapoptotic JNK signaling from physiological JNK activity. In this paper, we show that the mixed lineage kinase dual leucine zipper kinase (DLK) selectively regulates the JNK-based stress response pathway to mediate axon degeneration and neuronal apoptosis without influencing other aspects of JNK signaling. This specificity is dependent on interaction of DLK with the scaffolding protein JI

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Weiss, Linda, Alan J. Whitmarsh, Derek D. Yang, Mercedes Rincón, Roger J. Davis, and Richard A. Flavell. "Regulation of c-Jun NH2-terminal Kinase ( Jnk) Gene Expression during T Cell Activation." Journal of Experimental Medicine 191, no. 1 (2000): 139–46. http://dx.doi.org/10.1084/jem.191.1.139.

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The c-Jun NH2-terminal kinases (JNKs) are a group of mitogen-activated protein (MAP) kinases that participate in signal transduction events mediating specific cellular functions. Activation of JNK is regulated by phosphorylation in response to cellular stress and inflammatory cytokines. Here, we demonstrate that JNK is regulated by a second, novel mechanism. Induction of Jnk gene expression is required in specific tissues before activation of this signaling pathway. The in vivo and in vitro ligation of the T cell receptor (TCR) leads to induction of JNK gene and protein expression. TCR signals

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