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Journal articles on the topic 'C-Jun N-terminal kinase (JNK)'

Author: Grafiati

Published: 4 June 2021

Last updated: 6 September 2023

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1

Liu, Jing, Yuzuru Minemoto, and Anning Lin. "c-Jun N-Terminal Protein Kinase 1 (JNK1), but Not JNK2, Is Essential for Tumor Necrosis Factor Alpha-Induced c-Jun Kinase Activation and Apoptosis." Molecular and Cellular Biology 24, no. 24 (December 15, 2004): 10844–56. http://dx.doi.org/10.1128/mcb.24.24.10844-10856.2004.

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ABSTRACT Two ubiquitously expressed isoforms of c-Jun N-terminal protein kinase (JNK), JNK1 and JNK2, have shared functions and different functions. However, the molecular mechanism is unknown. Here we report that JNK1, but not JNK2, is essential for tumor necrosis factor alpha (TNF-α)-induced c-Jun kinase activation, c-Jun expression, and apoptosis. Using mouse fibroblasts deficient in either Jnk1 or Jnk2, we found that JNK1 was activated by TNF-α, whereas JNK2 activation was negligible. In addition, JNK2 interfered with JNK1 activation via its “futile” phosphorylation by upstream kinases. Co

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Ngoei, Kevin R. W., Bruno Catimel, Nicole Church, Daisy S. Lio, Con Dogovski, Matthew A. Perugini, Paul M. Watt, Heung-Chin Cheng, Dominic C. H. Ng, and Marie A. Bogoyevitch. "Characterization of a novel JNK (c-Jun N-terminal kinase) inhibitory peptide." Biochemical Journal 434, no. 3 (February 24, 2011): 399–413. http://dx.doi.org/10.1042/bj20101244.

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An improved understanding of the roles of protein kinases in intracellular signalling and disease progression has driven significant advances in protein kinase inhibitor discovery. Peptide inhibitors that target the kinase protein substrate-binding site have continued to attract attention. In the present paper, we describe a novel JNK (c-Jun N-terminal kinase) inhibitory peptide PYC71N, which inhibits JNK activity in vitro towards a range of recombinant protein substrates including the transcription factors c-Jun, ATF2 (activating trancription factor 2) and Elk1, and the microtubule regulatory

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3

Messoussi, A., G. Chevé, K. Bougrin, and A. Yasri. "Insight into the selective inhibition of JNK family members through structure-based drug design." MedChemComm 7, no. 4 (2016): 686–92. http://dx.doi.org/10.1039/c5md00562k.

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The c-Jun N-terminal kinase (JNK) family, which comprises JNK1, JNK2 and JNK3, belongs to the mitogen-activated protein kinase (MAPK) superfamily, whose members regulate myriad biological processes, including those implicated in tumorigenesis and neurodegenerative disorders.

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4

Schepetkin, Igor A., Oleksander S. Karpenko, Anastasia R. Kovrizhina, Liliya N. Kirpotina, Andrei I. Khlebnikov, Stepan I. Chekal, Alevtyna V. Radudik, Maryna O. Shybinska, and Mark T. Quinn. "Novel Tryptanthrin Derivatives with Selectivity as c–Jun N–Terminal Kinase (JNK) 3 Inhibitors." Molecules 28, no. 12 (June 16, 2023): 4806. http://dx.doi.org/10.3390/molecules28124806.

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The c-Jun N-terminal kinase (JNK) family includes three proteins (JNK1-3) that regulate many physiological processes, including cell proliferation and differentiation, cell survival, and inflammation. Because of emerging data suggesting that JNK3 may play an important role in neurodegenerative diseases, such as Alzheimer’s disease (AD) and Parkinson’s disease, as well as cancer pathogenesis, we sought to identify JNK inhibitors with increased selectivity for JNK3. A panel of 26 novel tryptanthrin-6-oxime analogs was synthesized and evaluated for JNK1-3 binding (Kd) and inhibition of cellular i

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5

Sedmíková, M., J. Petr, A. Dörflerová, J. Nevoral, B. Novotná, T. Krejčová, E. Chmelíková, and L. Tůmová. "Inhibition of c-Jun N-terminal kinase (JNK) suppresses porcine oocyte ageing in vitro." Czech Journal of Animal Science 58, No. 12 (November 25, 2013): 535–45. http://dx.doi.org/10.17221/7088-cjas.

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Oocyte ageing is a complex of processes that occur when matured in vitro oocytes are, after reaching the metaphase II stage, exposed to further in vitro culture. Aged oocytes remaining at the metaphase II stage undergo spontaneous parthenogenetic activation, or cellular death, through apoptosis (fragmentation) or lysis. The key factor in apoptotic pathway regulation is c-Jun-N-terminal kinase (JNK), stress kinase from the mitogene-activated protein kinase (MAPK) family. To investigate the effect of JNK inhibition on porcine oocytes ageing, cleavage rate, and embryonic development after parthen

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6

Unger, Elizabeth K., Merisa L. Piper, Louise E. Olofsson, and Allison W. Xu. "Functional Role of c-Jun-N-Terminal Kinase in Feeding Regulation." Endocrinology 151, no. 2 (February 1, 2010): 671–82. http://dx.doi.org/10.1210/en.2009-0711.

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c-Jun-N-terminal kinase (JNK) is a signaling molecule that is activated by proinflammatory signals, endoplasmic reticulum (ER) stress, and other environmental stressors. Although JNK has diverse effects on immunological responses and insulin resistance in peripheral tissues, a functional role for JNK in feeding regulation has not been established. In this study, we show that central inhibition of JNK activity potentiates the stimulatory effects of glucocorticoids on food intake and that this effect is abolished in mice whose agouti-related peptide (AgRP) neurons are degenerated. JNK1-deficient

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7

Choi, Hong Seok, Ann M. Bode, Jung-Hyun Shim, Sung-Young Lee, and Zigang Dong. "c-Jun N-Terminal Kinase 1 Phosphorylates Myt1 To Prevent UVA-Induced Skin Cancer." Molecular and Cellular Biology 29, no. 8 (February 9, 2009): 2168–80. http://dx.doi.org/10.1128/mcb.01508-08.

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ABSTRACT The c-Jun N-terminal kinase (JNK) signaling pathway is known to mediate both survival and apoptosis of tumor cells. Although JNK1 and JNK2 have been shown to differentially regulate the development of skin cancer, the underlying mechanistic basis remains unclear. Here, we demonstrate that JNK1, but not JNK2, interacts with and phosphorylates Myt1 ex vivo and in vitro. UVA induces substantial apoptosis in JNK wild-type (JNK +/+) or JNK2-deficient (JNK2 −/−) mouse embryonic fibroblasts but has no effect on JNK1-deficient (JNK1 −/−) cells. In addition, UVA-induced caspase-3 cleavage and

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8

LoGrasso, Philip, and Theodore Kamenecka. "Inhibitors of c-jun-N-Terminal Kinase (JNK)." Mini-Reviews in Medicinal Chemistry 8, no. 8 (July 1, 2008): 755–66. http://dx.doi.org/10.2174/138955708784912120.

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9

Ma, Hongpeng. "Relationship Between c-Jun N-terminal Kinase and Depression." E3S Web of Conferences 185 (2020): 03029. http://dx.doi.org/10.1051/e3sconf/202018503029.

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Depression is one of the most common emotional disorders. The cause of depression is still not clear. C-Jun N-terminal kinase (JNK) is one number of mitogen activated protein kinase (MAPK) family, which is closely related to the occurrence of many diseases. At present, it is believed that JNK plays an important role in the parthenogenesis of depression, but the specific mechanism is not clear. This review will focus on the possible mechanism of JNK protein and JNK signaling pathway affecting the parthenogenesis of depression.

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10

Ye, Zhiqiang, Yuxian Chen, Rongkai Zhang, Haitao Dai, Chun Zeng, Hua Zeng, Hui Feng, Gengheng Du, Hang Fang, and Daozhang Cai. "c-Jun N-terminal kinase – c-Jun pathway transactivates Bim to promote osteoarthritis." Canadian Journal of Physiology and Pharmacology 92, no. 2 (February 2014): 132–39. http://dx.doi.org/10.1139/cjpp-2013-0228.

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Osteoarthritis (OA) is a chronic degenerative joint disorder. Previous studies have shown abnormally increased apoptosis of chondrocytes in patients and animal models of OA. TNF-α and nitric oxide have been reported to induce chondrocyte ageing; however, the mechanism of chondrocyte apoptosis induced by IL-1β has remained unclear. The aim of this study is to identify the role of the c-Jun N-terminal kinase (JNK) – c-Jun pathway in regulating induction of Bim, and its implication in chondrocyte apoptosis. This study showed that Bim is upregulated in chondrocytes obtained from the articular cart

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11

See, Raymond H., and Yang Shi. "Adenovirus E1B 19,000-Molecular-Weight Protein Activates c-Jun N-Terminal Kinase and c-Jun-Mediated Transcription." Molecular and Cellular Biology 18, no. 7 (July 1, 1998): 4012–22. http://dx.doi.org/10.1128/mcb.18.7.4012.

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ABSTRACT Adenovirus E1B proteins (19,000-molecular-weight [19K] and 55K proteins) inhibit apoptosis and cooperate with adenovirus E1A to induce full oncogenic transformation of primary cells. The E1B 19K protein has previously been shown to be capable of activating transcription; however, the underlying mechanisms are unclear. Here, we show that adenovirus infection activates the c-Jun N-terminal kinase (JNK) and that the E1B gene products are necessary for adenovirus to activate JNK. In transfection assays, we show that the E1B 19K protein is sufficient to activate JNK and can strongly induce

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12

Smith, Abigail O., Julie A. Jonassen, Kenley M. Preval, Roger J. Davis, and Gregory J. Pazour. "c-Jun N-terminal kinase (JNK) signaling contributes to cystic burden in polycystic kidney disease." PLOS Genetics 17, no. 12 (December 28, 2021): e1009711. http://dx.doi.org/10.1371/journal.pgen.1009711.

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Polycystic kidney disease is an inherited degenerative disease in which the uriniferous tubules are replaced by expanding fluid-filled cysts that ultimately destroy organ function. Autosomal dominant polycystic kidney disease (ADPKD) is the most common form, afflicting approximately 1 in 1,000 people. It primarily is caused by mutations in the transmembrane proteins polycystin-1 (Pkd1) and polycystin-2 (Pkd2). The most proximal effects of Pkd mutations leading to cyst formation are not known, but pro-proliferative signaling must be involved for the tubule epithelial cells to increase in number

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13

Siddiqui, M. Arshad, and Panduranga A. Reddy. "Small Molecule JNK (c-Jun N-Terminal Kinase) Inhibitors." Journal of Medicinal Chemistry 53, no. 8 (April 22, 2010): 3005–12. http://dx.doi.org/10.1021/jm9003279.

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14

Sluss, H. K., T. Barrett, B. Dérijard, and R. J. Davis. "Signal transduction by tumor necrosis factor mediated by JNK protein kinases." Molecular and Cellular Biology 14, no. 12 (December 1994): 8376–84. http://dx.doi.org/10.1128/mcb.14.12.8376-8384.1994.

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JNK protein kinases are distantly related to mitogen-activated protein kinases (ERKs) and are activated by dual phosphorylation on Tyr and Thr. The JNK protein kinase group includes the 46-kDa isoform JNK1. Here we describe the molecular cloning of a second member of the JNK group, the 55-kDa protein kinase JNK2. The activities of both JNK isoforms are markedly increased by exposure of cells to UV radiation. Furthermore, JNK protein kinase activation is observed in cells treated with tumor necrosis factor. Although both JNK isoforms phosphorylate the NH2-terminal activation domain of the trans

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15

Sluss, H. K., T. Barrett, B. Dérijard, and R. J. Davis. "Signal transduction by tumor necrosis factor mediated by JNK protein kinases." Molecular and Cellular Biology 14, no. 12 (December 1994): 8376–84. http://dx.doi.org/10.1128/mcb.14.12.8376.

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JNK protein kinases are distantly related to mitogen-activated protein kinases (ERKs) and are activated by dual phosphorylation on Tyr and Thr. The JNK protein kinase group includes the 46-kDa isoform JNK1. Here we describe the molecular cloning of a second member of the JNK group, the 55-kDa protein kinase JNK2. The activities of both JNK isoforms are markedly increased by exposure of cells to UV radiation. Furthermore, JNK protein kinase activation is observed in cells treated with tumor necrosis factor. Although both JNK isoforms phosphorylate the NH2-terminal activation domain of the trans

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16

Zohn, I. E., H. Yu, X. Li, A. D. Cox, and H. S. Earp. "Angiotensin II stimulates calcium-dependent activation of c-Jun N-terminal kinase." Molecular and Cellular Biology 15, no. 11 (November 1995): 6160–68. http://dx.doi.org/10.1128/mcb.15.11.6160.

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In GN4 rat liver epithelial cells, angiotensin II (Ang II) and other agonists which activate phospholipase C stimulate tyrosine kinase activity in a calcium-dependent, protein kinase C (PKC)-independent manner. Since Ang II also produces a proliferative response in these cells, we investigated downstream signaling elements traditionally linked to growth control by tyrosine kinases. First, Ang II, like epidermal growth factor (EGF), stimulated AP-1 binding activity in a PKC-independent manner. Because increases in AP-1 can reflect induction of c-Jun and c-Fos, we examined the activity of the mi

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17

Yeap, Yvonne Y. C., Ivan H. W. Ng, Bahareh Badrian, Tuong-Vi Nguyen, Yan Y. Yip, Amardeep S. Dhillon, Steven E. Mutsaers, John Silke, Marie A. Bogoyevitch, and Dominic C. H. Ng. "c-Jun N-terminal kinase/c-Jun inhibits fibroblast proliferation by negatively regulating the levels of stathmin/oncoprotein 18." Biochemical Journal 430, no. 2 (August 13, 2010): 345–54. http://dx.doi.org/10.1042/bj20100425.

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The JNKs (c-Jun N-terminal kinases) are stress-activated serine/threonine kinases that can regulate both cell death and cell proliferation. We have developed a cell system to control JNK re-expression at physiological levels in JNK1/2-null MEFs (murine embryonic fibroblasts). JNK re-expression restored basal and stress-activated phosphorylation of the c-Jun transcription factor and attenuated cellular proliferation with increased cells in G1/S-phase of the cell cycle. To explore JNK actions to regulate cell proliferation, we evaluated a role for the cytosolic protein, STMN (stathmin)/Op18 (onc

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18

Guan, Z., T. Tetsuka, L. D. Baier, and A. R. Morrison. "Interleukin-1 beta activates c-jun NH2-terminal kinase subgroup of mitogen-activated protein kinases in mesangial cells." American Journal of Physiology-Renal Physiology 270, no. 4 (April 1, 1996): F634—F641. http://dx.doi.org/10.1152/ajprenal.1996.270.4.f634.

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We investigated whether JNK is activated by interleukin-1 beta (IL-1 beta) in mesangial cells. We performed in-gel kinase assays with His-c-jun-(1-79), which contains the amino-terminal activation domain of c-jun and a mutant His-c-jun in which Ser-63 and Ser-73 of His-c-jun were mutated to Ala as the substrates. JNK1 (p45) and JNK2 (p54) isoforms phosphorylated His-c-jun in mesangial cells. IL-1 beta produced a time- and concentration-dependent increase in JNK activity. IL-1 beta did not phosphorylated the mutant, His-c-jun. The IL-1 beta-activated JNK activity was independent of serum and su

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19

Hirasawa, Noriyasu, Yukako Sato, Yuhko Fujita, Suetsugu Mue, and Kazuo Ohuchi. "Inhibition by Dexamethasone of Antigen-Induced c-Jun N-Terminal Kinase Activation in Rat Basophilic Leukemia Cells." Journal of Immunology 161, no. 9 (November 1, 1998): 4939–43. http://dx.doi.org/10.4049/jimmunol.161.9.4939.

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Abstract Antigen stimulation of IgE-sensitized rat basophilic leukemia RBL-2H3 cells induced activation of c-Jun N-terminal kinase (JNK) within a few minutes with maximum activity attained 40 min later. The increase in JNK activity was accompanied with an increase in phosphorylation of c-Jun in the cells. The Ag-induced JNK activation was inhibited by the phosphatidylinositol 3-kinase inhibitors wortmannin (10–100 nM) and LY 294002 (100 μM) but not by the protein kinase C inhibitors calphostin C (1 and 3 μM) and Ro 31-8425 (1 and 3 μM). Pretreatment with dexamethasone (10 and 100 nM) for 18 h

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20

Jones, Emma V., Mark J. Dickman, and Alan J. Whitmarsh. "Regulation of p73-mediated apoptosis by c-Jun N-terminal kinase." Biochemical Journal 405, no. 3 (July 13, 2007): 617–23. http://dx.doi.org/10.1042/bj20061778.

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The JNK (c-Jun N-terminal kinase)/mitogen-activated protein kinase signalling pathway is a major mediator of stress responses in cells, including the response to DNA damage. DNA damage also causes the stabilization and activation of p73, a member of the p53 family of transcription factors. p73, like p53, can mediate apoptosis by up-regulating the expression of pro-apoptotic genes, including Bax (Bcl2-associated X protein) and PUMA (p53 up-regulated modulator of apoptosis). Changes in p73 expression have been linked to tumour progression, particularly in neuroblastomas, whereas in tumours that

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Moon, Il-Soo. "Expression of c-Jun N-Terminal Kinase (JNK)-Interacting Protein (JIP) in Cultured Rat Hippocampal Neurons." Journal of Life Science 17, no. 12 (December 30, 2007): 1627–33. http://dx.doi.org/10.5352/jls.2007.17.12.1627.

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22

Tai, Tina Y., Lindsay N. Warner, Terrance D. Jones, Sangwook Jung, David W. Skyrud, and Nicholas P. Poolos. "Antiepileptic action of c-Jun N-terminal kinase (JNK) inhibition." Epilepsy & Behavior 46 (May 2015): 55. http://dx.doi.org/10.1016/j.yebeh.2015.02.054.

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23

Schwertfeger, Kathryn L., Seija Hunter, Lynn E. Heasley, Valerie Levresse, Ronald P. Leon, James DeGregori, and Steven M. Anderson. "Prolactin Stimulates Activation of c-jun N-Terminal Kinase (JNK)." Molecular Endocrinology 14, no. 10 (October 1, 2000): 1592–602. http://dx.doi.org/10.1210/mend.14.10.0536.

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24

Li, Gang. "Recent Advances in c-Jun N-Terminal Kinase (JNK) Inhibitors." Current Medicinal Chemistry 28, no. 3 (2021): 607–27. http://dx.doi.org/10.2174/1875533xmta0tmzuv4.

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25

Min, Robert W. M., Filbert W. M. Aung, Bryant Liu, Aliza Arya, and Sanda Win. "Mechanism and Therapeutic Targets of c-Jun-N-Terminal Kinases Activation in Nonalcoholic Fatty Liver Disease." Biomedicines 10, no. 8 (August 20, 2022): 2035. http://dx.doi.org/10.3390/biomedicines10082035.

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Non-alcoholic fatty liver (NAFL) is the most common chronic liver disease. Activation of mitogen-activated kinases (MAPK) cascade, which leads to c-Jun N-terminal kinase (JNK) activation occurs in the liver in response to the nutritional and metabolic stress. The aberrant activation of MAPKs, especially c-Jun-N-terminal kinases (JNKs), leads to unwanted genetic and epi-genetic modifications in addition to the metabolic stress adaptation in hepatocytes. A mechanism of sustained P-JNK activation was identified in acute and chronic liver diseases, suggesting an important role of aberrant JNK acti

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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 (November 1, 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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KATZ, Sigal, and Ami ARONHEIM. "Differential targeting of the stress mitogen-activated protein kinases to the c-Jun dimerization protein 2." Biochemical Journal 368, no. 3 (December 15, 2002): 939–45. http://dx.doi.org/10.1042/bj20021127.

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The mitogen-activated kinases are structurally related proline-directed serine/threonine kinases that phosphorylate similar phosphoacceptor sites and yet, in vivo, they exhibit stringent substrate specificity. Specific targeting domains (kinase docking domains) facilitate kinase—substrate interaction and play a major role in substrate specificity determination. The c-Jun N-terminal kinase (JNK) consensus docking domain comprises of a KXXK/RXXXXLXL motif located in the Δ-domain of the c-Jun N-terminal to the phosphoacceptor site. The c-Jun dimerization protein 2 is phosphorylated by JNK on Thr-

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Ventura, Juan-Jose, Norman J. Kennedy, Jennifer A. Lamb, Richard A. Flavell, and Roger J. Davis. "c-Jun NH2-Terminal Kinase Is Essential for the Regulation of AP-1 by Tumor Necrosis Factor." Molecular and Cellular Biology 23, no. 8 (April 15, 2003): 2871–82. http://dx.doi.org/10.1128/mcb.23.8.2871-2882.2003.

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ABSTRACT The c-Jun NH2-terminal kinase (JNK) is activated by the cytokine tumor necrosis factor (TNF). This pathway is implicated in the regulation of AP-1-dependent gene expression by TNF. To examine the role of the JNK signaling pathway, we compared the effects of TNF on wild-type and Jnk1 −/− Jnk2 −/− murine embryo fibroblasts. We show that JNK is required for the normal regulation of AP-1 by TNF. The JNK-deficient cells exhibited decreased expression of c-Jun, JunD, c-Fos, Fra1, and Fra2; decreased phosphorylation of c-Jun and JunD; and decreased AP-1 DNA binding activity. The JNK-deficien

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Pirianov, Grisha, David A. MacIntyre, Yun Lee, Simon N. Waddington, Vasso Terzidou, Huseyin Mehmet, and Phillip R. Bennett. "Specific inhibition of c-Jun N-terminal kinase delays preterm labour and reduces mortality." REPRODUCTION 150, no. 4 (October 2015): 269–77. http://dx.doi.org/10.1530/rep-15-0258.

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Preterm labour (PTL) is commonly associated with infection and/or inflammation. Lipopolysaccharide (LPS) from different bacteria can be used to independently or mutually activate Jun N-terminal kinase (JNK)/AP1- or NF-κB-driven inflammatory pathways that lead to PTL. Previous studies using Salmonella abortus LPS, which activates both JNK/AP-1 and NF-κB, showed that selective inhibition of NF-κB delays labour and improves pup outcome. Where labour is induced using Escherichia coli LPS (O111), which upregulates JNK/AP-1 but not NF-κB, inhibition of JNK/AP-1 activation also delays labour. In this

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WILTSHIRE, Carolyn, Masato MATSUSHITA, Satoshi TSUKADA, David A. F. GILLESPIE, and Gerhard H. W. MAY. "A new c-Jun N-terminal kinase (JNK)-interacting protein, Sab (SH3BP5), associates with mitochondria." Biochemical Journal 367, no. 3 (November 1, 2002): 577–85. http://dx.doi.org/10.1042/bj20020553.

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We have identified a novel c-Jun N-terminal kinase (JNK)-interacting protein, Sab, by yeast two-hybrid screening. Sab binds to and serves as a substrate for JNK in vitro, and was previously found to interact with the Src homology 3 (SH3) domain of Bruton's tyrosine kinase (Btk). Inspection of the sequence of Sab reveals the presence of two putative mitogen-activated protein kinase interaction motifs (KIMs) similar to that found in the JNK docking domain of the c-Jun transcription factor, and four potential serine—proline JNK phosphorylation sites in the C-terminal half of the molecule. Using d

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Biggi, Silvia, Lucia Buccarello, Alessandra Sclip, Pellegrino Lippiello, Noemi Tonna, Cristiano Rumio, Daniele Di Marino, Maria Concetta Miniaci, and Tiziana Borsello. "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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Zhong, Shuping, Jody Fromm, and Deborah L. Johnson. "TBP Is Differentially Regulated by c-Jun N-Terminal Kinase 1 (JNK1) and JNK2 through Elk-1, Controlling c-Jun Expression and Cell Proliferation." Molecular and Cellular Biology 27, no. 1 (January 1, 2007): 54–64. http://dx.doi.org/10.1128/mcb.01365-06.

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ABSTRACT Emerging evidence supports the idea that the c-Jun N-terminal kinases (JNKs) possess overlapping but distinct functions. The potential roles of the ubiquitously expressed JNK1 and JNK2 in regulating expression of the central transcription initiation factor, TATA-binding protein (TBP), were examined. Relative to wild-type fibroblasts, TBP was decreased in Jnk1 −/− cells and increased in Jnk2 −/− cells. Similarly, reduction of JNK1 in human hepatoma cells decreased TBP expression, whereas reduction of JNK2 enhanced it. JNK-mediated regulation of TBP expression occurs at the transcriptio

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Anfinogenova, Nina D., Mark T. Quinn, Igor A. Schepetkin, and Dmitriy N. Atochin. "Alarmins and c-Jun N-Terminal Kinase (JNK) Signaling in Neuroinflammation." Cells 9, no. 11 (October 24, 2020): 2350. http://dx.doi.org/10.3390/cells9112350.

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Neuroinflammation is involved in the progression or secondary injury of multiple brain conditions, including stroke and neurodegenerative diseases. Alarmins, also known as damage-associated molecular patterns, are released in the presence of neuroinflammation and in the acute phase of ischemia. Defensins, cathelicidin, high-mobility group box protein 1, S100 proteins, heat shock proteins, nucleic acids, histones, nucleosomes, and monosodium urate microcrystals are thought to be alarmins. They are released from damaged or dying cells and activate the innate immune system by interacting with pat

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Fritz, G., and B. Kaina. "Activation of c-Jun N-Terminal Kinase 1 by UV Irradiation Is Inhibited by Wortmannin without Affecting c-jun Expression." Molecular and Cellular Biology 19, no. 3 (March 1, 1999): 1768–74. http://dx.doi.org/10.1128/mcb.19.3.1768.

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ABSTRACT Activation of c-Jun N-terminal kinases (JNKs)/stress-activated protein kinases is an early response of cells upon exposure to DNA-damaging agents. JNK-mediated phosphorylation of c-Jun is currently understood to stimulate the transactivating potency of AP-1 (e.g., c-Jun/c-Fos; c-Jun/ATF-2), thereby increasing the expression of AP-1 target genes. Here we show that stimulation of JNK1 activity is not a general early response of cells exposed to genotoxic agents. Treatment of NIH 3T3 cells with UV light (UV-C) as well as with methyl methanesulfonate (MMS) caused activation of JNK1 and an

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Busquets, Oriol, Miren Ettcheto, Amanda Cano, Patricia R. Manzine, Elena Sánchez-Lopez, Triana Espinosa-Jiménez, Ester Verdaguer, et al. "Role of c-Jun N-Terminal Kinases (JNKs) in Epilepsy and Metabolic Cognitive Impairment." International Journal of Molecular Sciences 21, no. 1 (December 30, 2019): 255. http://dx.doi.org/10.3390/ijms21010255.

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Previous studies have reported that the regulatory function of the different c-Jun N-terminal kinases isoforms (JNK1, JNK2, and JNK3) play an essential role in neurological disorders, such as epilepsy and metabolic-cognitive alterations. Accordingly, JNKs have emerged as suitable therapeutic strategies. In fact, it has been demonstrated that some unspecific JNK inhibitors exert antidiabetic and neuroprotective effects, albeit they usually show high toxicity or lack therapeutic value. In this sense, natural specific JNK inhibitors, such as Licochalcone A, are promising candidates. Nonetheless,

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Lai, Benjamin, Chien-Hsiang Wu, and Jenn-Haung Lai. "Activation of c-Jun N-Terminal Kinase, a Potential Therapeutic Target in Autoimmune Arthritis." Cells 9, no. 11 (November 12, 2020): 2466. http://dx.doi.org/10.3390/cells9112466.

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The c-Jun-N-terminal kinase (JNK) is a critical mediator involved in various physiological processes, such as immune responses, and the pathogenesis of various diseases, including autoimmune disorders. JNK is one of the crucial downstream signaling molecules of various immune triggers, mainly proinflammatory cytokines, in autoimmune arthritic conditions, mainly including rheumatoid arthritis, ankylosing spondylitis, and psoriatic arthritis. The activation of JNK is regulated in a complex manner by upstream kinases and phosphatases. Noticeably, different subtypes of JNKs behave differentially i

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Hepp Rehfeldt, Stephanie Cristine, Fernanda Majolo, Márcia Inês Goettert, and Stefan Laufer. "c-Jun N-Terminal Kinase Inhibitors as Potential Leads for New Therapeutics for Alzheimer’s Diseases." International Journal of Molecular Sciences 21, no. 24 (December 18, 2020): 9677. http://dx.doi.org/10.3390/ijms21249677.

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Alzheimer’s Disease (AD) is becoming more prevalent as the population lives longer. For individuals over 60 years of age, the prevalence of AD is estimated at 40.19% across the world. Regarding the cognitive decline caused by the disease, mitogen-activated protein kinases (MAPK) pathways such as the c-Jun N-terminal kinase (JNK) pathway are involved in the progressive loss of neurons and synapses, brain atrophy, and augmentation of the brain ventricles, being activated by synaptic dysfunction, oxidative stress, and excitotoxicity. Nowadays, AD symptoms are manageable, but the disease itself re

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Min, W., and J. S. Pober. "TNF initiates E-selectin transcription in human endothelial cells through parallel TRAF-NF-kappa B and TRAF-RAC/CDC42-JNK-c-Jun/ATF2 pathways." Journal of Immunology 159, no. 7 (October 1, 1997): 3508–18. http://dx.doi.org/10.4049/jimmunol.159.7.3508.

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Abstract TNF acts on the E-selectin gene promoter at three kappa B elements and at a variant cAMP-responsive element that binds ATF2/c-Jun. In human endothelial cells, TNF rapidly induces N-terminal domain phosphorylation of both c-Jun and ATF2. Transient overexpression of N-terminal truncated c-Jun or catalytically inactive Jun N-terminal kinase (JNK) 1 and 2 inhibits TNF-induced transcription of an E-selectin but not a kappa B promoter-reporter gene. Transient overexpression of the TRAF2 adaptor protein can activate NF-kappaB and endogenous JNK, whereas N-terminal truncated TRAF2 protein blo

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BUTTERFIELD, Laura, Eve ZENTRICH, Andrew BEEKMAN, and Lynn E. HEASLEY. "Stress- and cell type-dependent regulation of transfected c-Jun N-terminal kinase and mitogen-activated protein kinase kinase isoforms." Biochemical Journal 338, no. 3 (March 8, 1999): 681–86. http://dx.doi.org/10.1042/bj3380681.

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The cJun N-terminal kinases (JNKs) are encoded by three genes generating ten protein kinase polypeptides and are activated in settings of cell stress, mitogenesis, differentiation and morphogenesis. The specific role of the JNK family members in these diverse cell programmes is largely undefined. In this study, we tested the hypothesis that individual JNK isoforms would exhibit distinct patterns of regulation within cells. The cDNAs encoding five haemagglutinin (HA)-tagged JNK isoforms (p46JNK1α, p54JNK2α, p54JNK2β, p46JNK3 and p54JNK3) were expressed in cultured rat PC12 phaeochromocytoma cel

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Izadi, Hooman, Amirreza T. Motameni, Tonya C. Bates, Elias R. Olivera, Vega Villar-Suarez, Ila Joshi, Renu Garg, et al. "c-Jun N-Terminal Kinase 1 Is Required for Toll-Like Receptor 1 Gene Expression in Macrophages." Infection and Immunity 75, no. 10 (July 30, 2007): 5027–34. http://dx.doi.org/10.1128/iai.00492-07.

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ABSTRACT The regulation of innate immune responses to pathogens occurs through the interaction of Toll-like receptors (TLRs) with pathogen-associated molecular patterns and the activation of several signaling pathways whose contribution to the overall innate immune response to pathogens is poorly understood. We demonstrate a mechanism of control of murine macrophage responses mediated by TLR1/2 heterodimers through c-Jun N-terminal kinase 1 (JNK1) activity. JNK controls tumor necrosis factor alpha production and TLR-mediated macrophage responses to Borrelia burgdorferi, the causative agent of

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Taniguchi, Cullen M., José O. Aleman, Kohjiro Ueki, Ji Luo, Tomoichiro Asano, Hideaki Kaneto, Gregory Stephanopoulos, Lewis C. Cantley та C. Ronald Kahn. "The p85α Regulatory Subunit of Phosphoinositide 3-Kinase Potentiates c-Jun N-Terminal Kinase-Mediated Insulin Resistance". Molecular and Cellular Biology 27, № 8 (5 лютого 2007): 2830–40. http://dx.doi.org/10.1128/mcb.00079-07.

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ABSTRACT Insulin resistance is a defining feature of type 2 diabetes and the metabolic syndrome. While the molecular mechanisms of insulin resistance are multiple, recent evidence suggests that attenuation of insulin signaling by c-Jun N-terminal kinase (JNK) may be a central part of the pathobiology of insulin resistance. Here we demonstrate that the p85α regulatory subunit of phosphoinositide 3-kinase (PI3K), a key mediator of insulin's metabolic actions, is also required for the activation of JNK in states of insulin resistance, including high-fat diet-induced obesity and JNK1 overexpressio

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Bare, Yohanes, Mansur S, Sri Sulystyaningsih Natalia Daeng Tiring, Dewi Ratih Tirto Sari, and Andri Maulidi. "Virtual Screening: Prediksi potensi 8-shogaol terhadap c-Jun N-Terminal Kinase (JNK)." Jurnal Penelitian dan Pengkajian Ilmu Pendidikan: e-Saintika 4, no. 1 (March 5, 2020): 1. http://dx.doi.org/10.36312/e-saintika.v4i1.157.

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JNK adalah gen yang berperan dalam metabolisme DMT2. Dalam pengobatan T2DM digunakan JNK sebagai potensi terapi dengan menggunakan bahan alam. 8-shogaol adalah komponen kimia yang terkandung dalam jahe yang memiliki aktivitas antioksidan. Tujuan dari penelitina ini adalah menginversitagasi dan menganalisis peran 8-shogaol terhadap JNK. Protein JNK (ID: 464Y) diperoleh dari Protein Data Bank dan ligan 8-shogaol (CID:6442560 ) didapat dari pubchem. Ligan dan protein didocking menggunakan Hex 8.0.0. File dalam bentuk pdb divisualtisasi dan analisis menggunakan Discovery Studio Client 4.1 software

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Gaarde, William A., Tony Hunter, Helen Brady, Brion W. Murray, and Mark E. Goldman. "Development of a Nonradioactive, Time-Resolved Fluorescence Assay for the Measurement of Jun N-Terminal Kinase Activity." Journal of Biomolecular Screening 2, no. 4 (June 1997): 213–23. http://dx.doi.org/10.1177/108705719700200406.

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Activated transcription factor AP-1 is composed of c-Jun homodimers or c-Jun/c-Fos heterodimers and mediates expression of several gene products that have been implicated in disease pathogenesis. Activation of AP-1 is dependent on phosphorylation of c-Jun by Jun N-terminal kinase (JNK). Therefore, identification of inhibitors of JNK-mediated phosphorylation of c-Jun may lead to a novel class of therapeutics. A nonradioactive, high-through-put, time-resolved fluorescence assay was developed to measure and identify inhibitors of JNK activity. This assay utilized a lanthanide (europium)-labeled a

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Clarke, Melanie, Rowan Pentz, Jessica Bobyn, and Shawn Hayley. "Stressor-Like Effects of c-Jun N-Terminal Kinase (JNK) Inhibition." PLoS ONE 7, no. 8 (August 29, 2012): e44073. http://dx.doi.org/10.1371/journal.pone.0044073.

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Ju, Youn H., and Chang H. Cho. "Effects of c-Jun N-Terminal Kinase(JNK) on Neurite Growth." Otolaryngology–Head and Neck Surgery 147, no. 2_suppl (August 2012): P206—P207. http://dx.doi.org/10.1177/0194599812451426a258.

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Bogoyevitch, Marie A., Kevin R. W. Ngoei, Teresa T. Zhao, Yvonne Y. C. Yeap, and Dominic C. H. Ng. "c-Jun N-terminal kinase (JNK) signaling: Recent advances and challenges." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1804, no. 3 (March 2010): 463–75. http://dx.doi.org/10.1016/j.bbapap.2009.11.002.

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Kumar, Ashok, Sunil K. Manna, Subhash Dhawan, and Bharat B. Aggarwal. "HIV-Tat Protein Activates c-Jun N-Terminal Kinase and Activator Protein-1." Journal of Immunology 161, no. 2 (July 15, 1998): 776–81. http://dx.doi.org/10.4049/jimmunol.161.2.776.

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Abstract Human immunodeficiency virus-1 tat (HIV-tat) protein, like other proinflammatory cytokines (such as TNF), activates a wide variety of cellular responses, some of which play a critical role in progression of HIV infection. Whether HIV-tat, like TNF, also activates c-Jun N-terminal kinase (JNK) and the transcription factor activator protein (AP)-1 is not known. We show that treatment of human histiocytic lymphoma U937 cells with the HIV-tat protein causes activation of JNK and AP-1 in a time- and dose-dependent manner. Transfection of a T cell line, H9 cells with the HIV-tat gene also r

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Xu, Ping, and Roger J. Davis. "c-Jun NH2-Terminal Kinase Is Required for Lineage-Specific Differentiation but Not Stem Cell Self-Renewal." Molecular and Cellular Biology 30, no. 6 (January 11, 2010): 1329–40. http://dx.doi.org/10.1128/mcb.00795-09.

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ABSTRACT The c-Jun NH2-terminal kinase (JNK) is implicated in proliferation. Mice with a deficiency of either the Jnk1 or the Jnk2 genes are viable, but a compound deficiency of both Jnk1 and Jnk2 causes early embryonic lethality. Studies using conditional gene ablation and chemical genetic approaches demonstrate that the combined loss of JNK1 and JNK2 protein kinase function results in rapid senescence. To test whether this role of JNK was required for stem cell proliferation, we isolated embryonic stem (ES) cells from wild-type and JNK-deficient mice. We found that Jnk1 −/− Jnk2 −/− ES cells

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Lim, Nicholas R., Colleen J. Thomas, Lokugan S. Silva, Yvonne Y. Yeap, Suwan Yap, James R. Bell, Lea M. D. Delbridge, et al. "Cardioprotective 3′,4′-dihydroxyflavonol attenuation of JNK and p38MAPK signalling involves CaMKII inhibition." Biochemical Journal 456, no. 2 (November 8, 2013): 149–61. http://dx.doi.org/10.1042/bj20121538.

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3′,4′-Dihydroxyflavonol, a cardioprotective compound that prevents cardiac injury and cell death, targets Ca2+/camodulin-dependent protein kinase II to inhibit the activation of the stress-activated protein kinases, c-Jun N-terminal kinase and p38 mitogen-activated protein kinase.

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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 (October 26, 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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