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Human MAPK9 Protein expressed in Wheat germ - ABIN1310315
Prause, Christensen, Billestrup, Mandrup-Poulsen: JNK1 protects against glucolipotoxicity-mediated beta-cell apoptosis. dans PLoS ONE 2014
As levels of intracellular H2O2 rise, a switch occurs from activation to inhibition of JNK2 activity, linking JNK2 regulation to the redox status of the cell.
results revealed that melatonin attenuated chemokine CCL24 levels through inhibition of the JNK pathway to hinder human osteosarcoma cell invasion, thereby highlighting the therapeutic potential of melatonin for osteosarcoma metastasis.
HMBG2 overexpression promotes ischemia/reperfusion-induced cell apoptosis through activating the JNK1/2-NF-kappaBp65 signaling in AC16 cardiomyocytes.
Taken together, the silencing of H4R inhibited the H4R mediated Mast cell functions and SAPK/JNK phosphorylation. Furthermore, the H4R activation utilized SAPK/JNK signaling pathway for IL-1beta release in HMC-1 cells.
RhoGDIbeta overexpression led to downregulation of miR-200c, whereas miR-200c was able directly to target 3'-UTR of jnk2mRNA and attenuated JNK2 protein translation, which resulted in attenuation of Sp1mRNA and protein expression in turn, inhibiting Sp1-dependent MMP-2 transcription.
The MAP kinase JNK2 mediates cigarette smoke-induced tissue factor activation, arterial thrombosis and reactive oxygen species production.
these data provide new evidence for an indispensable role for JNK/SAPK signaling to overcome the well-established molecular barriers in human somatic cell induced reprogramming.
We found p-JNK2 up-regulation in AUC and its early down-regulation in UC-CRC and CRC carcinogenesis.
JNK2 was a novel direct target of miR-20a-5p.
The release of infectious respiratory syncytial virus (RSV) virions from infected cells was significantly reduced by JNK1/2 siRNA knockdown, implicating JNK1/2 as a key host factor for RSV virus production.
PXR regulates the intestinal epithelial barrier during inflammation by modulating cytokine-induced MLCK expression and JNK1/2 activation
Phloretin is able to inhibit NSCLC A549 cell growth by inducing apoptosis through P38 MAPK and JNK1/2 pathways, and therefore may prove to be an adjuvant to the treatment of non-small cell lung cancer
In hepatocytes, JNK1 and JNK2 appear to have combined effects in protecting from drug-induced liver injury.
Inhibition of JNK1/2 activity suppressed Hedgehog pathway activity in acquired chemoresistant cancer cells.
although JNK activation and RIP3 expression are induced by FS, neither contributes to the liver injury.
These data suggest that JNK1/2 may play an important role in promoting the replication of Penicillium marneffei.
Interleukin-1 acts via the JNK-2 signaling pathway to induce aggrecan degradation by human chondrocytes.
miR200c attenuates P-gp-mediated MDR and metastasis by targeting JNK2/c-Jun signaling pathway in colorectal cancer.
JNK1/2 and p38 MAPK signaling pathways are beneficial to enterovirus 71 infection and positively regulate secretions of inflammatory cytokines in dendritic cells.
suppression of tumorigenesis by JNK requires ATF2.
These data suggest that JNK2 signaling activation is necessary for the atherosclerosis and hypertension induced by vitamin D deficiency
The up-regulation of HMGB1 was thought to be modified by dual channels: in the transcriptional level, it was regulated by JNK1/JNK2-ATF2 axis; post-transcriptionally, it was regulated by the microRNA (miR)-200 family, especially miR-429. miR-429 liver conditional knockout mice (miR-429(Deltahep)), fed either a normal diet or an HFD, showed severe liver inflammation and dysfunction, accompanied by greater expression of ...
these results identify a protective role of epithelial JNK2 signaling to maintain mucosal barrier function, epithelial cell integrity, and mucus layer production in the event of inflammatory tissue damage
activation of JNK in the endoplasmic reticulum stress response precedes activation of XBP1.
JNK-2 regulates aggrecan degradation in cultured murine cartilage and surgically induced osteoarthritis in vivo following mechanical destabilization of the knee joint.
activation of astrocyte MMP2/JNK1/2 contributes to the pathogenesis of pain hypersensitivity in the complex regional pain syndrome model
JNK1/2-dependent regulation of p66ShcS36 phosphorylation, is reported.
This study demonstrated that the disruption of JNK2 appears to have a greater impact on tolerance than the other isoforms in the tail-flick but not the hot-plate test.
morphine activated JNK2 through an arrestin-independent Src- and PKC-dependent mechanism, whereas fentanyl activated JNK2 through a Src-GRK3/arrestin-2-dependent and PKC-independent mechanism.
studies herein support that JNK2 inhibits cell differentiation in normal and cancer-derived mammary cells
Presynaptic c-Jun N-terminal Kinase 2 regulates NMDA receptor-dependent glutamate release.
gene deficient mice displayed defective mitophagy, which resulted in tissue damage under hypoxic stress, and increased sepsis
JNK1 and JNK2 play primarily opposing roles in mucosal hyperplasia and neutrophil recruitment early in otitis media.
JNK2 activates pro-survival autophagy and inhibits palmitic acid lipotoxicity in hepatocytes.
The activity of JNK1 and JNK2, but not JNK3, was required for the exclusive localization of angulin-1/LSR at the tTJs.
GITR stimulation of nTregs and signaling through JNK2, but not JNK1, triggered the loss of regulatory function while concomitantly gaining pathogenic CD4(+) T effector cell function responsible for exacerbating asthma-like immunopathology.
activation in response to laminar shear stress is biphasic, with an early peak and a later peak.
this study indicates that JNK2 is a physiological kinase responsible for eNOS-Ser(116) phosphorylation and regulates NO production.
Data show that proinflammatory cytokines induction was ERK1/2 and JNK1/2 dependent.
These data suggest that the p38 and JNK signaling pathways play pivotal roles in PRRSV replication and may regulate immune responses during virus infection.
Novel molecular mechanism to explain the exacerbation of early diabetic retinopathy by concomitant hypertension.
MPK9 and MPK12 are positive regulators of salicylic acid signaling in Arabidopsis guard cells.
MPK9 and MPK12 are key regulators mediating both abscisic acid (ABA) and Methyl jasmonate (MeJA) signalling in guard cells.
Data suggest that MPK9 is autoactivated via phosphorylation independent of any upstream MAPK kinase signaling; autophosphorylation occurs at both threonine and tyrosine residues in Thr-Asp-Tyr motif and in C-terminal regulatory extension.
MPK9 and MPK12 function redundantly downstream of extracellular reactive oxygen production and intracellular accumulation, cytosolic alkalisation and Ca(2+)cytosolic oscillation in yeast elcictor-induced stomatal closure
MPK9 and MPK12 act downstream of ROS and cytosolic Ca2+ and upstream of anion channels in the guard cell abscisic acid signaling cascade.
MAP kinases MPK9 and MPK12 are preferentially expressed in guard cells and positively regulate ROS-mediated ABA signaling.
The protein encoded by this gene is a member of the MAP kinase family. MAP kinases act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation and development. This kinase targets specific transcription factors, and thus mediates immediate-early gene expression in response to various cell stimuli. It is most closely related to MAPK8, both of which are involved in UV radiation induced apoptosis, thought to be related to the cytochrome c-mediated cell death pathway. This gene and MAPK8 are also known as c-Jun N-terminal kinases. This kinase blocks the ubiquitination of tumor suppressor p53, and thus it increases the stability of p53 in nonstressed cells. Studies of this gene's mouse counterpart suggest a key role in T-cell differentiation. Several alternatively spliced transcript variants encoding distinct isoforms have been reported.
mitogen-activated protein kinase 9
, Jun kinase
, MAP kinase 9
, MAPK 9
, c-Jun N-terminal kinase 2
, c-Jun kinase 2
, stress-activated protein kinase 1a
, stress-activated protein kinase JNK2
, JNK/SAPK alpha
, mitogen activated protein kinase 9
, protein kinase, mitogen-activated 9
, stress activated protein kinase alpha II
, janus kinase 2
, c-JUN amino-terminal kinase-2 alpha1