594 Inactivation of GSK3b results in nuclear accumulation of NFATc4 but is not involved in GATA-4 dependent stimulation of SERCA2a transcription

2005 ◽  
Vol 4 (1) ◽  
pp. 134-134
Keyword(s):  
Nuclear Accumulation ◽  
Stimulation Of

scholarly journals Varicella-Zoster Virus Modulates NF-κB Recruitment on Selected Cellular Promoters

2007 ◽  
Vol 81 (23) ◽  
pp. 13092-13104 ◽  
Author(s):  
Nadia El Mjiyad ◽  
Sébastien Bontems ◽  
Geoffrey Gloire ◽  
Julie Horion ◽  
Patricia Vandevenne ◽  
...  
Keyword(s):  
Varicella Zoster Virus ◽  
Target Genes ◽  
Nuclear Translocation ◽  
Nuclear Accumulation ◽  
Intercellular Adhesion Molecule ◽  
Intercellular Adhesion Molecule 1 ◽  
Necrosis Factor Alpha ◽  
Varicella Zoster ◽  
Tnf Α ◽  
Stimulation Of

ABSTRACT Intercellular adhesion molecule 1 (ICAM-1) expression is down-regulated in the center of cutaneous varicella lesions despite the expression of proinflammatory cytokines such as gamma interferon and tumor necrosis factor alpha (TNF-α). To study the molecular basis of this down-regulation, the ICAM-1 induction of TNF-α was analyzed in varicella-zoster virus (VZV)-infected melanoma cells (MeWo), leading to the following observations: (i) VZV inhibits the stimulation of icam-1 mRNA synthesis; (ii) despite VZV-induced nuclear translocation of p65, p52, and c-Rel, p50 does not translocate in response to TNF-α; (iii) the nuclear p65 present in VZV-infected cells is no longer associated with p50 and is unable to bind the proximal NF-κB site of the icam-1 promoter, despite an increased acetylation and accessibility of the promoter in response to TNF-α; and (iv) VZV induces the nuclear accumulation of the NF-κB inhibitor p100. VZV also inhibits icam-1 stimulation of TNF-α by strongly reducing NF-κB nuclear translocation in MRC5 fibroblasts. Taken together, these data show that VZV interferes with several aspects of the immune response by inhibiting NF-κB binding and the expression of target genes. Targeting NF-κB activation, which plays a central role in innate and adaptive immune responses, leads to obvious advantages for the virus, particularly in melanocytes, which are a site of viral replication in the skin.

scholarly journals AMP-activated protein kinase (AMPK) activation inhibits nuclear translocation of Smad4 in mesangial cells and diabetic kidneys

2015 ◽  
Vol 308 (10) ◽  
pp. F1167-F1177 ◽  
Author(s):  
Jinghong Zhao ◽  
Satoshi Miyamoto ◽  
Young-Hyun You ◽  
Kumar Sharma
Keyword(s):  
Kidney Disease ◽  
Diabetic Kidney Disease ◽  
Nuclear Translocation ◽  
Mesangial Cells ◽  
Nuclear Accumulation ◽  
Ampk Activation ◽  
Mesangial Matrix ◽  
Diabetic Kidney ◽  
Amp Activated Protein Kinase ◽  
Stimulation Of

Diabetic nephropathy is characterized by diffuse mesangial matrix expansion and is largely dependent on the TGF-β/Smad signaling pathway. Smad4 is required for TGF-β signaling; however, its regulation has not been well characterized in diabetic kidney disease. Here, we report that high glucose is sufficient to stimulate nuclear translocation of Smad4 in mesangial cells and that stimulation of the major energy sensor AMP-activated protein kinase (AMPK) has a potent effect to block Smad4 nuclear translocation. Activation of AMPK by 5-aminoimidazole-4-carboxamide-1-β-d-ribofuranoside (AICAR) inhibited high glucose-induced and TGF-β stimulation of nuclear Smad4. To identify which of the catalytic α-subunits may be involved, small interfering (si) RNA-based inhibition of AMPK α1- or α2-subunit was employed. Inhibition of either subunit reduced overall AMPK activity and contributed to Smad4 nuclear accumulation. In an animal model of early diabetic kidney disease, induction of diabetes was found to markedly stimulate Smad4 protein levels and enhance nuclear accumulation. AMPK activation with AICAR completely prevented the upregulation of Smad4 and reduced mesangial matrix accumulation. We conclude that stimulation of Smad4 in cell culture and in in vivo models of early diabetic kidney disease is dependent on AMPK.

Stimulation of insulin secretion and associated nuclear accumulation of iPLA2β in INS-1 insulinoma cells

2002 ◽  
Vol 282 (4) ◽  
pp. E820-E833 ◽  
Author(s):  
Zhongmin Ma ◽  
Sheng Zhang ◽  
John Turk ◽  
Sasanka Ramanadham
Keyword(s):  
Insulin Secretion ◽  
Enzymatic Activity ◽  
Cytosolic Calcium ◽  
Nuclear Accumulation ◽  
Nuclear Fraction ◽  
Β Cells ◽  
Β Protein ◽  
Specific Enzymatic Activity ◽  
Insulinoma Cells ◽  
Stimulation Of

Accumulating evidence suggests that the cytosolic calcium-independent phospholipase A2 (iPLA2β) manifests a signaling role in insulin-secreting (INS-1) β-cells. Earlier, we reported that insulin-secretory responses to cAMP-elevating agents are amplified in iPLA2β-overexpressing INS-1 cells (Ma Z, Ramanadham S, Bohrer A, Wohltmann M, Zhang S, and Turk J. J Biol Chem276: 13198–13208, 2001). Here, immunofluorescence, immunoaffinity, and enzymatic activity analyses are used to examine distribution of iPLA2β in stimulated INS-1 cells in greater detail. Overexpression of iPLA2β in INS-1 cells leads to increased accumulation of iPLA2β in the nuclear fraction. Increasing glucose concentrations alone results in modest increases in insulin secretion, relative to parental cells, and in nuclear accumulation of the iPLA2β protein. In contrast, cAMP-elevating agents induce robust increases in insulin secretion and in time-dependent nuclear accumulation of iPLA2β fluorescence, which is reflected by increases in nuclear iPLA2β protein content and specific enzymatic activity. The stimulated effects are significantly attenuated in the presence of cell-permeable inhibitors of protein phosphorylation and glycosylation. These findings suggest that conditions that amplify insulin secretion promote translocation of β-cell iPLA2β to the nuclei, where it may serve a crucial signaling role.

NF-κB2 processing and p52 nuclear accumulation after androgenic stimulation of LNCaP prostate cancer cells

2007 ◽  
Vol 19 (5) ◽  
pp. 1093-1100 ◽  
Author(s):  
Laurent Lessard ◽  
Fred Saad ◽  
Cécile Le Page ◽  
Jean-Simon Diallo ◽  
Benjamin Péant ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Cancer Cells ◽  
Nuclear Accumulation ◽  
Prostate Cancer Cells ◽  
Stimulation Of

Effects of 5-5'-Diphenyl-2-thiohydantoin (DPTH) and Thyroxine on the Ultrastructure and Chemical Composition of Rat Liver

1971 ◽  
Vol 29 ◽  
pp. 570-571
Author(s):  
E. A. Elfont ◽  
R. B. Tobin ◽  
D. G. Colton ◽  
M. A. Mehlman
Keyword(s):  
Chemical Composition ◽  
Rat Liver ◽  
Future Study ◽  
Mode Of Action ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Effective Inhibitor ◽  
Biochemical Effects ◽  
Glycerophosphate Dehydrogenase ◽  
Stimulation Of

Summary5,-5'-diphenyl-2-thiohydantoin (DPTH) is an effective inhibitor of thyroxine (T4) stimulation of α-glycerophosphate dehydrogenase in rat liver mitochondria. Because this finding indicated a possible tool for future study of the mode of action of thyroxine, the ultrastructural and biochemical effects of DPTH and/or thyroxine on rat liver mere investigated.Rats were fed either standard or DPTH (0.06%) diet for 30 days before T4 (250 ug/kg/day) was injected. Injection of T4 occurred daily for 10 days prior to sacrifice. After removal of the liver and kidneys, part of the tissue was frozen at -50°C for later biocheailcal analyses, while the rest was prefixed in buffered 3.5X glutaraldehyde (390 mOs) and post-fixed in buffered 1Z OsO4 (376 mOs). Tissues were embedded in Araldlte 502 and the sections examined in a Zeiss EM 9S.Hepatocytes from hyperthyroid rats (Fig. 2) demonstrated enlarged and more numerous mitochondria than those of controls (Fig. 1). Glycogen was almost totally absent from the cytoplasm of the T4-treated rats.

Gap junctions in the prothoracic glands of the tobacco hornworm, Manduca sexta

1992 ◽  
Vol 50 (1) ◽  
pp. 706-707
Author(s):  
Ji-da Dai ◽  
M. Joseph Costello ◽  
Lawrence I. Gilbert
Keyword(s):  
Gap Junctions ◽  
Small Molecules ◽  
Manduca Sexta ◽  
Freeze Fracture ◽  
Cell Communication ◽  
Cellular Level ◽  
Thin Sections ◽  
Prothoracic Glands ◽  
Polyhydroxylated Steroids ◽  
Stimulation Of

Insect molting and metamorphosis are elicited by a class of polyhydroxylated steroids, ecdysteroids, that originate in the prothoracic glands (PGs). Prothoracicotropic hormone stimulation of steroidogenesis by the PGs at the cellular level involves both calcium and cAMP. Cell-to-cell communication mediated by gap junctions may play a key role in regulating signal transduction by controlling the transmission of small molecules and ions between adjacent cells. This is the first report of gap junctions in the PGs, the evidence obtained by means of SEM, thin sections and freeze-fracture replicas.

Activator protein-1 is necessary for angiotensin-II stimulation of human adrenocorticotropin receptor gene transcription

2001 ◽  
Vol 268 (6) ◽  
pp. 1802-1810
Author(s):  
Danielle Naville ◽  
Estelle Bordet ◽  
Marie-Claude Berthelon ◽  
Philippe Durand ◽  
Martine Begeot
Keyword(s):  
Angiotensin Ii ◽  
Gene Transcription ◽  
Receptor Gene ◽  
Activator Protein 1 ◽  
Activator Protein ◽  
Stimulation Of
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