Tumor Necrosis Factor ä-Induced E-selectin Expression Is Activated by the Nuclear Factor-κB and c-JUN N-terminal Kinase/p38 Mitogen-activated Protein Kinase Pathways

Read, Margaret; Whitley, Maryann Z.; Gupta, Shashi; Pierce, Jacqueline W.; Best, Jennifer L.; Davis, Roger J.; Collins, Tucker

doi:10.1074/jbc.272.5.2753

Cited by 318 publications

(240 citation statements)

References 72 publications

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“…This is in contrast to other data using transformed and established fibroblast cell lines, which suggests that signaling by the mitogen-activated protein (MAP) kinase cascade plays the dominant role in stimulating cellular proliferation (Williams and Roberts, 1994). JNK1/2 have been shown to be activated by a variety of similar stimuli, such as by hepatocyte growth factor (HGF), the proinflammatory cytokine tumor necrosis factor ␣ (TNF␣), and hyperosmotic shock (Bagrodia et al, 1995;Read et al, 1997;Rodrigues et al, 1997;Whitmarsh et al, 1997). However, despite this evidence, the direct significance of JNK1/2 activation or c-Jun function in proliferative responses of nontransformed, nonestablished epithelial cells has not been definitively tested by molecular dissection of this pathway.…”

Section: Introductioncontrasting

confidence: 51%

“…These data, along with the data presented in this article and elsewhere (Westwick et al, 1995;Bogoyevitch et al, 1996;Loyer, et al, 1996;Read et al, 1997;Whitmarsh et al, 1997) strongly suggest that the coordinate actions/activities of both the JNK/SAP kinase and p38-RK cascades play essential roles in the regulation of DNA synthesis in hepatocytes.…”

Section: Discussionmentioning

confidence: 82%

“…To test whether JNK1 activation is modulating c-Jun phosphorylation at its NH 2 terminus in our system, plasmids containing control (null plasmid), dominant-negative Ras N17 , dominantnegative Rac1 N17 , dominant-negative Cdc42 N17 , dominant-negative JNK1, and dominant-negative SEK1 (Verheij et al, 1996;Read et al, 1997;Rodrigues et al, 1997) were infected into hepatocytes at a high moi using a poly-l-lysine-conjugated adenovirus system. The infected hepatocytes were treated 24 h later with either 50 mM glucose, 1 ng/ l HGF, or 1 ng/ l TNF␣ for either 10 min (Table 1) or 20 min (Figure 2).…”

Section: Glucose Tnf␣ and Hgf Treatments Of Hepatocytesmentioning

confidence: 99%

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The Ras/Rac1/Cdc42/SEK/JNK/c-Jun Cascade Is a Key Pathway by Which Agonists Stimulate DNA Synthesis in Primary Cultures of Rat Hepatocytes

Auer¹,

Contessa²,

Brenz-Verca

et al. 1998

MBoC

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126

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The ability of signaling via the JNK (c-Jun NH2-terminal kinase)/stress-activated protein kinase cascade to stimulate or inhibit DNA synthesis in primary cultures of adult rat hepatocytes was examined. Treatment of hepatocytes with media containing hyperosmotic glucose (75 mM final), tumor necrosis factor α (TNFα, 1 ng/ml final), and hepatocyte growth factor (HGF, 1 ng/ml final) caused activation of JNK1. Glucose, TNFα, or HGF treatments increased phosphorylation of c-Jun at serine 63 in the transactivation domain and stimulated hepatocyte DNA synthesis. Infection of hepatocytes with poly-l-lysine–coated adenoviruses coupled to constructs to express either dominant negatives Ras N17, Rac1 N17, Cdc42 N17, SEK1−, or JNK1− blunted the abilities of glucose, TNFα, or HGF to increase JNK1 activity, to increase phosphorylation of c-Jun at serine 63, and to stimulate DNA synthesis. Furthermore, infection of hepatocytes by a recombinant adenovirus expressing a dominant-negative c-Jun mutant (TAM67) also blunted the abilities of glucose, TNFα, and HGF to stimulate DNA synthesis. These data demonstrate that multiple agonists stimulate DNA synthesis in primary cultures of hepatocytes via a Ras/Rac1/Cdc42/SEK/JNK/c-Jun pathway. Glucose and HGF treatments reduced glycogen synthase kinase 3 (GSK3) activity and increased c-Jun DNA binding. Co-infection of hepatocytes with recombinant adenoviruses to express dominant- negative forms of PI3 kinase (p110α/p110γ) increased basal GSK3 activity, blocked the abilities of glucose and HGF treatments to inhibit GSK3 activity, and reduced basal c-Jun DNA binding. However, expression of dominant-negative PI3 kinase (p110α/p110γ) neither significantly blunted the abilities of glucose and HGF treatments to increase c-Jun DNA binding, nor inhibited the ability of these agonists to stimulate DNA synthesis. These data suggest that signaling by the JNK/stress-activated protein kinase cascade, rather than by the PI3 kinase cascade, plays the pivotal role in the ability of agonists to stimulate DNA synthesis in primary cultures of rat hepatocytes.

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Section: Introductioncontrasting

confidence: 51%

Section: Discussionmentioning

confidence: 82%

Section: Glucose Tnf␣ and Hgf Treatments Of Hepatocytesmentioning

confidence: 99%

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The Ras/Rac1/Cdc42/SEK/JNK/c-Jun Cascade Is a Key Pathway by Which Agonists Stimulate DNA Synthesis in Primary Cultures of Rat Hepatocytes

Auer¹,

Contessa²,

Brenz-Verca

et al. 1998

MBoC

Self Cite

126

112

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“…Although regulated distinctively, this interaction does therefore appear to be conserved. In vitro evidence suggests that p38 and JNK can interact with the DNA-bound transcription factors ATF-2 and Jun, respectively (Read et al, 1997). This study reports that the interactions are constitutive in mammalian Journal of Cell Science 117 (17)…”

Section: Hog1p Kinase As a Central Component Of Yeast Transcription Cmentioning

confidence: 80%

“…Interaction of these docking sites with corresponding motifs in MAPKs could provide a molecular basis for stable and specific MAPK recruitment. A conserved MAPK domain, the common Journal of Cell Science 117 (17) Cano et al, 1995;Yang et al, 1998c;Yang et al, 1998b;Rao and Reddy, 1994 Yang et al, 1998b;Gupta et al, 1996 Jun GST pulldown, CIP Kallunki et al, 1996;Adler et al, 1992;Dai et al, 1995;Cano et al, 1995;Read et al, 1997;Gupta et al, 1996;Kallunki et al, 1994;Sluss et al, 1994;Hibi et al, 1993;Derijard et al, 1994 SAP-2 GST pulldown Ducret et al, 2000 ATF-2 GST pulldown Livingstone et al, 1995;Gupta et al, 1995;Gupta et al, 1996;Raingeaud et al, 1995 JunB GST pulldown Gupta et al, 1996;Kallunki et al, 1996 docking (CD) domain, is often used in the interaction with docking sites in MAPKKs, MKPs (MAPK-phosphatases) and MAPKAPKs (Tanoue and Nishida, 2003). However, whether or not the D domain of particular transcription factors can interact with the CD domain is not known.…”

Section: Protein Domains Potentially Involved In Stable and Specific mentioning

confidence: 99%

MAP kinases as structural adaptors and enzymatic activators in transcription complexes

Edmunds

Mahadevan

2004

Journal of Cell Science

103

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Mitogen-activated protein kinase (MAPK) pathways regulate eukaryotic gene expression in response to extracellular stimuli. MAPKs and their downstream kinases phosphorylate transcription factors, co-regulators and chromatin proteins to initiate transcriptional changes. However, the spatial context in which the MAPKs operate in transcription complexes is poorly understood. Recent findings in budding yeast show that MAPKs can form integral components of transcription complexes and have novel structural functions in addition to phosphorylating local substrates. Hog1p MAPK is stably recruited to target promoters by specific transcription factors in response to osmotic stress, and acts as both a structural adaptor and enzymatic activator driving the assembly and activation of the transcription complex. We review the evidence that suggests a similar bifunctional role for MAPKs in mammalian transcription complexes.

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Constitutive activity and differential localization of p38? and p38? MAPKs in adult mouse brain

et al. 2000

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To understand the roles of p38 mitogen-activated protein kinase (p38 MAPK) isoforms in adult mouse brain, in vivo activities and detailed expression patterns of two p38 isoforms, p38alpha and p38beta, were examined by using biochemical and immunohistochemical analyses. The result indicated that the activity of both p38alpha and p38b MAPKs in normal adult mouse brain was remarkably high, and the nuclear pool of the p38 isoforms was primarily responsible for most of the constitutive p38 MAPK activity in brain. Both p38alpha and p38beta were highly expressed in brain areas including cerebral cortex, hippocampus, cerebellum, and few nuclei of the brainstem. At the subcellular level, p38alpha was distributed in dendrites and in cytoplasmic and nuclear regions of cell body of neurons, which is in contrast to p38beta, since p38beta was preferentially expressed in nucleus of neurons. These results suggest that the p38 pathway may play an important role, not only in inflammation and neuronal cell death as previously suggested, but also in normal physiology of adult mouse brain.

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Tumor Necrosis Factor ä-Induced E-selectin Expression Is Activated by the Nuclear Factor-κB and c-JUN N-terminal Kinase/p38 Mitogen-activated Protein Kinase Pathways

Cited by 318 publications

References 72 publications

The Ras/Rac1/Cdc42/SEK/JNK/c-Jun Cascade Is a Key Pathway by Which Agonists Stimulate DNA Synthesis in Primary Cultures of Rat Hepatocytes

The Ras/Rac1/Cdc42/SEK/JNK/c-Jun Cascade Is a Key Pathway by Which Agonists Stimulate DNA Synthesis in Primary Cultures of Rat Hepatocytes

MAP kinases as structural adaptors and enzymatic activators in transcription complexes

Constitutive activity and differential localization of p38? and p38? MAPKs in adult mouse brain

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