Expression of c-jun, junB, c-fos, fra-1 and fra-2 mRNA in the rat brain following seizure activity and axotomy

Beer, J.; Mielke, Kirsten; Zipp, Monika; Zimmermann, M.; Herdegen, Thomas

doi:10.1016/s0006-8993(98)00233-9

Cited by 41 publications

(17 citation statements)

References 38 publications

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“…The implication that high levels of eIF2α(P) lead to protein synthesis shut off in hippocampal neurons is apparently at odds with data on the expression of IEG (immediate early gene) proteins in the hippocampus in experimental models of epilepsy, such as c-Jun and c-Fos [45,46]. The expression of these proteins at early SE (30 min), however, has been observed in the hippocampal granule cells where little eIF2α(P) was detected by immunohistochemistry [11].…”

Section: Discussionmentioning

confidence: 98%

Phosphorylation of the α subunit of translation initiation factor-2 by PKR mediates protein synthesis inhibition in the mouse brain during status epilepticus

Carnevalli

Pereira

Jaqueta

et al. 2006

Biochemical Journal

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In response to different cellular stresses, a family of protein kinases phosphorylates eIF2alpha (alpha subunit of eukaryotic initiation factor-2), contributing to regulation of both general and genespecific translation proposed to alleviate cellular injury or alternatively induce apoptosis. Recently, we reported eIF2alpha(P) (phosphorylated eIF2alpha) in the brain during SE (status epilepticus) induced by pilocarpine in mice, an animal model of TLE (temporal lobe epilepsy) [Carnevalli, Pereira, Longo, Jaqueta, Avedissian, Mello and Castilho (2004) Neurosci. Lett. 357, 191-194]. We show in the present study that one eIF2alpha kinase family member, PKR (double-stranded-RNA-dependent protein kinase), is activated in the cortex and hippocampus at 30 min of SE, reflecting the levels of eIF2alpha(P) in these areas. In PKR-deficient animals subjected to SE, eIF2alpha phosphorylation was clearly evident coincident with activation of a secondary eIF2alpha kinase, PEK/PERK (pancreatic eIF2alpha kinase/RNA-dependent-protein-kinase-like endoplasmic reticulum kinase), denoting a compensatory mechanism between the two kinases. The extent of eIF2alpha phosphorylation correlated with the inhibition of protein synthesis in the brain, as determined from polysome profiles. We also found that C57BL/6 mice, which enter SE upon pilocarpine administration but are more resistant to seizure-induced neuronal degeneration, showed very low levels of eIF2alpha(P) and no inhibition of protein synthesis during SE. These results taken together suggest that PKR-mediated phosphorylation of eIF2alpha contributes to inhibition of protein synthesis in the brain during SE and that sustained high levels of eIF2alpha phosphorylation may facilitate ensuing cell death in the most affected areas of the brain in TLE.

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Section: Discussionmentioning

confidence: 98%

Phosphorylation of the α subunit of translation initiation factor-2 by PKR mediates protein synthesis inhibition in the mouse brain during status epilepticus

Carnevalli

Pereira

Jaqueta

et al. 2006

Biochemical Journal

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“…This temporally staggered, but nevertheless congruent, AP-1 expression pattern is visible at mRNA and protein level following transynaptic stimulation e.g. following kainic acid or noxious stimulation (Beer et al, 1998;Herdegen and Leah, 1998). One essential particularity of c-Jun is its selective induction in the absence of other AP-1 proteins.…”

Section: Regulation Of Pathological-degenerative Functions Of the C-jmentioning

confidence: 89%

AP-1 proteins in the adult brain: facts and fiction about effectors of neuroprotection and neurodegeneration

Herdegen¹,

Waetzig²

2001

Oncogene

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187

118

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“…There is considerable structural similarity between promoters of the two genes. Both genes share a number of sequentially ordered putative enhancer elements in the 5' regulatory region (Yoshida et al, 1993, Foletta et al, 1994, Beer et al, 1998, allowing for the possibility of some overlap in trans-activation profiles. However, there are several key differences in the promoters of the two genes as well.…”

Section: Discussionmentioning

confidence: 99%

“…Early northern blot studies revealed readily detectable basal levels of fra-2 in whole mouse brain homogenates, contrasting with the much lower basal expression of other members of the fos family (including c-fos, fra-1, fra-2, and fosB) (Foletta et al, 1994). fra-2 mRNA expression, as detected by in situ hybridization, has only been described for the hippocampus (Beer et al, 1998), and the suprachiasmatic (SCN) and paraventricular nuclei (PVN) of the hypothalamus (Honkaniemi et al, 1994, Schwartz et al, 2000.…”

Section: Introductionmentioning

confidence: 99%

Restraint-induced fra-2 and c-fos expression in the rat forebrain: Relationship to stress duration

2007

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The protein product of the fra-2 gene (Fra-2), a fos-family member, can compete with Fos protein for participation in AP-1 transcription factor complexes and each protein can contribute different transactivational consequences to an AP-1 complex. To date, there is limited characterization of fra-2 mRNA expression in the rat forebrain. We examined basal and restraint-induced mRNA expression (in situ hybridization) of fra-2 in the rat forebrain and compared its temporal-spatial pattern to c-fos. In contrast to the very low basal expression of c-fos, fra-2 basal expression was moderately high throughout cortex and some subcortical structures, including prominent basal expression in the hypothalamic paraventricular nucleus (PVN). Restraint-induced fra-2 expression was quantified in the prefrontal cortex (PFC), lateral septum (LS) and PVN. Maximal fra-2 gene induction in the PFC and LS was delayed (60 min) after restraint onset with respect to c-fos (15 min), whereas in the PVN, fra-2 mRNA increased within 15 min of restraint. Additionally we compared c-fos and fra-2 gene expression in rats given shorter or longer restraint durations, but equal total time from stress onset to sample collection, to determine the extent to which the kinetics of gene induction matched that of a hypothalamic-pituitary-adrenal axis hormone response. Rats given 45 min recovery after 15 min restraint showed less c-fos expression in the PVN, less fra-2 expression in the prelimbic and infralimbic PFC, and no difference in the LS compared with rats restrained for 60 min. Thus, the expression of both genes was sensitive to stressor duration, but this sensitivity varied with brain region. Differential basal and stress-induced expression patterns of the fra-2 and c-fos genes are likely to have important functional consequences for AP-1 transcription factor dependent regulation of neural plasticity.

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Expression of c-jun, junB, c-fos, fra-1 and fra-2 mRNA in the rat brain following seizure activity and axotomy

Cited by 41 publications

References 38 publications

Phosphorylation of the α subunit of translation initiation factor-2 by PKR mediates protein synthesis inhibition in the mouse brain during status epilepticus

Phosphorylation of the α subunit of translation initiation factor-2 by PKR mediates protein synthesis inhibition in the mouse brain during status epilepticus

AP-1 proteins in the adult brain: facts and fiction about effectors of neuroprotection and neurodegeneration

Restraint-induced fra-2 and c-fos expression in the rat forebrain: Relationship to stress duration

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