Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Jun”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 91 records · Page 5Linked to original sources
PubMed2004

Interaction of an approximately 40 kDa protein from regenerating rat liver with the -148 to -124 region of c-jun complexed with RLjunRP coincides with enhanced c-jun expression in proliferating rat liver.

The c-jun belongs to the family of proto-oncogenes and encodes for the protein Jun, a component of transcription factor AP-1 involved in regulation of the expression of genes indispensable for cell proliferation and differentiation. While the role of c-jun in the regulation of such genes has been well examined, the regulation of c-jun in proliferating cells is not fully understood. We have earlier reported that the -148 to -124 region of c-jun is involved in the positive regulation of c-jun transcription, and interacts with a positive regulatory factor (rat liver jun regulatory protein; RLjunRP) present in rat liver. In this investigation, we report that this region is differentially recognized in proliferating liver as evidenced by the formation of a complex, different from that observed with normal liver extract. The new complex appears as early as 2 h after partial hepatectomy and its appearance coincides with the rise in c-jun mRNA levels after partial hepatectomy. In regenerating rat liver nuclear extract, an additional protein of approximately 40 kDa (rRLjunRP) interacts with a pre-existing dimer of RLjunRP complexed with the -148 to -124 region of c-jun to form a slow-migrating complex. rRLjunRP appears to pre-exist in the cytosol and translocate to the nucleus as indicated by the continued presence of the retarded complex in nuclear extract prepared from partially hepatectomized rats treated with cycloheximide. UV crosslinking studies, South-Western blot analysis, SDS/PAGE of affinity-purified factor(s), and 2D-PAGE analysis clearly demonstrate that the additional factor induced in response to growth stimulus is an approximately 40 kDa, that binds with the dimer of RLjunRP and enhances the c-jun transcription.

Animals↗
PubMed1996

Age-related changes in light-induced Jun-B and Jun-D expression: effects of transplantation of fetal tissue containing the suprachiasmatic nucleus.

Fos and Jun mRNA and peptide exhibit a daily light-induced rhythm in the suprachiasmatic nucleus (SCN). The authors previously have reported that Fos expression in the SCN is elevated prematurely during the dark, light-induced Fos expression is attenuated in middle-aged rats, and transplantation of fetal SCN tissue into the third ventricle of rats of this age restores the daily pattern of Fos expression to that of the young. Using immunocytochemistry, the authors performed the present study to determine whether Jun-B and Jun-D expression in the SCN is altered at the same stage during aging and, if so, whether transplantation of fetal tissue containing the SCN can restore the light-induced rhythms of these two immediate early genes. All groups of rats were transcardially perfused 90 min prior to and after light onset. In young rats, light induced a robust increase in the number of Jun-B positive cells in the SCN, whereas very few cells were labeled before light onset. In middle-aged rats, the light-induced increase in the number of Jun-B positive cells was significantly attenuated. Transplantation of fetal SCN tissue into the middle-aged rats successfully restored light-induced Jun-B expression to the levels of young rats. By contrast, Jun-D exhibited a constitutively high level of expression in the SCN both before and after light onset, and light induced only a slight but significant increase. No age-related changes were detected in the expression of Jun-D either before or after light onset. Transplantation of fetal SCN tissue did not alter the daily pattern of Jun-D expression in the middle-aged rats. These data suggest that (1) light-induced activation of SCN neural activity is blunted during aging, (2) fetal SCN tissue can provide the critical support to allow the host to respond properly to light cues, and (3) the age-related change in Jun-B expression in the middle-aged host SCN can be rescued by fetal SCN transplants.

Aging↗
PubMed1992

Regulation of c-fos, c-jun and jun-B messenger ribonucleic acids by angiotensin-II and corticotropin in ovine and bovine adrenocortical cells.

Previous work has shown that corticotropin (ACTH) and angiotensin-II (A-II), in addition to their acute steroidogenic effects, exert long-term influences on adrenal cell differentiated function, stimulatory or inhibitory, respectively. Certain nuclear proto-oncogenes have been implicated in the regulation of gene expression in many cell systems. We have investigated the effects of ACTH and A-II on the levels of c-fos, c-jun, and jun-B messenger RNAs (mRNAs), in bovine and ovine (OAC) adrenal fasciculata cells. In both cell types ACTH produced time- (maximum at 1 h) and dose-dependent (ED50 congruent to 10(-12) M) increase in c-fos (2- to 4-fold) and jun-B (10- to 20-fold) mRNA levels but did not affect c-jun. The concentrations required to induce half-maximal mRNA accumulation and cortisol production were similar. A-II also produced a dose-dependent increase in c-fos and jun-B mRNAs but also in c-jun in both cell types, despite the fact that OAC are resistant to the steroidogenic action of the hormone. The stimulatory effects of A-II on c-fos mRNA were higher than those produced by ACTH, whereas the effects on jun-B were similar but ACTH abolished (OAC) or decreased (bovine adrenal fasciculata cells) the stimulatory effects of A-II on c-jun mRNA. The effects of ACTH and A-II on cortisol production and proto-oncogene mRNAs were in part mimicked by 8 Bromo-cAMP and the phorbol ester phorbol-12-myristate-13 acetate plus calcium ionophore A23187, respectively. In the presence of cycloheximide, which blocks the steroidogenic effects of both hormones, proto-oncogene mRNAs were superinduced by both hormones. This result, together with the fact that dexamethasone failed to affect the mRNA levels suggests that the stimulatory effects of ACTH and A-II on proto-oncogene expression were not related to an autocrine/intracrine action of cortisol. Taken together, these findings show that the proto-oncogene mRNAs in normal adrenal cells are regulated by ACTH and A-II, acting through different intracellular pathways. They also demonstrate differential responsiveness of the Jun family to both hormones. Thus, the opposite long-term action of ACTH and A-II on adrenal cell differentiated function could be mediated by its different initial effects on proto-oncogene expression, in particular in the members of the Jun family.

8-Bromo Cyclic Adenosine Monophosphate↗
PubMed1996

Developmental expression and activities of specific fos and jun proteins are functionally related to osteoblast maturation: role of Fra-2 and Jun D during differentiation.

Developmental studies of oncogene expression implicate the Fos and Jun family of transcription factors in the regulation of bone growth and differentiation. Promoters of many developmentally regulated genes, including osteocalcin, a marker of osteoblast differentiation, contain AP-1 sites that bind Fos/Jun dimers. Here, we demonstrate that the selective expression of fos- and jun-related genes is functionally related to the stage of osteoblast growth and differentiation in vitro. During osteoblast proliferation, nuclear protein levels of all seven activating protein-1 (AP-1) members are maximal. Subsequently, during the period of extracellular matrix maturation, levels decline. In fully differentiated osteoblasts, Fra-2 and (to a lesser extent) Jun D are the principal AP-1 members detectable by Western blot analysis. AP-1 complex composition and binding activity also exhibit developmental changes. All Fos and Jun family members are involved in AP-1 complex formation in proliferating cells, whereas Fra-2 and Jun D predominate in AP-1 complexes in differentiated osteoblasts. Overexpression of Fos and Jun family members in ROS 17/2.8 cells markedly affects the expression of an osteocalcin promoter-chloramphenicol acetyltransferase construct. Coexpression of only one AP-1 pair, Fra-2 and Jun D, stimulated reporter expression, whereas coexpression of other AP-1 pairs down-regulated expression (i.e. c-jun and any Fos family member) or had no effect (i.e. Fra-1 and Jun B). Promoter deletion analyses indicate that these effects are site specific. Consequential effects of Fra-2 on osteoblast differentiation are further demonstrated by antisense studies in which osteoblast differentiation and the development of a bone tissue-like organization were suppressed. Consistent with recent findings suggesting that AP-1 complex composition can selectively regulate gene transcription, our findings demonstrate that differential expression of Fos and Jun family members could play a role in the developmental regulation of bone-specific gene expression and, as a result, may be functionally significant for osteoblast differentiation.

Animals↗
PubMed1994

A peptide encoding the c-Jun delta domain inhibits the activity of a c-jun amino-terminal protein kinase.

Evidence suggests that the c-Jun protooncogene delta (delta) domain (amino acids 31-60) helps regulate the transcriptional activating capacity of c-Jun by modulating the amino-terminal phosphorylation of this protein. By using a peptide encoding the delta domain and purified amino-terminal c-Jun protein kinase, we demonstrate that the delta domain peptide inhibits phosphorylation of the amino terminus of both c-Jun and the related protein JunD. The delta domain peptide inhibited the activation of the c-Jun amino-terminal protein kinase by phorbol esters in permeabilized U937 leukemic cells. Mutation of c-Jun followed by transfection into U937 leukemic cells demonstrated that partial deletions of the delta domain are sufficient to block phosphorylation of the amino terminus of c-Jun. In vitro deletion of the amino-terminal (amino acids 31-44) half of the delta domain inhibited the phosphorylation of c-Jun. However, deletion of the carboxyl-terminal (amino acids 45-60) half only partially inhibited c-Jun phosphorylation. Therefore, these results indicate that the delta domain sequence is an important regulator of c-Jun amino-terminal phosphorylation.

Amino Acid Sequence↗
PubMed2002

Regulation of platinum-compound cytotoxicity by the c-Jun N-terminal kinase and c-Jun signaling pathway in small-cell lung cancer cells.

Cytotoxic platinum compounds including cisplatin are standard cancer chemotherapeutics and are also activators of stress-signaling pathways. In this study, we tested the role of the c-Jun N-terminal kinase (JNK) family of mitogen-activated protein kinases and their transcription factor target, c-Jun, in the cytotoxic response of small-cell lung cancer (SCLC) cells to cisplatin and its less effective trans-isomer, transplatin. Both agents stimulated JNK activity; the transplatin response was rapid and transient, whereas JNK activation by cisplatin was delayed and sustained. Despite the differential kinetics of JNK activation, expression of nonphosphorylatable JNK mutants sensitized the SCLC cells to killing by cisplatin or transplatin, suggesting that JNK activation in response to these agents signals a protective response. Consistent with this finding, overexpression of the JNK target, c-Jun, significantly protected SCLC cells from platinum compounds, whereas expression of a c-Jun mutant encoding only the DNA binding domain increased the sensitivity of the SCLC cells to these drugs. These findings support the hypothesis that activation of the JNKs by platinum compounds controls c-Jun-dependent transcriptional events that promote a protective response in SCLC cells. Oligonucleotide array analysis identified genes encoding a variety of signaling proteins whose expression was reciprocally changed by c-Jun and c-Jun-DBD (c-Jun-DNA binding domain). It is noteworthy that genes whose products are involved in DNA repair, glutathione synthesis, or drug accumulation did not exhibit altered expression by c-Jun or c-Jun-DBD. The findings indicate that inhibition of the JNK pathway is a potential means to enhance the sensitivity of SCLC cells to platinum compounds.

Carcinoma, Small Cell↗
PubMed1995

c-jun and multistage carcinogenesis: association of overexpression of introduced c-jun with progression toward a neoplastic endpoint in mouse JB6 cells sensitive to tumor promoter-induced transformation.

Tumor promoters such as 12-O-tetradecanoylphorbol-13-acetate (TPA) and epidermal growth factor (EGF) induce neoplastic transformation, elevated c-jun protein expression, and activator protein-1 (AP-1)-dependent gene expression in JB6 mouse epidermal cells sensitive to tumor promoters (clone 415a P+ cells). In contrast, JB6 cells resistant to tumor promoter-induced transformation (clone 307b P- cells) exhibit a greatly reduced TPA or EGF inducible c-jun expression and AP-1 activity. We have recently shown that induced AP-1 is necessary for tumor promoter-induced transformation of P+ cells because introduction of a dominant negative c-jun mutant into P+ cells inhibits both AP-1 dependent transactivation and the transformation response to tumor promoter. The intent of the investigation presented here was to test the hypothesis that elevation of AP-1 activity is sufficient to cause progression to the P+ phenotype in P- cells or to the transformed phenotype in P+ cells. Clonally derived P+ and P- recipient cells transfected with a human c-jun expression construct and overexpressing c-jun protein were tested for progression by assaying for constitutive or inducible anchorage independent phenotype and nude-mouse tumorigenicity. Overexpression of c-jun did not produce progression in P- cells but did increase the probability of progression in P+ cells (two of five transfectant cell lines progressed to the tumor phenotype). In addition, c-jun overexpression did not increase AP-1 activity in any of the P-/c-jun transfectants or in the two of five P+/c-jun transfectants that acquired the transformed phenotype. The P+/c-jun transfectants that showed elevated AP-1 activity did not progress to the tumor phenotype, demonstrating that an increase in AP-1 activity is insufficient for this progression. Since P(+)-to-tumor phenotype progression occurred in cells overexpressing c-jun but not AP-1, we propose that P(+)-to-transformed phenotype progression is c-jun dependent and AP-1 independent.

Animals↗
PubMed1990

Control of c-Jun activity by interaction of a cell-specific inhibitor with regulatory domain delta: differences between v- and c-Jun.

Analysis of transcriptional activation properties of c-Jun chimeras in different cell lines suggests that it contains an activator domain (A1) that is negatively regulated by a cell type-specific inhibitor. A regulatory domain of c-Jun, delta, previously identified by in vitro experiments, also regulates transcriptional activation by c-Jun in vivo. The delta domain facilitates or stabilizes the interaction of the cellular inhibitor with A1. v-Jun, which lacks delta, is a stronger transcriptional activator than c-Jun, since its activity is not efficiently repressed by the cellular inhibitor. In vitro transcription with chimeric Jun proteins and extracts from different cell types confirms that the A1 and delta domains are repressed in a cell type-specific manner. These findings implicate a specific cellular factor in the negative regulation of c-Jun activity and suggest a molecular basis for the observed difference in transcriptional properties between v-Jun and c-Jun.

Animals↗
PubMed1999

Differential induction of c-Fos, c-Jun and Jun B in the rat central nervous system following unilateral entorhinal cortex lesion.

In order to identify some of the molecular mechanisms that occur after a central nervous system trauma, the immediate early gene encoded proteins c-Fos, c-Jun and Jun B were analysed by immunocytochemistry following unilateral entorhinal cortex lesion (controls, 30 min, 2, 5, 12 and 24 h, two, six, 10 and 14 days, four weeks and six months postlesion). In the dentate gyrus, c-Fos was induced in some supragranular neurons (30 min), massively expressed in granule cells ipsilaterally to the lesion (2 h), expressed in hilar neurons (5 h and two days) and was absent at all later stages. A basal expression of c-Jun was found in dentate granule cells of controls, which was strongly increased on the lesion side (2 h) and on the side contralateral to the lesion (12 h). c-Jun expression returned to control levels by 24 h. Jun B was induced in granule cells ipsilateral to the lesion within 2 h and was back to control levels by 5 h. In the lateral septal area, c-Fos and c-Jun were induced 30 min postlesion and decreased rapidly thereafter. In the cerebral cortex, a widespread induction of c-Fos and c-Jun occurred within 30 min after entorhinal cortex lesion and this up-regulation lasted until two days postlesion. These data indicate that electrolytic lesion of the entorhinal cortex leads to a rapid and widespread induction of c-Fos, c-Jun and Jun B. Within the denervated fascia dentata, some of these changes may be linked to the reorganization processes following the lesion. Alternatively, the alterations in immediate early gene expression reported here may be due to changes in synaptic activity or postlesional seizures which occur in this lesioning paradigm.

Animals↗
PubMed2003

Oncogenic effect of delta deletion in v-Jun does not result from uncoupling Jun from JNK signaling.

The protein encoded by the v-Jun oncogene shows increased transforming activity compared to c-Jun, its normal cellular counterpart. One major determinant of this increased transforming activity is an in-frame deletion of a region near the amino-terminus of the protein. This region, referred to as the delta domain, functions as a docking site for Jun N-terminal kinase (JNK), the mitogen-activated protein (MAP) kinase that phosphorylates c-Jun to regulate its transcriptional properties. As a consequence of this deletion, v-Jun is unresponsive to JNK signaling, and it is widely believed that it is the uncoupling of v-Jun from JNK signaling that underlies the oncogenic effects of the delta-domain deletion; however, this idea has never been directly tested. Here we use JNK overexpression as well as alanine scanning mutagenesis to test this idea. Point mutants that are uncoupled from JNK signaling do not show enhanced transforming activity, suggesting that disruption of the Jun-JNK interaction is not the mechanism by which the delta-domain deletion enhances transforming activity. Consistent with this idea, we have generated a panel of point mutants that show markedly enhanced transforming activity, despite the fact that they do not perturb the ability of JNK to either dock with or phosphorylate c-Jun in vitro or in vivo. The fact that these mutants cluster in a small region suggests the existence of an additional regulator of Jun function whose activity is disrupted by mutations in this region.

Amino Acid Sequence↗
PubMed1995

Effects of c-Jun and a negative dominant mutation of c-Jun on differentiation and gene expression in lens epithelial cells.

We have used a retroviral vector (RCAS) to overexpress wild-type chicken c-Jun or a deletion mutant of chicken c-Jun (Jun delta 7) lacking the DNA binding region to investigate the possible role of c-Jun in lens epithelial cell proliferation and differentiation. Both constructs were efficiently expressed in primary cultures of embryonic chicken lens epithelial cells. Overexpression of c-Jun increased the rate of cell proliferation and greatly delayed the appearance of "lentoid bodies," structures which contain differentiated cells expressing fiber cell markers. Excess c-Jun expression also significantly decreased the level of beta A3/A1-crystallin mRNA, without affecting alpha A-crystallin mRNA. In contrast, the mutated protein, Jun delta 7, had no effect on proliferation or differentiation but markedly increased the level of alpha A-crystallin mRNA in proliferating cell cultures. These results suggest that c-Jun or Jun-related proteins may be negative regulators of alpha A- and beta A3/A1-crystallin genes in proliferating lens cells.

Amino Acid Sequence↗
PubMed1991

Constitutive expression of c-jun and jun-B in cell lines infected with human T-lymphotropic virus types I and II.

To better understand the transcriptional regulation of human T-lymphotropic viruses, expression of the nuclear proto-oncogenes, jun-B and c-jun were examined in cell lines infected with HTLV-I/II. Constitutive high levels of jun-B and c-jun expression were observed in HTLV-I (MT-2, Hut-102, IR, FS, SP) and HTLV-II infected cell lines (Mo-T, PAN). In contrast, the uninfected cell lines (Jurkat, Hut-78) expressed only basal levels of jun. This expression of jun was not dependent upon IL-2, as both IL-2 dependent (IR, FS, SP, and Pan) and IL-2 independent (MT-2, Hut-102, Mo-T) cell lines constitutively expressed transcripts for jun-B and c-jun. These data demonstrate that deregulated expression of nuclear protooncogenes such as jun may lead to cellular proliferation and the protein products of these nuclear oncogenes may potentially serve as transcriptional activators of HTLV-LTR by complexing with other nuclear proteins.

Blotting, Northern↗
PubMed2005

Heterodimer formation between c-Jun and Jun B proteins mediated by Epstein Barr virus encoded latent membrane protein 1.

Epstein-Barr virus (EBV) encoded latent membrane protein 1 (LMP1) may trigger the transcription factor AP-1 including c-Jun and c-fos. In this report, using a Tet-on LMP1 HNE2 cell line which is a dual-stable LMP1 integrated nasopharyngeal carcinoma (NPC) cell line and the expression of LMP1 in which could be regulated by the Tet-on system, we show that Jun B can efficiently form a new heterodimeric complex with the c-Jun protein under the regulation of LMP1, phosphorylation of c-Jun (ser 63, ser 73) and Jun B is involved in the process of the new heterodimeric formation. We also find that this heterodimeric form can bind to the AP-1 consensus sequence. Transfection studies suggest that JNK interaction protein (JIP) could inhibit the heterodimer formation of c-Jun and Jun B through blocking the AP-1 signaling pathway triggered by LMP1. The interaction and function between c-Jun protein and Jun B protein increase the repertoire of possible regulatory complexes by LMP1 that could play an important role in the regulation of transcription of specific cellular genes in the process of genesis of nasopharyngeal carcinoma.

Blotting, Western↗
PubMed2004

HMG-I/Y is a c-Jun/activator protein-1 target gene and is necessary for c-Jun-induced anchorage-independent growth in Rat1a cells.

The transcription complex activator protein-1 (AP-1) plays a role in a diverse number of cellular processes including proliferation, differentiation, and apoptosis. To identify AP-1-responsive target genes, we used a doxycycline-inducible c-Jun system in Rat1a cells. The HMG-I/Y chromatin binding protein was found to be up-regulated by c-Jun. Following induction of c-Jun expression, Rat1a cells under nonadherent growth conditions have sustained HMG-I/Y mRNA expression and 2-fold higher protein than uninduced cells. HMG-I/Y promoter reporter assays show that HMG-I/Y promoter activity increases in the presence of c-Jun expression, and gel mobility shift assays demonstrate that induced c-Jun binds to an AP-1 consensus site at position -1,091 in the HMG-I/Y promoter. Suppression of HMG-I/Y expression by its antisense sequence significantly reduces the ability of c-Jun-overexpressing Rat1a cells to grow in an anchorage-independent fashion. HMG-I/Y transforms Rat1a cells (although the colonies are smaller than that observed for the cells overexpressing c-Jun). Taken together, these results suggest that HMG-I/Y is a direct transcriptional target of c-Jun necessary for c-Jun-induced anchorage-independent growth in Rat1a cells.

Animals↗
PubMed1995

Stress-activated protein kinases bind directly to the delta domain of c-Jun in resting cells: implications for repression of c-Jun function.

The transactivating function of the c-Jun proto-oncogene component of the AP-1 transcription factor is acutely regulated by a wide variety of cellular signals via modulation of phosphorylation of two serines (63 and 73). The viral oncoprotein, v-Jun, while containing homologous serines, is not phosphorylated in cells. A novel family of stress-activated protein kinases (SAPKs), also termed Jun N-terminal domain kinases (JNKs), are responsible for mediating S63/73 phosphorylation in response to a variety of cellular stimuli including tumor necrosis factor-alpha, heat stress and u.v. light. The p54 alpha 1, alpha 2, p54 beta and p46 beta SAPKs are shown to bind directly to c-Jun but not to v-Jun, with an absolute requirement for c-Jun amino acids 31-47, a region deleted in v-Jun. Inactive SAPKs tightly bind c-Jun in resting cells and may be a manifestation of the 'delta' inhibitor, a previously described repressor of c-Jun function.

Calcium-Calmodulin-Dependent Protein Kinases↗
PubMed1995

Stimulation of c-Jun activity by CBP: c-Jun residues Ser63/73 are required for CBP induced stimulation in vivo and CBP binding in vitro.

The CBP protein mediates PKA induced transcription by binding to the PKA phosphorylated activation domain of CREB. Here we show that CBP also stimulates the activity of both c-Jun and v-Jun in vivo. The CREB binding domain of CBP is sufficient to contact to c-Jun in vitro. When this domain of CBP is linked to the activation domain of VP16 and expressed in vivo it stimulates c-Jun dependent transcription. Deletion analysis of c-Jun indicate that the CBP binding site is within the N-terminal activation domain. Loss of binding to CBP in vitro correlates with severely reduced transactivation capacity in vivo. Mutation of Ser63/73 in c-Jun, or the corresponding position in v-Jun (Ser36/46) leads to reduced binding to CBP in vitro and abolishes augmentation of transcription in vivo. These data are consistent with a mechanism by which CBP acts as a co-activator protein for Jun dependent transcription by interacting with the Jun N-terminal activation domain.

Binding Sites↗
PubMed1993

Long-term induction of c-jun mRNA and Jun protein in rabbit retinal ganglion cells following axotomy or colchicine treatment.

The expression of the c-jun, c-fos, and NGFI-A genes was studied in the rabbit retina after optic nerve crush (ONC) or an intravitreal injection of colchicine. By Northern blotting, the basal expression of c-fos and NGFI-A mRNAs were undetectable, whereas c-jun mRNA showed a low basal expression in sham-operated control retinas. Very few or no Jun- or Fos-immunoreactive nuclei were seen in control retinas. From 1 to 95 days after ONC a marked induction of JUN- but not FOS-immunoreactive neurons was seen in the ganglion cell layer peaking at 3 and 7 days. Jun-positive neurons also accumulated immunoreactive phosphorylated neurofilaments, indicating that they were ganglion cells. Northern blots demonstrated that retinal levels of c-jun mRNA, but not of c-fos or NGFI-A mRNAs, were increased 3 and 7 days after ONC. An intravitreal injection of colchicine also induced Jun-immunoreactivity within 24 hr in most of the neurons in the ganglion cell layer, but not in the inner nuclear and outer nuclear layers. The results indicate that axonal damage induces a specific pattern of IEG expression including a long-term induction of the c-jun gene in CNS neurons.

Animals↗