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1.
Mol Cell Biol ; 37(11)2017 06 01.
Article in English | MEDLINE | ID: mdl-28320871

ABSTRACT

The layers of the epithelial syncytium, i.e., syncytiotrophoblasts, differentiate from chorionic trophoblasts via cell fusion and separate maternal and fetal circulations in hemochorial placentas. L-type amino acid transporter 1 (LAT1) and its covalently linked ancillary subunit 4F2hc are colocalized on both maternal and fetal surfaces of syncytiotrophoblasts, implying their roles in amino acid transfer through the placental barrier. In this study, LAT1 knockout, in addition, revealed a novel role of LAT1 in syncytiotrophoblast development. LAT1 at midgestation was selectively expressed in trophoblastic lineages in the placenta, exclusively as a LAT1-4F2hc heterodimer. In LAT1 homozygous knockout mice, chorionic trophoblasts remained largely mononucleated, and the layers of syncytiotrophoblasts were almost completely absent. The amount of 4F2hc protein, which possesses a fusogenic function in trophoblastic cells, as well as in virus-infected cells, was drastically reduced by LAT1 knockout, with less affecting the mRNA level. Knockdown of LAT1 in trophoblastic BeWo cells also reduced 4F2hc protein and suppressed forskolin-induced cell fusion. These results demonstrate a novel fundamental role of LAT1 to support the protein expression of 4F2hc via a chaperone-like function in chorionic trophoblasts and to promote syncytiotrophoblast formation by contributing to cell fusion in the developing placenta.


Subject(s)
Fusion Regulatory Protein 1, Heavy Chain/metabolism , Large Neutral Amino Acid-Transporter 1/metabolism , Trophoblasts/metabolism , Animals , Apoptosis/drug effects , Cell Fusion , Cell Line , Cell Lineage , Cell Proliferation/drug effects , Colforsin/pharmacology , Crosses, Genetic , Embryo Loss/pathology , Female , Gene Deletion , Gene Knockdown Techniques , Gene Targeting , Homozygote , Humans , Male , Mice, Inbred C57BL , Mice, Knockout , Placenta/abnormalities , Placenta/drug effects , Pregnancy , Trophoblasts/cytology , Trophoblasts/drug effects
2.
Proc Natl Acad Sci U S A ; 113(3): 775-80, 2016 Jan 19.
Article in English | MEDLINE | ID: mdl-26739563

ABSTRACT

Heterodimeric amino acid transporters play crucial roles in epithelial transport, as well as in cellular nutrition. Among them, the heterodimer of a membrane protein b(0,+)AT/SLC7A9 and its auxiliary subunit rBAT/SLC3A1 is responsible for cystine reabsorption in renal proximal tubules. The mutations in either subunit cause cystinuria, an inherited amino aciduria with impaired renal reabsorption of cystine and dibasic amino acids. However, an unsolved paradox is that rBAT is highly expressed in the S3 segment, the late proximal tubules, whereas b(0,+)AT expression is highest in the S1 segment, the early proximal tubules, so that the presence of an unknown partner of rBAT in the S3 segment has been proposed. In this study, by means of coimmunoprecipitation followed by mass spectrometry, we have found that a membrane protein AGT1/SLC7A13 is the second partner of rBAT. AGT1 is localized in the apical membrane of the S3 segment, where it forms a heterodimer with rBAT. Depletion of rBAT in mice eliminates the expression of AGT1 in the renal apical membrane. We have reconstituted the purified AGT1-rBAT heterodimer into proteoliposomes and showed that AGT1 transports cystine, aspartate, and glutamate. In the apical membrane of the S3 segment, AGT1 is suggested to locate itself in close proximity to sodium-dependent acidic amino acid transporter EAAC1 for efficient functional coupling. EAAC1 is proposed to take up aspartate and glutamate released into luminal fluid by AGT1 due to its countertransport so that preventing the urinary loss of aspartate and glutamate. Taken all together, AGT1 is the long-postulated second cystine transporter in the S3 segment of proximal tubules and a possible candidate to be involved in isolated cystinuria.


Subject(s)
Amino Acid Transport Systems, Basic/metabolism , Amino Acid Transport Systems, Neutral/metabolism , Amino Acid Transport Systems/metabolism , Cell Membrane/metabolism , Cystinuria/metabolism , Kidney Tubules, Proximal/metabolism , Amino Acid Sequence , Amino Acid Transport Systems/chemistry , Amino Acid Transport Systems/genetics , Animals , Antibodies/metabolism , Blotting, Western , Excitatory Amino Acid Transporter 3/metabolism , Female , HEK293 Cells , Humans , Immunohistochemistry , In Situ Hybridization , Kidney/metabolism , Male , Mice, Inbred C57BL , Molecular Sequence Data , Protein Binding , Protein Multimerization , Proteolipids/metabolism , RNA, Messenger/genetics , RNA, Messenger/metabolism , Response Elements/genetics
3.
J Neurochem ; 128(2): 246-55, 2014 Jan.
Article in English | MEDLINE | ID: mdl-24117996

ABSTRACT

Cholinergic neurons in the CNS are involved in synaptic plasticity and cognition. Both muscarinic and nicotinic acetylcholine receptors (nAChRs) influence plasticity and cognitive function. The mechanism underlying nAChR-induced plasticity, however, has remained elusive. Here, we demonstrate morphological changes in dendritic spines following activation of α4ß2* nAChRs, which are expressed on glutamatergic pre-synaptic termini of cultured hippocampal neurons. Exposure of the neurons to nicotine resulted in a lateral enlargement of spine heads. This was abolished by dihydro-ß-erythroidine, an antagonist of α4ß2* nAChRs, but not by α-bungarotoxin, an antagonist of α7 nAChRs. Tetanus toxin or a mixture of 2-amino-5-phosphonovaleric acid and 6-cyano-7-nitroquinoxaline-2,3-dione, antagonists of NMDA- and AMPA-type glutamate receptors, blocked the nicotine-induced spine remodeling. In addition, nicotine exerted full spine-enlarging response in the post-synaptic neuron whose ß2 nAChR expression was knocked down. Finally, pre-treatment with nicotine enhanced the Ca(2+)-response of the neurons to glutamate. These data suggest that nicotine influences the activity of glutamatergic neurotransmission through the activation of pre-synaptic α4ß2 nAChRs, resulting in the modulation of spinal architecture and responsiveness. The present findings may represent one of the cellular mechanisms underlying cholinergic tuning of brain function. Activation of nicotinic acetylcholine receptors (nAChRs) in brain influences plasticity and cognition. Here, activation of α4ß2* nAChRs, which are expressed on glutamatergic presynaptic termini, results in the enlargement of dendritic spines through the modulation of the glutamatergic neurotransmission. The remodeled spinal architecture might be responsible for the change in responsiveness of neural circuitry, leading to cholinergic tuning of brain function.


Subject(s)
Dendritic Spines/drug effects , Hippocampus/cytology , Neurons/drug effects , Nicotine/pharmacology , Nicotinic Agonists/pharmacology , Receptors, Nicotinic/metabolism , Animals , Cells, Cultured , Dendritic Spines/ultrastructure , Glutamates/metabolism , Neurons/ultrastructure , Rats , Rats, Sprague-Dawley
4.
PLoS One ; 7(8): e43050, 2012.
Article in English | MEDLINE | ID: mdl-22916205

ABSTRACT

The NHERF (Na(+)/H(+) exchanger regulatory factor) family has been proposed to play a key role in regulating transmembrane protein localization and retention at the plasma membrane. Due to the high homology between the family members, potential functional compensations have been a concern in sorting out the function of individual NHERF numbers. Here, we studied C. elegans NRFL-1 (C01F6.6) (nherf-like protein 1), the sole C. elegans orthologue of the NHERF family, which makes worm a model with low genetic redundancy of NHERF homologues. Integrating bioinformatic knowledge of C. elegans proteins into yeast two-hybrid scheme, we identified NRFL-1 as an interactor of AAT-6, a member of the C. elegans AAT (amino acid transporter) family. A combination of GST pull-down assay, localization study, and co-immunoprecipitation confirmed the binding and characterized the PDZ interaction. AAT-6 localizes to the luminal membrane even in the absence of NRFL-1 when the worm is up to four-day old. A fluorescence recovery after photobleaching (FRAP) analysis suggested that NRFL-1 immobilizes AAT-6 at the luminal membrane. When the nrfl-1 deficient worm is six-day or older, in contrast, the membranous localization of AAT-6 is not observed, whereas AAT-6 tightly localizes to the membrane in worms with NRFL-1. Sorting out the in vivo functions of the C. elegans NHERF protein, we found that NRFL-1, a PDZ-interactor of AAT-6, is responsible for the immobilization and the age-dependent maintenance of AAT-6 on the intestinal luminal membrane.


Subject(s)
Amino Acid Transport Systems/metabolism , Caenorhabditis elegans Proteins/metabolism , Caenorhabditis elegans/metabolism , Phosphoproteins/metabolism , Sodium-Hydrogen Exchangers/metabolism , Amino Acid Transport Systems/genetics , Animals , Caenorhabditis elegans Proteins/genetics , Intestinal Mucosa/metabolism , Phosphoproteins/genetics , Phosphorylation , Protein Binding , Sodium-Hydrogen Exchangers/genetics , Two-Hybrid System Techniques
5.
Brain Res ; 1306: 1-7, 2010 Jan 08.
Article in English | MEDLINE | ID: mdl-19833109

ABSTRACT

Anti-oxidative stress responses are crucial for the survival of nerve-injured motor neurons. Herein, we examined changes in expression of glutathione reductase (GSHr), thioredoxins (TRX1 and TRX2), and thioredoxin reductases (TRXr1 and TRXr2), important constituents of anti-oxidative pathways, following rat hypoglossal nerve transection. RT-PCR and in situ hybridization demonstrated that GSHr, TRX1, and TRXr1 mRNAs were significantly up-regulated during the first few weeks in nerve-injured motor neurons, while TRX2 and TRXr2 mRNAs were unchanged throughout 8 weeks after nerve transection. The up-regulation of GSH, GSHr, TRX1, and TRXr1 proteins in injured neurons was confirmed by immunohistochemical analysis. Western blotting also demonstrated up-regulation of GSHr, TRX1, and TRXr1 in injured neurons. These data suggest that the two major redox systems, GSH/GSHr and TRX1/TRXr1, are simultaneously activated in injured neurons, and likely provide protection of injured neurons against oxidative stress.


Subject(s)
Hypoglossal Nerve Injuries , Hypoglossal Nerve/physiopathology , Motor Neurons/physiology , Oxidative Stress/physiology , Animals , Glutathione/metabolism , Glutathione Reductase/metabolism , Hypoglossal Nerve/enzymology , Male , Motor Neurons/enzymology , RNA, Messenger/metabolism , Rats , Rats, Wistar , Signal Transduction , Thioredoxin Reductase 1/metabolism , Thioredoxin Reductase 2/metabolism , Thioredoxins/metabolism , Time Factors
6.
J Biol Chem ; 283(11): 6988-96, 2008 Mar 14.
Article in English | MEDLINE | ID: mdl-18192274

ABSTRACT

Nerve injury requires the expression of large ensembles of genes. The key molecular mechanism for this gene transcription regulation in injured neurons is poorly understood. Among many nerve injury-inducible genes, the gene encoding damage-induced neuronal endopeptidase (DINE) showed most marked expression response to various kinds of nerve injuries in central and peripheral nervous system neurons. This unique feature led us to examine the promoter region of the DINE gene and clarify both the injury-responsive element within the promoter and its related transcriptional machinery. This study showed that DINE promoter was activated by leukemia inhibitory factor and nerve growth factor withdrawal, which were pivotal for the up-regulation of DINE mRNA after nerve injury. The injury-inducible transcription factors such as activating transcription factor 3 (ATF3), c-Jun, and STAT3, which were located at the downstream of leukemia inhibitory factor and nerve growth factor withdrawal, seemed to be involved in the activation of the DINE promoter. Surprisingly, these transcription factors did not bind to the DINE promoter directly. Instead, the general transcription factor, Sp1, bound to a GC box within the promoter. ATF3, c-Jun, and STAT3 interacted with Sp1 and are associated with the GC box region of the DINE gene in injured neurons. These findings suggested that Sp1 recruit ATF3, c-Jun, and STAT3 to obtain the requisite synergistic effect. Of these transcription factors, ATF3 may be the most critical, because ATF3 is specifically expressed after nerve injury.


Subject(s)
Activating Transcription Factor 3/physiology , Gene Expression Regulation , Metalloendopeptidases/physiology , Neurons/metabolism , Neurons/pathology , Proto-Oncogene Proteins c-jun/physiology , STAT3 Transcription Factor/physiology , Sp1 Transcription Factor/metabolism , Animals , Cell Line, Tumor , Humans , Male , Mice , Mice, Inbred C57BL , Rats , Rats, Wistar
7.
Neurobiol Dis ; 29(2): 221-31, 2008 Feb.
Article in English | MEDLINE | ID: mdl-17964175

ABSTRACT

The Golgi apparatus processes intracellular proteins, but undergoes disassembly and fragmentation during apoptosis in several neurodegenerative disorders such as amyotrophic lateral sclerosis and Alzheimer's disease. It is well known that other cytoplasmic organelles play important roles in cell death pathways. Thus, we hypothesized that Golgi fragmentation might participate in transduction of cell death signals. Here, we found that Golgi fragmentation and dispersal precede neuronal cell death triggered by excitotoxins, oxidative/nitrosative insults, or ER stress. Pharmacological intervention or overexpression of the C-terminal fragment of Grasp65, a Golgi-associated protein, inhibits fragmentation and decreases or delays neuronal cell death. Inhibition of mitochondrial or ER cell death pathways also decreases Golgi fragmentation, indicating crosstalk between organelles and suggesting that the Golgi may be a common downstream-effector of cell death. Taken together, these findings implicate the Golgi as a sensor of stress signals in cell death pathways.


Subject(s)
Golgi Apparatus/pathology , Nerve Degeneration/pathology , Neurons/pathology , Signal Transduction/physiology , Analysis of Variance , Animals , Apoptosis/drug effects , Apoptosis/physiology , Cells, Cultured , Cerebral Cortex/pathology , Cysteine/analogs & derivatives , Cysteine/pharmacology , Dose-Response Relationship, Drug , Embryo, Mammalian , Excitatory Amino Acid Agonists/pharmacology , Golgi Apparatus/drug effects , Luminescent Proteins/biosynthesis , Mitochondria/drug effects , Mitochondria/metabolism , N-Methylaspartate/pharmacology , Nerve Degeneration/chemically induced , Nerve Degeneration/genetics , Neurons/drug effects , Nitric Oxide Donors/pharmacology , Rats , S-Nitrosothiols/pharmacology , Signal Transduction/drug effects , Time Factors , Transfection/methods , Tubulin/metabolism
8.
J Comp Neurol ; 488(1): 1-10, 2005 Jul 18.
Article in English | MEDLINE | ID: mdl-15912498

ABSTRACT

Autosomal dominant optic atrophy (DOA) is the most common form of hereditary optic neuropathy. DOA presents in the first decade of life and manifests as progressive vision loss. In DOA retinal ganglion cells and the optic nerve degenerate by an unknown mechanism. The gene mutated in DOA, Optic Atrophy Type 1 (OPA1), encodes a dynamin-related GTPase implicated in mitochondrial fusion and maintenance of the mitochondrial network and genome. Here, we determine which cell types in the normal retina and the optic nerve express OPA1. In the normal rat retina, OPA1 is expressed in the ganglion cell layer as well as in the outer plexiform layer, the inner nuclear layer, and the inner plexiform layer. In the ganglion cell layer, OPA1 is expressed predominantly in retinal ganglion cells. By contrast, OPA1 protein is low or undetectable in astrocytes and oligodendrocytes of the optic nerve. Additionally, OPA1 protein is present in axonal mitochondria. Last, OPA1 expression is present in mitochondria of processes and cell bodies of purified retinal ganglion cells and of the RGC-5 cell line. Thus, OPA1 is predominantly expressed in retinal ganglion cells of the normal rat retina and axons of the optic nerve. These findings may explain the selective vulnerability of retinal ganglion cells to OPA1 loss of function.


Subject(s)
Axons/metabolism , GTP Phosphohydrolases/metabolism , Optic Nerve/metabolism , Retina/metabolism , Retinal Ganglion Cells/metabolism , Animals , Astrocytes/metabolism , Male , Oligodendroglia/metabolism , Optic Nerve/cytology , Rats , Rats, Sprague-Dawley , Reference Values , Retina/cytology
9.
Neurosci Res ; 48(3): 305-14, 2004 Mar.
Article in English | MEDLINE | ID: mdl-15154676

ABSTRACT

This study was designed to evaluate whether the vesicular acetylcholine transporter (VAChT), which packages acetylcholine into synaptic vesicles, can be used as a marker for regenerating motor axon terminal. We examined motor axon regeneration in the tongue after hypoglossal nerve axotomy, using an anterograde tracer biotin-dextran (BD), retrograde tracer Fluoro-Gold (FG), electron microscopic (EM) observation, and VAChT immunocytochemistry. BD study demonstrated that outgrowth of thin regenerating axons into the frontal area of the tongue was firstly observed at 14 post-operative days, and presynaptic formation of neuromuscular junction (NMJ) was observed from 21 post-operative days. Under electron microscopic observation, reconstruction of new NMJs was observed within the interval between 21 and 28 days. VAChT-immunoreactive nerve terminals disappeared by 3 days after axotomy, slightly appeared at 14 post-operative days, and thereafter gradually increased in number from 21 to 28 post-operative days. The re-expression of VAChT positive presynaptic terminal was almost the same as those obtained in BD, FG and EM studies. Regenerating axons tip in the crush model of the hypoglossal nerve exhibited prominent VAChT immunoreactivity in growing tip of regenerating axons. These indicate that VAChT is an excellent morphological indicator for regenerating nerve terminals of motor neurons.


Subject(s)
Axons/metabolism , Biotin/analogs & derivatives , Carrier Proteins/metabolism , Membrane Transport Proteins , Muscles/innervation , Nerve Regeneration/physiology , Vesicular Transport Proteins , Animals , Axotomy/methods , Biomarkers/analysis , Biotin/metabolism , Bungarotoxins/metabolism , Dextrans/metabolism , Fluorescent Dyes/metabolism , Functional Laterality , Hypoglossal Nerve Injuries , Immunohistochemistry/methods , Male , Microscopy, Electron , Muscles/metabolism , Nerve Crush/methods , Neuromuscular Junction/ultrastructure , Rats , Rats, Wistar , Stilbamidines/metabolism , Time Factors , Tongue/ultrastructure , Vesicular Acetylcholine Transport Proteins
10.
Brain Res Mol Brain Res ; 115(2): 147-56, 2003 Jul 23.
Article in English | MEDLINE | ID: mdl-12877985

ABSTRACT

It has been demonstrated that some of immediate early genes such as c-Jun are induced immediately and transiently following focal cerebral ischemia. Here we newly characterize the activating transcription factor (ATF)-3 as a focal ischemia associated immediate early gene. Using in situ hybridization and immunohistochemistry, we compared the expression profile of ATF-3 with those of ATF-2 and c-Jun after middle cerebral artery (MCA) occlusion. Focal cerebral ischemia induced two temporal and spatial patterns of ATF-3 expression. Early and transient induction of ATF-3 mRNA was observed in the core and margins of the cortex immediately after MCA occlusion. Late-onset and prolonged expression of ATF-3 mRNA and its protein were specifically identified in the peri-infarct cortex and thalamus where neurons survive at least 1 month. The expression profiles of ATF-3 and c-Jun were virtually similar, but c-Jun expression was also observed in other regions of the brain in control rats. Expression of ATF-2 was ubiquitously seen in neuronal cells throughout the brain in normal rats, but was suppressed in ischemic regions. Double immunohistochemical labeling revealed concurrent expression of ATF-3 and phospho-c-Jun in neurons. We conclude that the transcription factor ATF-3 is a suitable marker of neurons subjected to ischemic insult directly and indirectly, and that cooperative works of ATF-3 and c-Jun may be crucial triggers of various transcriptional responses to the ischemic insult.


Subject(s)
Cerebral Infarction/pathology , Neurons/metabolism , Transcription Factors/metabolism , Activating Transcription Factor 2 , Activating Transcription Factor 3 , Animals , Brain/metabolism , Brain/pathology , Cerebral Infarction/etiology , Cyclic AMP Response Element-Binding Protein/genetics , Cyclic AMP Response Element-Binding Protein/metabolism , Disease Models, Animal , Gene Expression Regulation/physiology , Glial Fibrillary Acidic Protein/metabolism , Immunohistochemistry , In Situ Hybridization , In Situ Nick-End Labeling , Infarction, Middle Cerebral Artery/complications , Male , Nerve Tissue Proteins/metabolism , Proto-Oncogene Proteins c-jun/genetics , Proto-Oncogene Proteins c-jun/metabolism , RNA, Messenger/biosynthesis , Rats , Rats, Sprague-Dawley , Reverse Transcriptase Polymerase Chain Reaction/methods , Time Factors , Transcription Factors/genetics
11.
J Neurochem ; 86(4): 1042-50, 2003 Aug.
Article in English | MEDLINE | ID: mdl-12887701

ABSTRACT

The rat collapsin response mediator protein-2 (CRMP-2) is a member of CRMP family (CRMP-1-5). The functional consequence of CRMP-2 during embryonic development, particularly in neurite elongation, is relatively understood; however, the role in nerve regeneration is unclear. Here we examined the role of CRMP-2 during nerve regeneration using rat hypoglossal nerve injury model. Among the members, CRMP-1, CRMP-2, CRMP-5 mRNA expressions increased after nerve injury, whereas CRMP-3 and CRMP-4 mRNA did not show any significant change. In the N1E-115 cells, CRMP-2 has the most potent neurite elongation activity among the CRMP family members. In dorsal root ganglion (DRG) organ culture, CRMP-2 overexpression by adenoviral vector demonstrated substantial neurite elongation. On the other hand, CRMP-2 (DeltaC381), which acts as a dominant negative form of CRMP-2, inhibited neurite formation. Collectively, it would be plausible that CRMP-2 has potent nerve regeneration activity after nerve injury. We therefore examined whether CRMP-2 overexpression in the injured hypoglossal motor neurons accelerates nerve regeneration. A retrograde-tracer, Fluoro-Gold (FG), was used to evaluate the number of reprojecting motor neurons after nerve injury. CRMP-2-overexpressing motor neurons demonstrated the accelerated reprojection. The present study suggests that CRMP-2 has potent neurite elongation activity in nerve regeneration in vivo.


Subject(s)
Axons/physiology , Hypoglossal Nerve/physiology , Motor Neurons/metabolism , Nerve Regeneration/physiology , Nerve Tissue Proteins/metabolism , Animals , Axonal Transport/physiology , Axons/drug effects , Cells, Cultured , Disease Models, Animal , Ganglia, Spinal/cytology , Hypoglossal Nerve/cytology , Hypoglossal Nerve/drug effects , Intercellular Signaling Peptides and Proteins , Male , Motor Neurons/cytology , Motor Neurons/drug effects , Nerve Regeneration/drug effects , Nerve Tissue Proteins/genetics , Nerve Tissue Proteins/pharmacology , Neurites/drug effects , Neurites/physiology , Phosphoproteins/genetics , Phosphoproteins/metabolism , RNA, Messenger/metabolism , Rats , Rats, Wistar
12.
J Neurosci ; 23(12): 5187-96, 2003 Jun 15.
Article in English | MEDLINE | ID: mdl-12832543

ABSTRACT

Activating transcription factor 3 (ATF3) is induced and functions both as a cellular response to stress and to stimulate proliferation in multiple tissues. However, in the nervous system ATF3 is expressed only in injured neurons. Here we reveal a function of ATF3 in neurons under death stress. Overexpression of ATF3 by adenovirus inhibits the mitogen-activated kinase kinase kinase 1 (MEKK1)-c-Jun N-Terminal Kinase (JNK)-induced apoptosis and induces neurite elongation via Akt activation in PC12 cells and superior nerve ganglion neurons. A DNA microarray study reveals that ATF3 expression and JNK activation induce expression of the heat shock protein 27 (Hsp27). Immunoprecipitation analysis and promoter assay for Hsp27 expression suggest that both ATF3 and c-Jun are necessary for transcriptional activation of Hsp27. Hsp27 expression significantly inhibits JNK-induced apoptosis as well as Akt activation in PC12 cells and superior cervical ganglion neurons. We conclude that the combination of ATF3 and c-Jun induces the anti-apoptotic factor Hsp27, which directly or indirectly activates Akt, and thereby possibly inhibits apoptosis and induces nerve elongation. Our results suggest that ATF3- and c-Jun-induced Hsp27 expression is a novel survival response in neurons under death stress such as nerve injury.


Subject(s)
Heat-Shock Proteins , Mitogen-Activated Protein Kinases/metabolism , Neoplasm Proteins/biosynthesis , Neurons/metabolism , Protein Serine-Threonine Kinases , Proto-Oncogene Proteins/metabolism , Transcription Factors/biosynthesis , Activating Transcription Factor 2 , Activating Transcription Factor 3 , Adenoviridae/genetics , Animals , Brain/cytology , Brain/metabolism , Cell Death/drug effects , Cell Death/physiology , Cell Survival/drug effects , Cell Survival/physiology , Cells, Cultured , Cyclic AMP Response Element-Binding Protein/biosynthesis , Cyclic AMP Response Element-Binding Protein/genetics , Enzyme Activation/drug effects , Enzyme Activation/physiology , Gene Expression Regulation , HSP27 Heat-Shock Proteins , Hypoglossal Nerve/cytology , Hypoglossal Nerve/physiology , JNK Mitogen-Activated Protein Kinases , Motor Neurons/cytology , Motor Neurons/metabolism , Neoplasm Proteins/genetics , Neoplasm Proteins/pharmacology , Nerve Growth Factor/pharmacology , Neurites/drug effects , Neurites/physiology , Neurons/cytology , Neurons/drug effects , PC12 Cells , Promoter Regions, Genetic , Proto-Oncogene Proteins c-akt , RNA, Messenger/biosynthesis , Rats , Rats, Wistar , Superior Cervical Ganglion/cytology , Transcription Factors/genetics , Transcription Factors/pharmacology
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