scholarly journals Immunohistochemical Localization of Translationally Controlled Tumor Protein in Axon Terminals of Mouse Hippocampal Neurons

2017 ◽  
Vol 26 (2) ◽  
pp. 82-89 ◽  
Author(s):  
Seong-Yeon Bae ◽  
Vadim Sheverdin ◽  
Jeehye Maeng ◽  
In Kyoon Lyoo ◽  
Pyung-Lim Han ◽  
...  
Keyword(s):  
Hippocampal Neurons ◽  
Immunohistochemical Localization ◽  
Translationally Controlled Tumor Protein ◽  
Axon Terminals

Immunohistochemical localization of lysosomal cysteine protease cathepsins B and L in monkey hippocampal neurons after transient ischemia

1999 ◽  
Vol 19 (3) ◽  
pp. 302-310
Author(s):  
Yukihiko Kohda ◽  
Katsuhiro Tsuchiya ◽  
Junkoh Yamashita ◽  
Masaki Yoshida ◽  
Takashi Ueno ◽  
...  
Keyword(s):  
Cysteine Protease ◽  
Hippocampal Neurons ◽  
Immunohistochemical Localization ◽  
Transient Ischemia ◽  
Lysosomal Cysteine Protease

scholarly journals Adaptor protein APPL1 links neuronal activity to chromatin remodeling in cultured hippocampal neurons

2020 ◽  
Author(s):  
Yu Wu ◽  
Xinyou Lv ◽  
Haiting Wang ◽  
Kai Qian ◽  
Jinjun Ding ◽  
...  
Keyword(s):  
Chromatin Remodeling ◽  
Neuronal Activity ◽  
Hippocampal Neurons ◽  
Late Phase ◽  
Adaptor Protein ◽  
Long Term Potentiation ◽  
Nuclear Accumulation ◽  
Transcriptional Responses ◽  
Axon Terminals ◽  
Term Potentiation

Abstract Local signaling events at synapses or axon terminals are communicated to the nucleus to elicit transcriptional responses, and thereby translate information about the external environment into internal neuronal representations. This retrograde signaling is critical to dendritic growth, synapse development, and neuronal plasticity. Here, we demonstrate that neuronal activity induces retrograde translocation and nuclear accumulation of endosomal adaptor APPL1. Disrupting the interaction of APPL1 with Importin α1 abolishes nuclear accumulation of APPL1, which in turn decreases the levels of histone acetylation. We further demonstrate that retrograde translocation of APPL1 is required for the regulation of gene transcription and then maintenance of hippocampal late-phase long-term potentiation. Thus, these results illustrate an APPL1-mediated pathway that contributes to the modulation of synaptic plasticity via coupling neuronal activity with chromatin remodeling.

scholarly journals Decrease of glutamate decarboxylase (GAD)-immunoreactive nerve terminals in the substantia nigra after kainic acid lesion of the striatum.

1981 ◽  
Vol 29 (8) ◽  
pp. 977-980 ◽  
Author(s):  
W H Oertel ◽  
D E Schmechel ◽  
M J Brownstein ◽  
M L Tappaz ◽  
D H Ransom ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Substantia Nigra ◽  
Kainic Acid ◽  
Glutamate Decarboxylase ◽  
Marked Reduction ◽  
Immunohistochemical Localization ◽  
Nerve Terminals ◽  
Immunohistochemical Examination ◽  
Axon Terminals ◽  
Gad Activity

Antiserum sheep 3 against rat brain glutamate decarboxylase (GAD) was employed for the immunohistochemical localization of GAD-immunoreactive nerve terminals in the substantia nigra (SN). To test whether the antiserum specifically localized GAD-containing axon terminals, the effect of kainic acid-induced striatal lesions on the reactive nerve endings in the SN was investigated. Seven days after the injection of 1 microgram kainic acid into the striatum, a 65% decrease in GAD-enzyme activity occurred in the ipsilateral SN. On immunohistochemical examination there was correspondingly a marked reduction of GAD-positive terminals. The parallel decrease in biochemical and immunohistochemical GAD activity indicates that antiserum sheep 3 can be used as a specific immunohistochemical probed for GAD-containing elements.

scholarly journals Bassoon, a Novel Zinc-finger CAG/Glutamine-repeat Protein Selectively Localized at the Active Zone of Presynaptic Nerve Terminals

1998 ◽  
Vol 142 (2) ◽  
pp. 499-509 ◽  
Author(s):  
Susannetom Dieck ◽  
Lydia Sanmartí-Vila ◽  
Kristina Langnaese ◽  
Karin Richter ◽  
Stefan Kindler ◽  
...  
Keyword(s):  
Active Zone ◽  
Hippocampal Neurons ◽  
Late Onset ◽  
Coiled Coil ◽  
Ultrastructural Level ◽  
Nerve Terminals ◽  
Molecular Architecture ◽  
Coding Region ◽  
Axon Terminals ◽  
Presynaptic Nerve Terminals

The molecular architecture of the cytomatrix of presynaptic nerve terminals is poorly understood. Here we show that Bassoon, a novel protein of >400,000 Mr, is a new component of the presynaptic cytoskeleton. The murine bassoon gene maps to chromosome 9F. A comparison with the corresponding rat cDNA identified 10 exons within its protein-coding region. The Bassoon protein is predicted to contain two double-zinc fingers, several coiled-coil domains, and a stretch of polyglutamines (24 and 11 residues in rat and mouse, respectively). In some human proteins, e.g., Huntingtin, abnormal amplification of such poly-glutamine regions causes late-onset neurodegeneration. Bassoon is highly enriched in synaptic protein preparations. In cultured hippocampal neurons, Bassoon colocalizes with the synaptic vesicle protein synaptophysin and Piccolo, a presynaptic cytomatrix component. At the ultrastructural level, Bassoon is detected in axon terminals of hippocampal neurons where it is highly concentrated in the vicinity of the active zone. Immunogold labeling of synaptosomes revealed that Bassoon is associated with material interspersed between clear synaptic vesicles, and biochemical studies suggest a tight association with cytoskeletal structures. These data indicate that Bassoon is a strong candidate to be involved in cytomatrix organization at the site of neurotransmitter release.

scholarly journals Shank3 is localized in axons and presynaptic specializations of developing hippocampal neurons and involved in the modulation of NMDA receptor levels at axon terminals

2016 ◽  
Vol 137 (1) ◽  
pp. 26-32 ◽  
Author(s):  
Sonja Halbedl ◽  
Michael Schoen ◽  
Marisa S Feiler ◽  
Tobias M Boeckers ◽  
Michael J Schmeisser
Keyword(s):  
Nmda Receptor ◽  
Hippocampal Neurons ◽  
Axon Terminals

scholarly journals Production and characterization of a novel monoclonal antibody against neurotensin: immunohistochemical localization in the midbrain and hypothalamus.

1989 ◽  
Vol 37 (6) ◽  
pp. 831-841 ◽  
Author(s):  
F G Williams ◽  
A J Beitz
Keyword(s):  
Monoclonal Antibody ◽  
Immunohistochemical Localization ◽  
Competitive Elisa ◽  
Peptide Fragments ◽  
Peptide Bonds ◽  
Axon Terminals ◽  
Pre Treatment ◽  
Rough Endoplasmic Reticula ◽  
Immunohistochemical Studies

We developed a mouse monoclonal antibody against neurotensin (NT), termed NT8, for applications in immunohistochemistry and for ELISA analysis of NT. The antibody's paratope was determined by competitive ELISA using several peptide fragments of NT. That paratope requires intact peptide bonds between NT residues proline-7, arginine-8, and arginine-9. The antibody is of the IgG2B sub-isotype, having an IC50 for intact NT of approximately 3 nM when measured by competitive ELISA. Light microscopic immunohistochemical studies in the periaqueductal gray (PAG) and hypothalamus demonstrated staining patterns that agreed well with previous reports. Neuron perikarya were visualized even in the absence of colchicine pre-treatment, indicating that NT8 antibody is very sensitive in immunohistochemical applications. At the EM level, the antibody stained axon terminals, dendrites, and perikarya in the PAG. In lightly immunoreactive perikarya, rough endoplasmic reticula were visualized, suggesting that biosynthetic precursors to NT might be recognized by NT8.

Calotropis gigantea Promotes Neuritogenesis and Synaptogenesis through Activation of NGF-TrkA-Erk1/2 Signaling in Rat Hippocampal Neurons

2018 ◽  
Vol 46 (08) ◽  
pp. 1861-1877 ◽  
Author(s):  
Md Nazmul Haque ◽  
Md Mohibbullah ◽  
Yong-Ki Hong ◽  
Il Soo Moon
Keyword(s):  
Hippocampal Neurons ◽  
Neuronal Development ◽  
Early Stage ◽  
Specific Inhibitor ◽  
Therapeutic Effects ◽  
Active Components ◽  
Calotropis Gigantea ◽  
Traditional Medicines ◽  
Axon Terminals ◽  
Neuritogenic Activity

Calotropis gigantea (L.) R. Br (Apocynaceae) (commonly known as milkweed or crown flower) is a large shrub native to temperate regions of Asia, including China, Bangladesh and India and has a long history of use in traditional medicines. In this study, we investigated the neuromodulatory effects of the ethanol extracts of C. gigantea leaves (CGE) during synaptogenesis in the late stage of neuronal development and during early stage neuritogenesis in cultured rat hippocampal neurons. Maximum neuritogenic activity was achieved at a CGE concentration of 7.5[Formula: see text][Formula: see text]g/ml. At this concentration, CGE facilitated the early development of cytoarchitecture, as evidenced by increases in morphometric parameters, such as, the numbers, lengths, and number of branches of initial neurites, axon and dendrites. During the synaptogenic stage (DIV 14), immunocytochemistry (ICC) showed that CGE upregulated synaptic vesicle 2 (SV2, a marker of axon terminals) and postsynaptic density-95 (PSD-95, a postsynaptic marker) and their colocalization. CGE upregulated nerve growth factor (NGF) and activated extracellular signal-regulated kinase 1/2 (Erk1/2), which is blocked by a TrkA-specific inhibitor suggesting the neuritogenic and synaptogenic potential of CGE was due to the activation of NGF-TrkA-Erk1/2 signaling. Moreover, UPLC of CGE did not detect stigmasterol, an active component of C. gigantea. However, the chloroform-methanol and ethyl acetate subfractions of CGE exhibited initial neuritogenic activity, suggesting that multiple active components were responsible for the neurotrophic-mimetic properties of CGE. Our data prove the neuromodulatory ability of CGE and provide a means of identifying new active phytochemicals with potential nootropic, preventative or therapeutic effects on the human brain.

scholarly journals Immunohistochemical Localization of P-glycoprotein in Rat Brain and Detection of Its Increased Expression by Seizures Are Sensitive to Fixation and Staining Variables

2005 ◽  
Vol 53 (4) ◽  
pp. 517-531 ◽  
Author(s):  
Holger Volk ◽  
Heidrun Potschka ◽  
Wolfgang Löscher
Keyword(s):  
Rat Brain ◽  
Hippocampal Neurons ◽  
Efflux Pump ◽  
Polyclonal Antibodies ◽  
Cell Types ◽  
Immunohistochemical Localization ◽  
Multi Drug Resistance ◽  
Normal Brain ◽  
P Glycoprotein ◽  
Immunohistochemical Techniques

The MDR1 gene product, P-glycoprotein (P-gp), was shown to confer multi-drug resistance to cancer cells, but its overexpression is also suggested to be involved in pharmacoresistance of epilepsy by acting as an energy-dependent drug-efflux pump in the blood-brain barrier (BBB). In normal brain tissue, P-gp is almost exclusively expressed by capillary endothelial cells (EC) of the BBB, whereas little or no expression is detected in other cell types. Increased P-gp expression was observed after seizures, but localization of this increase, i.e., within brain capillary EC or within parenchymal or perivascular astrocytes, which contribute to the BBB function, is controversial. To test whether these antithetic data arise from unusual properties of the antigen itself, we compared different immunohistochemical techniques and monoclonal or polyclonal antibodies to P-gp in normal rat brain and rat brain after kainate-induced seizures. Using acetone-fixed cryostat sections of snap-frozen tissue, strong P-gp labeling was detected in EC and, after seizures, in hippocampal neurons, but not in astrocytes. In contrast, EC and neuronal P-gp immunolabeling were not seen in paraformaldehyde-fixed sections, whereas both perivascular and parenchymal astrocytes exhibited strong P-gp labeling after seizures. The lack of P-gp labeling in EC by paraformaldehyde fixation, was reversed by treatment of the sections with acetate/ethanol. These experiments demonstrate that various fixation conditions have a striking effect on the immunohistochemical localization of P-gp in rat brain and detection of its increased expression by seizures. When data obtained from different immunohistochemical techniques are taken together, seizures seem to induce overexpression of P-gp in four different cell types, i.e., EC, perivascular astrocytes, parenchymal astrocytes, and neurons.

Immunohistochemical localization of lysosomal cysteine protease cathepsins B and L in monkey hippocampal neurons after transient ischemia

1999 ◽  
Vol 19 (3) ◽  
pp. 302-310 ◽  
Author(s):  
Yukihiko Kohda ◽  
Katsuhiro Tsuchiya ◽  
Junkoh Yamashita ◽  
Masaki Yoshida ◽  
Takashi Ueno ◽  
...  
Keyword(s):  
Cysteine Protease ◽  
Hippocampal Neurons ◽  
Immunohistochemical Localization ◽  
Transient Ischemia ◽  
Lysosomal Cysteine Protease
Sign in / Sign up

Export Citation Format

Share Document